Bibliografías temáticas / Aromatic amino acid decarboxylase

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Literatura académica sobre el tema "Aromatic amino acid decarboxylase"

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Publicado: 11 de marzo de 2023

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Artículos de revistas sobre el tema "Aromatic amino acid decarboxylase"

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Komori, Hirofumi, Yoko Nitta, Hiroshi Ueno y Yoshiki Higuchi. "Structural basis for the histamine synthesis by human histidine decarboxylase". Acta Crystallographica Section A Foundations and Advances 70, a1 (5 de agosto de 2014): C458. http://dx.doi.org/10.1107/s2053273314095412.

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Histamine is a bioactive amine responsible for a variety of physiological reactions, including allergy, gastric acid secretion, and neurotransmission. In mammals, histamine production from histidine is catalyzed by histidine decarboxylase (HDC). Mammalian HDC is a pyridoxal 5'-phosphate (PLP)-dependent decarboxylase and belongs to the same family as mammalian glutamate decarboxylase (GAD) and mammalian aromatic L-amino acid decarboxylase (AroDC). The decarboxylases of this family function as homodimers and catalyze the formation of physiologically important amines like GABA and dopamine via decarboxylation of glutamate and DOPA, respectively. Despite high sequence homology, both AroDC and HDC react with different substrates. For example, AroDC catalyzes the decarboxylation of several aromatic L-amino acids, but has little activity on histidine. Although such differences are known, the substrate specificity of HDC has not been extensively studied because of the low levels of HDC in the body and the instability of recombinant HDC, even in a well-purified form. However, knowledge about the substrate specificity and decarboxylation mechanism of HDC is valuable from the viewpoint of drug development, as it could help lead to designing of novel drugs to prevent histamine biosynthesis. We have determined the crystal structure of human HDC in complex with inhibitors, histidine methyl ester (HME) and alpha-fluoromethyl histidine (FMH). These structures showed the detailed features of the PLP-inhibitor adduct (external aldimine) in the active site of HDC. These data provided insight into the molecular basis for substrate recognition among the PLP-dependent L-amino acid decarboxylases.
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Sköldberg, Filip, Fredrik Rorsman, Jaakko Perheentupa, Mona Landin-Olsson, Eystein S. Husebye, Jan Gustafsson y Olle Kämpe. "Analysis of Antibody Reactivity against Cysteine Sulfinic Acid Decarboxylase, A Pyridoxal Phosphate-Dependent Enzyme, in Endocrine Autoimmune Disease". Journal of Clinical Endocrinology & Metabolism 89, n.º 4 (1 de abril de 2004): 1636–40. http://dx.doi.org/10.1210/jc.2003-031161.

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Abstract The structurally related group II pyridoxal phosphate (PLP)-dependent amino acid decarboxylases glutamic acid decarboxylase (GAD), aromatic l-amino acid decarboxylase (AADC), and histidine decarboxylase (HDC) are known autoantigens in endocrine disorders. We report, for the first time, the prevalence of serum autoantibody reactivity against cysteine sulfinic acid decarboxylase (CSAD), an enzyme that shares 50% amino acid identity with the 65- and 67-kDa isoforms of GAD (GAD-65 and GAD-67), in endocrine autoimmune disease. Three of 83 patients (3.6%) with autoimmune polyendocrine syndrome type 1 (APS1) were anti-CSAD positive in a radioimmunoprecipitation assay. Anti-CSAD antibodies cross-reacted with GAD-65, and the anti-CSAD-positive sera were also reactive with AADC and HDC. The low frequency of anti-CSAD reactivity is in striking contrast to the prevalence of antibodies against GAD-65, AADC, and HDC in APS1 patients, suggesting that different mechanisms control the immunological tolerance toward CSAD and the other group II decarboxylases. Moreover, CSAD may be a useful mold for the construction of recombinant chimerical antigens in attempts to map conformational epitopes on other group II PLP-dependent amino acid decarboxylases.
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Pons, R., B. Ford, C. A. Chiriboga, P. T. Clayton, V. Hinton, K. Hyland, R. Sharma y D. C. De Vivo. "Aromatic l-amino acid decarboxylase deficiency". Neurology 62, n.º 7 (12 de abril de 2004): 1058–65. http://dx.doi.org/10.1212/wnl.62.7.1058.

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Lauweryns, J. M. y L. Van Ranst. "Immunocytochemical localization of aromatic L-amino acid decarboxylase in human, rat, and mouse bronchopulmonary and gastrointestinal endocrine cells." Journal of Histochemistry & Cytochemistry 36, n.º 9 (septiembre de 1988): 1181–86. http://dx.doi.org/10.1177/36.9.2900264.

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Aromatic L-amino acid decarboxylase (AADC) catalyzes the cellular decarboxylation of L-aromatic amino acids and is therefore involved in the synthesis of several biogenic amines. Application of the indirect immunoperoxidase method on human, rat, and mouse tissues using specific antibodies to AADC revealed all AADC-containing cells. Besides mast cells and adrenergic nerve fibers, the following cells were immunostained: neuroendocrine cells in the tracheobronchial epithelium; neuroepithelial bodies in the bronchopulmonary epithelium; Kultschitzky cells in the small intestine and appendix as well as adrenal chromaffin cells. All the latter cells belong to the so-called APUD system, the "D" in the acronym standing for the activity of the enzyme aromatic L-amino acid decarboxylase. Immunocytochemistry for AADC may become an additional tool not only to highlight APUD cells in tissue sections but also to differentiate the sites of cellular amine synthesis from those of amine storage.
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Hyland, K. y P. T. Clayton. "Aromatic L-Amino Acid Decarboxylase Deficiency: Diagnostic Methodology". Clinical Chemistry 38, n.º 12 (1 de diciembre de 1992): 2405–10. http://dx.doi.org/10.1093/clinchem/38.12.2405.

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Abstract Aromatic L-amino acid decarboxylase (EC. 4.1.1.28) deficiency is a newly described inborn error of metabolism that affects serotonin and dopamine biosynthesis. The major biochemical markers for this disease are increases of L-dopa, 3-methoxytyrosine, and 5-hydroxytryptophan in urine, plasma, and cerebrospinal fluid together with decreased cerebrospinal fluid concentrations of homovanillic acid and 5-hydroxyindoleacetic acid. In addition, concentrations of vanillactic acid are increased in the urine. Specific HPLC and gas chromatography-mass spectrometry methods are described that permit the identification and measurement of these metabolites in the above body fluids. Simplified assays for human plasma L-dopa decarboxylase and liver L-dopa and 5-hydroxytryptophan decarboxylase, used to demonstrate the enzyme deficiency, are also reported.
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Hyland, K. y P. T. Clayton. "Aromatic amino acid decarboxylase deficiency in twins". Journal of Inherited Metabolic Disease 13, n.º 3 (mayo de 1990): 301–4. http://dx.doi.org/10.1007/bf01799380.

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Kang, Un Jung y Tong H. Joh. "Deduced amino acid sequence of bovine aromatic l-amino acid decarboxylase: homology to other decarboxylases". Molecular Brain Research 8, n.º 1 (junio de 1990): 83–87. http://dx.doi.org/10.1016/0169-328x(90)90013-4.

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Pal Chowdhury, Piyali, Soumik Basu, Arindam Dutta y Tapan K. Dutta. "Functional Characterization of a Novel Member of the Amidohydrolase 2 Protein Family, 2-Hydroxy-1-Naphthoic Acid Nonoxidative Decarboxylase from Burkholderia sp. Strain BC1". Journal of Bacteriology 198, n.º 12 (11 de abril de 2016): 1755–63. http://dx.doi.org/10.1128/jb.00250-16.

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ABSTRACTThe gene encoding a nonoxidative decarboxylase capable of catalyzing the transformation of 2-hydroxy-1-naphthoic acid (2H1NA) to 2-naphthol was identified, recombinantly expressed, and purified to homogeneity. The putative gene sequence of the decarboxylase (hndA) encodes a 316-amino-acid protein (HndA) with a predicted molecular mass of 34 kDa. HndA exhibited high identity with uncharacterized amidohydrolase 2 proteins of variousBurkholderiaspecies, whereas it showed a modest 27% identity with γ-resorcylate decarboxylase, a well-characterized nonoxidative decarboxylase belonging to the amidohydrolase superfamily. Biochemically characterized HndA demonstrated strict substrate specificity toward 2H1NA, whereas inhibition studies with HndA indicated the presence of zinc as the transition metal center, as confirmed by atomic absorption spectroscopy. A three-dimensional structural model of HndA, followed by docking analysis, identified the conserved metal-coordinating and substrate-binding residues, while their importance in catalysis was validated by site-directed mutagenesis.IMPORTANCEMicrobial nonoxidative decarboxylases play a crucial role in the metabolism of a large array of carboxy aromatic chemicals released into the environment from a variety of natural and anthropogenic sources. Among these, hydroxynaphthoic acids are usually encountered as pathway intermediates in the bacterial degradation of polycyclic aromatic hydrocarbons. The present study reveals biochemical and molecular characterization of a 2-hydroxy-1-naphthoic acid nonoxidative decarboxylase involved in an alternative metabolic pathway which can be classified as a member of the small repertoire of nonoxidative decarboxylases belonging to the amidohydrolase 2 family of proteins. The strict substrate specificity and sequence uniqueness make it a novel member of the metallo-dependent hydrolase superfamily.
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Jung, M. J. "Substrates and inhibitors of aromatic amino acid decarboxylase". Bioorganic Chemistry 14, n.º 4 (diciembre de 1986): 429–43. http://dx.doi.org/10.1016/0045-2068(86)90007-6.

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Lee, Hsiu-Fen, Chi-Ren Tsai, Ching-Shiang Chi, Tung-Ming Chang y Huei-Jane Lee. "Aromatic l-amino acid decarboxylase deficiency in Taiwan". European Journal of Paediatric Neurology 13, n.º 2 (marzo de 2009): 135–40. http://dx.doi.org/10.1016/j.ejpn.2008.03.008.

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Tesis sobre el tema "Aromatic amino acid decarboxylase"

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Spence, Michael Patrick. "Plant aromatic amino acid decarboxylases: Evolutionary divergence, physiological function, structure function relationships and biochemical properties". Diss., Virginia Tech, 2014. http://hdl.handle.net/10919/49432.

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Plant aromatic amino acid decarboxylases (AAADs) are a group of economically important enzymes categorically joined through their pyridoxal 5'-phosphate (PLP) dependence and sequence homology. Extensive evolutionary divergence of this enzyme family has resulted in a selection of enzymes with stringent aromatic amino acid substrate specificities. Variations in substrate specificities enable individual enzymes to catalyze key reactions in a diverse set of pathways impacting the synthesis of monoterpenoid indole alkaloids (including the pharmacologically active vinblastine and quinine), benzylisoquinoline alkaloids (including the pharmacologically active papaverine, codeine, morphine, and sanguinarine), and antioxidant and chemotherapeutic amides. Recent studies of plant AAAD proteins demonstrated that in addition to the typical decarboxylation enzymes, some annotated plant AAAD proteins are actually aromatic acetaldehyde synthases (AASs). These AASs catalyze a decarboxylation-oxidative deamination process of aromatic amino acids, leading to the production of aromatic acetaldehydes rather than the AAAD derived arylalkylamines. Research has implicated that plant AAS enzymes are involved in the production of volatile flower scents, floral attractants, and defensive phenolic acetaldehyde secondary metabolites. Historically, the structural elements responsible for differentiating plant AAAD substrate specificity and activity have been difficult to identify due to strong AAAD and AAS inter-enzyme homology. Through extensive bioinformatic analysis and experimental verification of plant AAADs, we have determined some structural elements unique to given types of AAADs. This document highlights structural components apparently responsible for the differentiation of activity and substrate specificity. In addition to producing primary sequence identifiers capable of AAAD activity and substrate specificity differentiation, this work has also demonstrated applications of AAAD enzyme engineering and novel activity identification.
Ph. D.
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2

Allen, G. F. G. "The neurochemical consequences of aromatic L-amino acid decarboxylase deficiency". Thesis, University College London (University of London), 2011. http://discovery.ucl.ac.uk/1310134/.

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Aromatic L-amino acid decarboxylase (AADC) catalyses the conversion of 5-hydroxytryptophan (5-HTP) and L-3,4-dihydroxyphenylalanine (L-dopa) to the neurotransmitters serotonin and dopamine respectively. The inherited disorder AADC deficiency leads to a severe deficit of serotonin and dopamine as well as an accumulation of 5-HTP and L-dopa. This thesis investigated the potential role of 5-HTP/L-dopa accumulation in the pathogenesis of AADC deficiency. Treatment of human neuroblastoma cells with L-dopa or dopamine was found to increase intracellular levels of the antioxidant reduced glutathione (GSH). However inhibiting AADC prevented the GSH increase induced by L-dopa. Furthermore dopamine but not L-dopa, increased GSH release from human astrocytoma cells, which do not express AADC activity. GSH release is the first stage of GSH trafficking from astrocytes to neurons. This data indicates dopamine may play a role in controlling brain GSH levels and consequently antioxidant status. The inability of L-dopa to influence GSH concentrations in the absence of AADC or with AADC inhibited indicates GSH trafficking/metabolism may be compromised in AADC deficiency. 5-HTP was demonstrated to potentially be mildly toxic to human neuroblastoma cells but not astrocytoma cells; however the concentrations required for this response are likely to be higher than pathophysiological levels in AADC deficiency. These results indicate the need for investigations addressing the effects of chronic 5-HTP exposure as only acute effects were investigated in the current study. This thesis also investigated the effect of altered availability of the AADC coenzyme pyridoxal 5‟-phosphate (PLP) on AADC activity, protein and expression. In two patients with inherited disorders of PLP metabolism reductions in plasma AADC activity were observed. Furthermore PLP-deficient human neuroblastoma cells were found to exhibit reduced levels of AADC activity and protein but not altered expression. These findings suggest maintaining adequate PLP availability may be important for optimal treatment of AADC deficiency.
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Fisher, Andrew. "Pharmacological manipulation of aromatic L-amino acid decarboxylase in the rat". Thesis, University College London (University of London), 1999. http://ethos.bl.uk/OrderDetails.do?uin=uk.bl.ethos.325114.

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Cho, Seongeun. "Modulation of tyrosine hydroxylase and aromatic L-amino acid decarboxylase by dopaminergic drugs in mouse brain /". The Ohio State University, 1995. http://rave.ohiolink.edu/etdc/view?acc_num=osu148786592945682.

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Liang, Jing. "Biochemical Studies of Aromatic Amino Acid Decarboxylases and Acetaldehyde Synthases". Diss., Virginia Tech, 2018. http://hdl.handle.net/10919/96242.

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Pyridoxal 5'-phosphate (PLP)-dependent enzymes widely exist in most living organisms from bacteria to human. Among different types of PLP-dependent enzymes, aromatic amino acid decarboxylases play critical physiological roles because many aromatic amines are essential neurotransmitters. This dissertation concerns the biochemical characterization of several PLP-dependent decarboxylases and aims to understand the structure-function relationships, especially critical residues involved in their catalysis. We first present an overview of the current opinions and recent advances in structure-function relationships of several PLP-dependent enzymes with the first reaction step at substrate Cα position, including decarboxylase and acetaldehyde synthase. L-3, 4-dihydroxyphenylalanine (L-dopa) decarboxylase (DDC) is a model enzyme we use as a reference because the structures and functions of DDC are relatively well established. We previously identified two annotated DDC-like proteins from Drosophila indeed catalyzing a decarboxylation-oxidative deamination reaction of L-dopa to form 3,4-dihydroxyphenylacetaldehyde (DHPA), CO2, NH3, and H2O2 and we named these proteins as DHPA synthases due to the physiological importance of DHPA for cuticle protein crosslinking. Our results provide an efficient way to identify more DHPA synthase enzymes from DDC based on sequence identity and the signature residues we identified (Asn192 in DHPA synthase versus His192 in DDC), and we also propose a reasonable explanation of the mechanism. The results that H2O2 produced by the reaction can be reused in the reaction as an oxidizing agent suggest a way to avoid the oxidative stress of H2O2. We then compared tyrosine decarboxylase (TyDC) with DDC. As the enzyme catalyzing the first step of insect neurotransmitter tyramine/octopamine synthesis, the biochemical characteristics of insect TyDC have not been thoroughly elucidated yet because of the expression difficulty. We expressed one insect TyDC and analyzed its biochemical properties. Our enzyme analyses reveal that insect TyDC prefers tyrosine as a substrate, but it also displays some activity to L-dopa. Spectral analysis also shows that the absorbance spectra of insect TyDC have major differences as compared to those of DDC. Site-directed mutagenesis indicates that the interactions between residue Asn304 with PLP is primarily responsible for its spectra differences of TyDC as compared to those of DDC and also is involved in higher substrate affinity to L-tyrosine. Another active site residue (Ser353) has the main effect on substrate selectivity. Our results show the biochemical properties of TyDC for the first time and also provide some insights into the mechanism of its substrate selectivity.
PHD
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Phillips, Susan R. "Spectroscopic investigation of tryptophan microenvironments in bovine lens proteins". Diss., Georgia Institute of Technology, 1986. http://hdl.handle.net/1853/32973.

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Silvia, Christopher Paul. "The isolation, partial peptide sequence, and cDNA sequence of aromatic L-amino acid decarboxylase from bovine adrenal medulla /". The Ohio State University, 1990. http://rave.ohiolink.edu/etdc/view?acc_num=osu1487677267729241.

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Young, Elizabeth A. "Second Messenger System Modulation of Aromatic L-Amino Acid Decarboxylase and Tyrosine Hydroxylase in Normal and MPTP Lesioned Mice /". The Ohio State University, 1995. http://rave.ohiolink.edu/etdc/view?acc_num=osu1487929230741091.

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Höfig, Carolin. "Establishment, validation and application of immunological and LC-MS/MS-based detection methods to study the role of human aromatic L-amino acid decarboxylase as an enzyme potentially involved in thyronamine biosynthesis". Doctoral thesis, Humboldt-Universität zu Berlin, Mathematisch-Naturwissenschaftliche Fakultät I, 2012. http://dx.doi.org/10.18452/16645.

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Thyronamine (TAM) sind eine neue Molekülklasse, die endokrinologische und metabolische Prozesse miteinander vereinen. Der biologisch aktive Metabolit 3-Iod-L-Thyronamin (3-T1AM) wird durch eine kombinierte Deiodierung und Decarboxylierung von Schilddrüsenhormonen (TH) gebildet. Existierende Methoden zum Nachweis und zur Quantifizierung von 3-T1AM im menschlichen Serum sind immer noch umstritten. Auch die an der Biosynthese vermutlich beteiligte TH-Decarboxylase konnte noch nicht identifiziert werden. Für die Identifizierung und Quantifizierung von TH und TAM Profilen wurde die Flüssigchromatographie-Tandem-Massenspektrometrie (LC-MS/MS) verwendet. In der bisherigen präanalytischen Aufarbeitung liefern weder Flüssig-Flüssig- noch Festphasenextraktionen reproduzierbare Ergebnisse des 3-T1AM-Gehalts im Serum. Mit der Entwicklung eines spezifischen Extraktionsverfahrens und nachfolgender Detektion mittels LC-MS/MS gelang der gleichzeitige Nachweis der häufigsten TH im humanen Serum. Parallel dazu wurden monoklonale Antikörper gegen 3-T1AM entwickelt, auf deren Basis ein quantitativer 3-T1AM Chemilumineszenz-Immunoassay entstand. Ergebnisse aus klinischen Kollektiven zeigen, dass 3-T1AM im Serum im nM Konzentrationsbereich vorkommt und dass 3-T1AM bei Patienten außerhalb der Schilddrüse produziert wird. Viele Forscher gehen davon aus, dass die aromatische L-Aminosäure Decarboxylase (AADC) die Synthese von TAM über Decarboxylierung von TH katalysiert. Diese Hypothese wurde durch Inkubation von rekombinanter humaner AADC mit TH getestet. In keinem der Experimente konnte AADC die Decarboxylierung von TH katalysieren. Zusammenfassend ist die Bestimmung von 3-T1AM im Serum mittels LC-MS/MS aufgrund der nicht reproduzierbaren präanalytischen Probenaufbereitung problematisch. In dieser Arbeit wird der erste MAb-basierte 3-T1AM assay vorgestellt, der 3-T1AM zuverlässig in humanem Serum quantifiziert. Die AADC ist wahrscheinlich nicht an der Biosynthese von TAM beteiligt.
Thyronamines (TAM) are a new class of molecules linking endocrinology and metabolism. Combined deiodination and decarboxylation of thyroid hormones (TH) generates a biologically active ‘cooling’ metabolite, 3-iodo-L-thyronamine (3-T1AM).. It remains controversial, which methods are able or not to reliably detect 3-T1AM in human serum, and the presumed TH decarboxylase is still elusive. Liquid chromatography-tandem mass spectrometry (LC-MS/MS) was used for the simultane-ous identification and quantification of TH and TAM profiles in biological samples. Several preanalytical methods were tested for complete extraction of 3-T1AM in human serum. Thus far, neither liquid-liquid nor solid-phase extraction methods allowed reproducible extraction of 3-T1AM from human serum samples in the preanalytical sample workup. Nevertheless, a rapid and sensitive extraction procedure was developed for detection of the major TH by LC-MS/MS in a single human serum sample. In parallel, monoclonal antibodies (MAb) targeting 3-T1AM were developed and characterized, and a highly specific quantitative 3-T1AM MAb-based chemiluminescence immunoassay was developed. Studies in clinical cohorts provide evidence that 3-T1AM is present in human serum in the nM concentration range and that 3-T1AM is produced extrathyroidally. Many researchers have reasoned that the aromatic L-amino acid decarboxylase (AADC) mediates TAM synthesis via decarboxylation of TH. This hypothesis was tested by incubating recombinant human AADC with several TH. In all tested conditions, AADC failed to catalyze the decarboxylation of TH. These in vitro observations are supported by the finding that 3-T1AM is also present in plasma samples of patients with AADC deficiency. In summary, 3-T1AM detection in serum using LC-MS/MS encounters preanalytical problems. The first MAb-based 3-T1AM CLIA is presented, which reliably quantifies 3-T1AM in human serum. AADC is likely not involved in TAM biosynthesis.
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Höfig, Carolin [Verfasser], Werner [Akademischer Betreuer] Kloas, Josef [Akademischer Betreuer] Köhrle y Dagmar [Akademischer Betreuer] Führer-Sakel. "Establishment, validation and application of immunological and LC-MS/MS-based detection methods to study the role of human aromatic L-amino acid decarboxylase as an enzyme potentially involved in thyronamine biosynthesis / Carolin Höfig. Gutachter: Werner Kloas ; Josef Köhrle ; Dagmar Führer-Sakel". Berlin : Humboldt Universität zu Berlin, Mathematisch-Naturwissenschaftliche Fakultät I, 2012. http://d-nb.info/1029763844/34.

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Libros sobre el tema "Aromatic amino acid decarboxylase"

1

Goddijn, Oscar Johannes Maria. Regulation of terpenoid indole alkaloid biosynthesis in Catharanthus roseus: The tryptophan decarboxylase gene. Alblasserdam: Offsetdrukkerij Haveka BV, 1992.

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1949-, Sayler Gary S. y Blackburn James W. 1950-, eds. Microbiological decomposition of chlorinated aromatic compounds. New York: M. Dekker, 1987.

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Lednicer, Daniel. The organic chemistry of drug synthesis. Chichester: Wiley, 1990.

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Lednicer, Daniel. The organic chemistry of drug synthesis. New York: Wiley, 1995.

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Baek, Jae-Kyeong. Behavioral studies of dopa-decarboxylase mutant Drosophila lacking serotonin and dopamine in central nervous system. 1987.

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Pearl, Phillip L. y William P. Welch. Pediatric Neurotransmitter Disorders. Oxford University Press, 2017. http://dx.doi.org/10.1093/med/9780199937837.003.0059.

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The pediatric neurotransmitter disorders represent an enlarging group of neurological syndromes characterized by inherited abnormalities of neurotransmitter synthesis, metabolism, and transport. Disorders involving monoamine synthesis include guanosine triphosphate cyclohydrolase deficiency (Segawa disease or classical Dopa-responsive dystonia as the heterozygous form), aromatic amino acid decarboxylase deficiency, tyrosine hydrolase deficiency, sepiapterin reductase deficiency, and disorders of tetrahydrobiopterin synthesis. These disorders can be classified according to whether they feature elevated serum levels of phenylalanine. Disorders of γ-amino butyric acid (GABA) metabolism include succinic semialdehyde dehydrogenase deficiency and GABA-transaminase deficiency. Glycine encephalopathy is typically manifested by refractory neonatal seizures due to a defect in the glycine degradative pathway. Pyridoxine-responsive seizures have now been associated with deficiency of α-aminoadipic semialdehyde dehydrogenase as well as a variants requiring therapy with pyridoxal-5-phosphate and folinic acid.
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Heales, Simon, Simon Pope, Viruna Neergheen y Manju Kurian. Abnormalities of CSF Neurotransmitters/Folates. Oxford University Press, 2016. http://dx.doi.org/10.1093/med/9780199972135.003.0082.

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The term Neurotansmitter disorder, in the area of metabolic disease, focuses particularly on inborn errors affecting monoamine (dopamine & serotonin), pyridoxal phosphate (B6) and folate metabolism. Whilst there has been considerable focus on these disorders with regards to the paediatric population, it is clear that an increasing number of adult patients are being identified. Adult neurologists need to be aware of the clinical presentation of such patients and the appropriate tests that need to be requested to ensure a correct diagnosis is achieved. CSF profiling, by a specialist laboratory, is often required. This has the ability to very often identify the nature of a primary defect with regards to implementation of appropriate treatment. For some of these disorders, treatment can be effective. This may be in the form of monoamine/vitamin replacement. However there are exceptions, e.g. aromatic amino acid decarboxylase and dopamine transporter deficiencies. There also needs also to be an awareness of the growing list of secondary factors that can cause impaired dopamine and serotonin metabolism.
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Hsu, Jean Wei-Chen. Aromatic amino acid requirements and metabolism. 2006.

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Berry, Alan. The physiology and regulation of aromatic amino acid biosynthesis in Pseudomonas aeruginosa. 1985.

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D'Amato, Thomas Andrew. Gene-enzyme relationships in Nicotina silvestris: Subcellular localization of genes and enzymes for aromatic amino acid biosynthesis. 1986.

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Capítulos de libros sobre el tema "Aromatic amino acid decarboxylase"

1

Schomburg, Dietmar y Margit Salzmann. "Aromatic-L-amino-acid decarboxylase". En Enzyme Handbook 1, 103–7. Berlin, Heidelberg: Springer Berlin Heidelberg, 1990. http://dx.doi.org/10.1007/978-3-642-86605-0_24.

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Scharnagl, Hubert, Winfried März, Markus Böhm, Thomas A. Luger, Federico Fracassi, Alessia Diana, Thomas Frieling et al. "Aromatic L-Amino Acid Decarboxylase Deficiency". En Encyclopedia of Molecular Mechanisms of Disease, 137. Berlin, Heidelberg: Springer Berlin Heidelberg, 2009. http://dx.doi.org/10.1007/978-3-540-29676-8_7447.

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Lindström, Per. "A stimulatory effect of substrates for aromatic L-amino acid decarboxylase on insulin secretion in mice". En Amino Acids, 781–88. Dordrecht: Springer Netherlands, 1990. http://dx.doi.org/10.1007/978-94-011-2262-7_94.

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Hwu, Wuh-Liang, Yin-Hsiu Chien, Ni-Chung Lee y Mei-Hsin Li. "Natural History of Aromatic l-Amino Acid Decarboxylase Deficiency in Taiwan". En JIMD Reports, 1–6. Berlin, Heidelberg: Springer Berlin Heidelberg, 2017. http://dx.doi.org/10.1007/8904_2017_54.

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Ebadi, M. y V. Simonneaux. "Ambivalence on the Multiplicity of Mammalian Aromatic L-Amino Acid Decarboxylase". En Advances in Experimental Medicine and Biology, 115–25. Boston, MA: Springer New York, 1991. http://dx.doi.org/10.1007/978-1-4684-5952-4_10.

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Schomburg, Dietmar y Dörte Stephan. "Aromatic-amino-acid transaminase". En Enzyme Handbook 13, 463–66. Berlin, Heidelberg: Springer Berlin Heidelberg, 1997. http://dx.doi.org/10.1007/978-3-642-59176-1_92.

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Fitzpatrick, Paul F. "The Aromatic Amino Acid Hydroxylases". En Advances in Enzymology - and Related Areas of Molecular Biology, 235–94. Hoboken, NJ, USA: John Wiley & Sons, Inc., 2006. http://dx.doi.org/10.1002/9780470123201.ch6.

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Schomburg, Dietmar y Dörte Stephan. "Aromatic-amino-acid-glyoxylate transaminase". En Enzyme Handbook 13, 479–82. Berlin, Heidelberg: Springer Berlin Heidelberg, 1997. http://dx.doi.org/10.1007/978-3-642-59176-1_95.

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Maitre, L., P. R. Hedwall y P. C. Waldmeier. "α-Methyldopa, An Unnatural Aromatic Amino Acid". En Novartis Foundation Symposia, 335–42. Chichester, UK: John Wiley & Sons, Ltd., 2008. http://dx.doi.org/10.1002/9780470720059.ch19.

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Geiger, Donald R. y Mark A. Fuchs. "Inhibitors of Aromatic Amino Acid Biosynthesis (Glyphosate)". En Herbicide Classes in Development, 59–85. Berlin, Heidelberg: Springer Berlin Heidelberg, 2002. http://dx.doi.org/10.1007/978-3-642-59416-8_3.

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Actas de conferencias sobre el tema "Aromatic amino acid decarboxylase"

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Liang Hwu, Paul Wuh, Yin Hsiu Chien, Ni Chung Lee, Sheng Hong Tseng, Chun Hwei Ta, Anne Marie Conway, Luciana Giugliani, Pedro Pachelli, Andressa Federhen y Mark Pykett. "Safety and Improved Efficacy Outcomes in Children With AADC Deficiency Treated With Eladocagene Exuparvovec Gene Therapy: Results From Three Clinical Trials". En XIII Congresso Paulista de Neurologia. Zeppelini Editorial e Comunicação, 2021. http://dx.doi.org/10.5327/1516-3180.049.

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Introduction: aromatic L-amino acid decarboxylase (AADC) deficiency, a rare genetic disorder of neurotransmitter synthesis, is characterized by motor developmental deficits and clinical features associated with the autonomic nervous system, including dyskinesia, and oculogyric crisis. Objective: To evaluate clinical outcomes in children with AADC deficiency treated with eladocagene exuparvovec, a recombinant adeno-associated virus vector containing the human cDNA encoding the AADC enzyme. Methods: In 3 open-label clinical studies, children with AADC deficiency who had no full head control and no ability to sit, stand, or walk received eladocagene exuparvovec as bilateral, intraputaminal, stereotactic infusions during a single operative session (total dose, 1.8 x 1011vg). Body weight, oculogyric crisis episodes, and adverse events (AE) were recorded. Results: In the 3 studies, patients aged 21 months to 8.5 years (N=26) received eladocagene exuparvovec, constituting the safety population. In the intent-to- treat population (N=21), mean body weight at baseline was 12.0 kg (median 10.5 kg) and increased to 15.2 kg (median 13.2 kg) at 12 months posttreatment. Frequency of oculogyric crises was improved at 12 months posttreatment. Dyskinesia was recorded as an AE in 23 patients in the safety population; most events were mild or moderate, occurred within 3 months after eladocagene exuparvovec treatment, generally responded to standard pharmacotherapy, and resolved in all patients by 10 months. Conclusions: In children with AADC deficiency who received eladocagene exuparvovec gene therapy, body weight increased and oculogyric crises and dyskinesia improved.
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Ludwig, M. y S. A. Asher. "UV Resonance Raman Studies of Aromatic Amino Acids and Proteins". En Laser Applications to Chemical Analysis. Washington, D.C.: Optica Publishing Group, 1987. http://dx.doi.org/10.1364/laca.1987.pdp3.

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The ultraviolet resonance Raman (UVRR) excitation profiles have been measured for the aromatic amino acids phenylalanine, tryptophan, tyrosine and tyrosinate. Resonance excitation enhances Raman scattering from vibrational modes that distort the ground state configuration towards the configuration of the excited state. The excitation profile maxima are red-shifted with respect to the absorption spectral maxima for each aromatic amino acid. These excitation profiles indicate the excitation required to maximally enhance a particular aromatic amino acid residue in a protein. Individual aromatic amino acids in environmentally distinguishable positions in a protein may have slightly different transition energies, and could therefore be identified and distinguished by proper tuning of the excitation frequency. For example, surface tyrosyl residues in hydrophilic environments will have lower lying excited states due to extensive hydrogen bonding. These residues will be maximally enhanced with longer wavelength excitation than residues buried in hydrophobic pockets within a protein. The frequency of certain vibrational bands, particularly those known to be influenced by substituents on the aromatic ring may also be indicative of the local environment. The relative intensities of other enhanced bands may also contain information concerning specific local environment. For example, the relative intensity of the peaks of the 830/850 cm-1 Fermi resonance doublet of tyrosine are known from normal Raman studies to be sensitive to hydgrogen bonding. Vibrational substructure is not observed in absorption spectral measurements due to the breadth of the absorption spectral features. The vibrational substructure is amplified in the resonance Raman excitation profiles.
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Angiolillo, Paul J. y Jane M. Vanderkooi. "Products of Excited State Molecules: Evidence for Hydrogen Atom Generation Within a Protein". En Biomedical Optical Spectroscopy and Diagnostics. Washington, D.C.: Optica Publishing Group, 2006. http://dx.doi.org/10.1364/bosd.1996.dr6.

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The UV photolysis of the aromatic amino acid, tryptophan (Trp), in the Ca2+ binding protein, cod parvalbumin, Type III, was studied using electron paramagnetic resonance (EPR) spectroscopy in the temperature range 4-80 K. For the Ca2+-bound protein, irradiation with UV light (250-400 nm) resulted in the generation of atomic hydrogen with a hyperfine splitting of 50.8 mT, whereas in the Ca2+-free form, where the Trp is exposed to solvent, the trapped atomic hydrogen was not in evidence. This is the first report of H atom generation in a protein, and it is suggested that the highly reactive free radical species may be involved in the many reactions that Trp is known to undergo.
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Yu, Wan-Lin, Yu Li y Bao-Hui Li. "Polycyclic aromatic hydrocarbons analysis in river by Cu(II)-2-amino terephthalic acid metal organic framework as novel sorbent for solid-phase extraction combined with HPLC". En Proceedings of the 2018 7th International Conference on Sustainable Energy and Environment Engineering (ICSEEE 2018). Paris, France: Atlantis Press, 2019. http://dx.doi.org/10.2991/icseee-18.2019.7.

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Fang, Baochen y Jiajia Rao. "Functional, nutritional properties and aroma profile of hemp protein isolate by reverse micelles extraction technique: impact of defatting processing". En 2022 AOCS Annual Meeting & Expo. American Oil Chemists' Society (AOCS), 2022. http://dx.doi.org/10.21748/wzgi5968.

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There is an increased awareness of the incorporation of hemp protein in a commercial product on account of its high nutritional value and neutral flavor. One of the factors that impact the functional properties of hemp protein is the isolation conditions. In recent years, reverse micelles (RMs) has emerged as a powerful technique for extracting protein and enzyme because of low cost, convenience, and potential for scaling up in the manufacturing process. For oil crops, it generally requires long defatting processing before protein extraction. Therefore, it would be interesting to investigate whether the defatting of hempseed flour would impact on physicochemical properties of hemp protein using the RM extraction method. Our results revealed that high protein recovery yield (69.37-70.21%) and protein purity (92.76-95.2%) of hemp protein isolate (HPI) could be obtained through the RM technique using either non-defatted hemp flour (ND-HF) or defatted hemp flour (D-HF). Concerning the defatting processing, both HPIs showed great similarity in protein composition, and functional properties including solubility, thermal stability, foaming, and emulsifying properties. Interestingly, HPI obtained from ND-HF had higher essential amino acid ratio when compared to D-HF. Beyond that, distinct gelling behaviors (least gelling concentration, gel strength, and color) have been observed. The HPI gel obtained from ND-HF displayed a higher least gelling concentration (4%) with yellowish color than that of HPI gel from D-HF (2%). In terms of aroma profile, a significantly high number of aromatic compounds with a greater abundancy were detected in HPI from ND-HF (33) as compared to HPI isolated from D-HF (26), which contributed to the different process conditions and lipid content. The research findings provided an eco-friendly protein isolation method with premium functional attributes, especially for oil crops, which pave the way for the future application of RMs in a wide range of protein extraction.
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Suttie, W. J., A. Cheung y M. G. Wood. "ENZYMOLOGY OF THE VITAMIN K-DEPENDENT CARBOXYLASE: CURRENT STATUS". En XIth International Congress on Thrombosis and Haemostasis. Schattauer GmbH, 1987. http://dx.doi.org/10.1055/s-0038-1643991.

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The vitamin K-dependent microsomal carboxylase converts glutamyl residues in precursor proteins to γ-carboxyglutamyl (Gla) residues in completed proteins. The enzyme activity is present in significant activities in most non-skeletal tissues but has been studied most extensively in rat and bovine liver. Early studies of the enzyme utilized bound precursors of vitamin K-dependent clotting factors as substrates for the enzyme and demonstrated that the enzyme requires the reduced form of vitamin K (vitamin KH2), O2, and CO2. Subsequent investigations have taken advantage of the observation that the enzyme will carboxylate low-molecular-weight peptide substrates with Glu-Glu sequences. Utilizing a substrate such as Phe-Leu-Glu-Glu-Leu, it has been possible to demonstrate that γ-C-H release from the Glu residue of a substrate is independent of CO2 concentration. The formation of vitamin K 2,3-epoxide can also be demonstrated in a crude microsomal system, and it can be shown that the formation of this metabolite can be stimulated by the presence of a peptide substrate of the carboxylase. These observations have led to the general hypothesis that the mechanism of action of the enzyme involves interaction of vitamin KH2 with O2 to form an oxygenated intermediate that can interact with a substrate Glu residue to abstract a γ-hydrogen and in the process he converted to vitamin K epoxide (KO). The current evidence suggests that, either directly or indirectly, removal of the γ-C-H results in the formation of a carbanion at the γ-position of the Glu residue which can interact with CO2 to form Gla. The Glu residue intermediate which is formed can be demonstrated to partition between accepting a proton in the media to reform Glu, or interacting with CO2 to form Gla. Current data do not distinguish between the direct formation of a carbanion coupled to proton removal, or the participation of a reduced intermediate. Recent studies have demonstrated that the enzyme will carry out a partial reaction, the formation of vitamin K epoxide, at a decreased rate in the absence of a Glu site substrate. Epoxide formation under these conditions has the same for O2 as the carboxylation reaction and is inhibited in the same manner as the carboxylation reaction. In the presence of saturating concentrations of a Glu site substrate and C02, the ratio of KO formed, γ-C-H released, and C02 formed is 1:1:1. However, KO formation can be uncoupled from and proceeds at a higher rate than γ-C-H bond cleavage and Gla formation at low Glu site substrate concentrations. At saturating concentrations of CO2, Gla formation is equivalent to γ-C-H bond cleavage, and this unity is not altered by variations in vitamin KH2 or peptide substrate concentrations. Natural compounds with vitamin K activity are 2-Me-l,4-naphthoquinones with a polyprenyl side chain at the 3-position. Studies of vitamin K analogs have demonstrated that a 2-Me group is essential for activity but that the group at the 3-position can vary significantly. Modification of the aromatic ring of the naphthoquinone nucleus by methyl group substitution can result in alterations of either the rate of the carboxylation reaction or the apparent affinity of the enzyme for the vitamin. Studies of a large number of peptide substrates have failed to reveal any unique primary amino acid sequence which is a signal for carboxylation. However, current evidence from a number of sources suggests that a basic amino acid rich "propeptide" region of the intracellular form of the vitamin K-dependent proteins is an essential recognition site for the enzyme. This region of the precursor is lost in subsequent processing, and the manner in which it directs this posttranslational event is not yet clarified. Supported by NIH grant AM-14881.
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Informes sobre el tema "Aromatic amino acid decarboxylase"

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Author, Not Given. Gene-Enzyme Relationships of Aromatic Amino Acid Biosynthesis in Higher Plants. Office of Scientific and Technical Information (OSTI), agosto de 2002. http://dx.doi.org/10.2172/834384.

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Locy, Robert D., Hillel Fromm, Joe H. Cherry y Narendra K. Singh. Regulation of Arabidopsis Glutamate Decarboxylase in Response to Heat Stress: Modulation of Enzyme Activity and Gene Expression. United States Department of Agriculture, enero de 2001. http://dx.doi.org/10.32747/2001.7575288.bard.

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Most plants accumulate the nonprotein amino acid, g-aminobutyric acid (GABA), in response to heat stress. GABA is made from glutamate in a reaction catalyzed by glutamate decarboxylase (GAD), an enzyme that has been shown by the Israeli PI to be a calmodulin (CaM) binding protein whose activity is regulated in vitro by calcium and CaM. In Arabidopsis there are at least 5 GAD genes, two isoforms of GAD, GAD1 and GAD2, are known to be expressed, both of which appear to be calmodulin-binding proteins. The role of GABA accumulation in stress tolerance remains unclear, and thus the objectives of the proposed work are intended to clarify the possible roles of GABA in stress tolerance by studying the factors which regulate the activity of GAD in vivo. Our intent was to demonstrate the factors that mediate the expression of GAD activity by analyzing the promoters of the GAD1 and GAD2 genes, to determine the role of stress induced calcium signaling in the regulation of GAD activity, to investigate the role of phosphorylation of the CaM-binding domain in the regulation of GAD activity, and to investigate whether ABA signaling could be involved in GAD regulation via the following set of original Project Objectives: 1. Construction of chimeric GAD1 and GAD2 promoter/reporter gene fusions and their utilization for determining cell-specific expression of GAD genes in Arabidopsis. 2. Utilizing transgenic plants harboring chimeric GAD1 promoter-luciferase constructs for isolating mutants in genes controlling GAD1 gene activation in response to heat shock. 3. Assess the role of Ca2+/CaM in the regulation of GAD activity in vivo in Arabidopsis. 4. Study the possible phosphorylation of GAD as a means of regulation of GAD activity. 5. Utilize ABA mutants of Arabidopsis to assess the involvement of this phytohormone in GAD activation by stress stimuli. The major conclusions of Objective 1 was that GAD1 was strongly expressed in the elongating region of the root, while GAD2 was mainly expressed along the phloem in both roots and shoots. In addition, GAD activity was found not to be transcriptionally regulated in response to heat stress. Subsequently, The Israeli side obtained a GAD1 knockout mutation, and in light of the objective 1 results it was determined that characterization of this knockout mutation would contribute more to the project than the proposed Objective 2. The major conclusion of Objective 3 is that heat-stress-induced changes in GAD activity can be explained by heat-stress-induced changes in cytosolic calcium levels. No evidence that GAD activity was transcriptionally or translationally regulated or that protein phosphorylation was involved in GAD regulation (objective 4) was obtained. Previously published data by others showing that in wheat roots ABA regulated GABA accumulation proved not to be the case in Arabidopsis (Objective 5). Consequently, we put the remaining effort in the project into the selection of mutants related to temperature adaptation and GABA utilization and attempting to characterize events resulting from GABA accumulation. A set of 3 heat sensitive mutants that appear to have GABA related mutations have been isolated and partially characterized, and a study linking GABA accumulation to growth stimulation and altered nitrate assimilation were conducted. By providing a better understanding of how GAD activity was and was not regulated in vivo, we have ruled out the use of certain genes for genetically engineering thermotolerance, and suggested other areas of endeavor related to the thrust of the project that may be more likely approaches to genetically engineering thermotolerance.
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Galili, Gad, Harry J. Klee y Asaph Aharoni. Elucidating the impact of enhanced conversion of primary to secondary metabolism on phenylpropanoids secondary metabolites associated with flavor, aroma and health in tomato fruits. United States Department of Agriculture, enero de 2012. http://dx.doi.org/10.32747/2012.7597920.bard.

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• Targeted manipulating Phenylalanine (Phe) synthesis is one of the most powerful strategies to boost the biologically and economically important secondary metabolites, including phenylpropaniods, aromatic volatiles and specialized secondary metabolites. • Over-expression of the petunia MYB transcript factor, ODORANT1 (ODO1), results in significant alterations of the levels of specific phenylpropanoid compounds in plants. • Our previous studies indicated that ectopic expression of the feedback-insensitive AroG could break the bottleneck between primary and secondary metabolisms in tomato, thereby aiding in producing new tomato composition and identifying the unknown roles of multiple key regulators in specialized metabolism. Therefore, combining the AroG and ODO1 is of particular interest for elucidating the combined regulatory role of both of these genes in the Phe metabolic pathway, as well as generating tomato fruits that contain higher levels of secondary metabolites. • Here, we performed the LC-MS and GC-MS analyses on fruits of four tomato genotypes, namely, wild type tomato fruits as well as tomato fruits expressing the AroG, ODO1 and the combination of AroG plus ODO1 (AO) genotypes. Our results elaborated that the levels of many of the Phe-derived metabolites were predominately altered in fruits of the AO genotype, compared to tomato fruits expressing either AroG or ODO1 individually. The levels of most of these metabolites were significantly stimulated, such as Tyrosine (Tyr), coumaric acid and ferulic acid derived metabolites, but the levels of some important secondary metabolites were reduced in the AO transgenic genotypes as compared to either AroG or ODO1 lines. Nevertheless, our results also revealed that the levels of aromatic volatiles were obviously down regulated in the AO, compared to that in AroG transgenic fruits, but were boosted while compared to the wild type and ODO1 transgenic fruits. • Our results suggest that ODO1 expression may also have a negative effect on the production of some of the aromatic volatiles in tomato fruits, indicating that ODO1 acts as an important regulator of the shikimate pathway, which leads to the production of the aromatic amino acids and secondary metabolites derived from them. Key words: AroG, ODO1, tomato, metabolism, shikimate pathway
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Gurevitz, Michael, Michael Adams y Eliahu Zlotkin. Insect Specific Alpha Neurotoxins from Scorpion Venoms: Mode of Action and Structure-Function Relationships. United States Department of Agriculture, junio de 1996. http://dx.doi.org/10.32747/1996.7613029.bard.

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This study was motivated by the need to develop new means and approaches to the design of future, environmentally-safe, insecticides. Utilization of anti-insect selective toxins from scorpion venoms and clarification of the molecular basis for their specificity, are a major focus in this project and may have an applicative value. Our study concentrated on the highly insecticidal toxin, LqhaIT, and was devoted to: (I) Characterization of the neuropharmacological and electrophysiological features of this toxin. (II) Establishment of a genetic system for studying structure/activity relationships of the toxin. (III) Analysis of the insecticidal efficacy of an entomopathogenic baculovirus engineered and expressing LqhaIT. The results obtained in this project suggest that: 1) The receptor binding site of LqhaIT on insect sodium channels differs most likely from its analogous receptor site 3 on vertebrate sodium channels. 2) The effects of LqhaIT are presynaptic. Hyperexcitation at the neuromuscular results from dramatic slowing of sodium channel inactivation and enhanced peak sodium currents causes by LqhaIT. 3) The putative toxic surface of LqhaIT involves aromatic and charged amino acid residues located around the C-terminal region and five-residue-turn of the toxin (unpublished). 4) The anti-insect/anti-mammalian toxicity ratio can be altered by site-directed mutagenesis (publication 8). This effect was partly shown at the level of sodium channel function. 5) The insecticidal efficacy of AcNPV baculovirus increased to a great extent when infection was accompanied by expression of LqhaIT (publication 5).
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Whitham, Steven A., Amit Gal-On y Victor Gaba. Post-transcriptional Regulation of Host Genes Involved with Symptom Expression in Potyviral Infections. United States Department of Agriculture, junio de 2012. http://dx.doi.org/10.32747/2012.7593391.bard.

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Understanding how RNA viruses cause disease symptoms in their hosts is expected to provide information that can be exploited to enhance modern agriculture. The helper component-proteinase (HC-Pro) protein of potyviruses has been implicated in symptom development. Previously, we demonstrated that symptom expression is associated with binding of duplex small-interfering-RNA (duplex-siRNA) to a highly conserved FRNK amino acid motif in the HC-Pro of Zucchini yellow mosaic virus (ZYMV). This binding activity also alters host microRNA (miRNA) profiles. In Turnip mosaic virus (TuMV), which infects the model plant Arabidopsis, mutation of the FRNK motif to FINK was lethal providing further indication of the importance of this motif to HC-Pro function. In this continuation project, our goal was to further investigate how ZYMV and TuMV cause the mis-expression of genes in cucurbits and Arabidopsis, respectively, and to correlate altered gene expression with disease symptoms. Objective 1 was to examine the roles of aromatic and positively charged residues F164RNH and K215RLF adjacent to FR180NK in small RNA binding. Objective 2 was to determine the target genes of the miRNAs which change during HC-Pro expression in infected tissues and transgenic cucumber. Objective 3 was to characterize RNA silencing mechanisms underlying differential expression of host genes. Objective 4 was to analyze the function of miRNA target genes and differentially expressed genes in potyvirus-infected tissues. We found that the charged K/R amino acid residues in the FKNH and KRLF motifs are essential for virus viability. Replacement of K to I in FKNH disrupted duplex-siRNA binding and virus infectivity, while in KRLF mutants duplex-siRNA binding was maintained and virus infectivity was limited: symptomless following a recovery phenomenon. These findings expanded the duplex-siRNA binding activity of HC-Pro to include the adjacent FRNK and FRNH sites. ZYMV causes many squash miRNAs to hyper-accumulate such as miR166, miR390, mir168, and many others. Screening of mir target genes showed that only INCURVATA-4 and PHAVOLUTA were significantly upregulated following ZYMVFRNK infection. Supporting this finding, we found similar developmental symptoms in transgenic Arabidopsis overexpressing P1-HC-Pro of a range of potyviruses to those observed in miR166 mutants. We characterized increased transcription of AGO1 in response to infection with both ZYMV strains. Differences in viral siRNA profiles and accumulation between mild and severe virus infections were characterized by Illumina sequencing, probably due to the differences in HC-Pro binding activity. We determined that the TuMV FINK mutant could accumulate and cause symptoms in dcl2 dcl4 or dcl2 dcl3 dcl4 mutants similar to TuMV FRNK in wild type Arabidopsis plants. These dcl mutant plants are defective in antiviral defenses, and the results show that factors other than HC-ProFRNK motif can induce symptoms in virus-infected plants. As a result of this work, we have a better understanding of the FRNK and FKNH amino acid motifs of HC-Pro and their contributions to the duplex-siRNA binding functions. We have identified plant genes that potentially contribute to infectivity and symptoms of virus infected plants when they are mis-expressed during potyviral infections. The results establish that there are multiple underlying molecular mechanisms that lead viral pathogenicity, some dependent on HC-Pro. The potential benefits include the development of novel strategies for controlling diseases caused by viruses, methods to ensure stable expression of transgenes in genetically improved crops, and improved potyvirus vectors for expression of proteins or peptides in plants.
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