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Статті в журналах з теми "Histidine decarboxyase"

Автор: Grafiati
Опубліковано: 11 березня 2023

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1

MORII, HIDEAKI, and KENTARO KASAMA. "Activity of Two Histidine Decarboxylases from Photobacterium phosphoreum at Different Temperatures, pHs, and NaCl Concentrations." Journal of Food Protection 67, no. 8 (August 1, 2004): 1736–42. http://dx.doi.org/10.4315/0362-028x-67.8.1736.

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Анотація:
The major causative agent of scombroid poisoning is histamine formed by bacterial decarboxylation of histidine. The authors reported previously that histamine was exclusively formed by the psychrotrophic halophilic bacteria Photobacterium phosphoreum in scombroid fish during storage at or below 10°C. Moreover, histamine-forming ability was affected by two histidine decarboxylases: constitutive and inducible enzymes. This article reports the effect of various growth and reaction conditions, such as temperature, pH, and NaCl concentration, on the activity of two histidine decarboxylases that were isolated and separated by gel chromatography from cell-free extracts of P. phosphoreum. The histidine decarboxylase activity of the cell-free extracts was highest in 7°C culture; in 5% NaCl, culture growth was inhibited, and growth was best in the culture grown at pH 6.0. Moreover, percent activity of the constitutive and inducible enzymes was highest for the inducible enzyme in cultures grown at 7°C and pH 7.5 and in 5% NaCl. The temperature and pH dependences of histidine decarboxylase differed between the constitutive and inducible enzymes; that is, the activity of histidine decarboxylases was optimum at 30°C and pH6.5 for the inducible enzyme and 40°C and pH 6.0 for the constitutive enzyme. The differences in the temperature and pH dependences between the two enzymes extended the activity range of histidine decarboxylase under reaction conditions. On the other hand, histidine decarboxylase activity was optimum in 0% NaCl for the two enzymes. Additionally, the effects of reaction temperature, pH, and NaCl concentration on the constitutive enzyme activity of the cell-free extracts were almost the same as those on the whole histidine decarboxylase activity of the cell-free extracts, suggesting that the constitutive enzyme activity reflected the whole histidine decarboxylase activity.
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2

Akirthasary, Desty. "REVIEW ARTIKEL : ENZIM L-HISTIDIN DEKARBOKSILASE DAN MEKANISME PENGHAMBATAN." Unesa Journal of Chemistry 10, no. 2 (May 30, 2021): 147–57. http://dx.doi.org/10.26740/ujc.v10n2.p147-157.

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Анотація:
Abstrak. Enzim L-Histidin dekarboksilase merupakan suatu enzim yang digunakan untuk mengkatalis histidin dalam membentuk histamin. Enzim L-Histidin dekarboksilase dapat dimanfaatkan sebagai antialergi, antihistamin serta menjadi komponen dalam memahami mekanisme histamin. Enzim L-histidin dekarboksilase dapat diperoleh dari asam amino yang ada didalam daging, keju dan ikan. Namun sumber utama yaitu ikan busuk disebabkan aktivitas mikroba diatas 4oC dengan waktu cukup lama, kemudian enzim L-Histidin dekarboksilase yang ada dalam ikan akan disintesis menghasilkan histamin. Enzim L-Histidin dekarboksilase terdapat dalam bakteri mesofilik yang tumbuh pada suhu 30oC-37oC. Bakteri tersebut antara lain Morganella morganii, Klebsiella pneumonia, Hafnia alvei, Citrobacter freundii, Clostridium perfringens, Enterobacter aerogenes, Vibrio alginolyticus, dan Proteus sp yang dapat memberikan pengaruh negatif terhadap kesehatan antara lain diare akibat keracunan, sakit kepala, hipotensi, pruritus dan tubuh akan terlihat memerah. Sehingga diperlukan adanya penghambatan aktivitas enzim L- Histidin dekarboksilase. Penghambatan dapat dilakukan untuk mengontrol terbentuknya histamin dengan cara penambahan senyawa yang akan merusak dinding sel suatu bakteri yang mengakibatkan terhentinya fungsi kerja enzim tersebut. Senyawa penghambat yang dapat digunakan dapat berupa senyawa kimiawi seperti asam benzoat atau dapat juga menggunakan senyawa alami yang memiliki kandungan flavonoid, saponin, terpenoid, dan tanin yang akan mencegah pertumbuhan bakteri. Senyawa penghambat tersebut banyak ditemukan pada Teh Hijau, asam jawa, bawang merah atau tanaman rempah lainnya. Kata Kunci : Enzim L-Histidin dekarboksilase, Histidin, Histamin, Abstract. The enzyme L-Histidine decarboxylase is an enzyme used to catalyze histidine to form histamine. The enzyme L-Histidine decarboxylase can be used as antiallergy, antihistamine and a component in understanding the mechanism of histamine. The enzyme L-histidine decarboxylase can be obtained from amino acids present in meat, cheese and fish. However, the main source is rotten fish due to microbial activity above 4oC for a long time, then the L-Histidine decarboxylase enzyme in fish will be synthesized to produce histamine. L-Histidine decarboxylase enzyme is present in mesophilic bacteria that grow at temperatures of 30oC-37oC. These bacteria include Morganella morganii, Klebsiella pneumonia, Hafnia alvei, Citrobacter freundii, Clostridium perfringens, Enterobacter aerogenes, Vibrio alginolyticus, and Proteus sp which can have negative effects on health, including diarrhea due to poisoning, headaches, hypotension, pruritus and the body. looks red. So that it is necessary to inhibit the activity of the enzyme L-Histidine decarboxylase. Inhibition can be done to control the formation of histamine by adding compounds that will damage the cell wall of a bacteria which results in the cessation of the enzyme function. Inhibition compounds that can be used can be chemical compounds such as benzoic acid or you can also use natural compounds that contain flavonoids, saponins, terpenoids, and tannins that will prevent bacterial growth. These inhibiting compounds are found in green tea, tamarind, onions or other spices. Keyword : Decarboxylated L-Histidine Enxymes, HIstidin, Histamine.
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3

WENDAKOON, CHITRA N., and MORIHIKO SAKAGUCHI. "Inhibition of Amino Acid Decarboxylase Activity of Enterobacter aerogenes by Active Components in Spices." Journal of Food Protection 58, no. 3 (March 1, 1995): 280–83. http://dx.doi.org/10.4315/0362-028x-58.3.280.

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Анотація:
The water and ethanol extracts of several commercially available spices were examined for their inhibitory action on the decarboxylase activity of a crude extract of Enterobacter aerogenes. The water extracts had a negligible effect on histidine decarboxylase activity, except for water extract of cloves which reduced the activity by about 40%. However, the ethanol extracts had a rather higher inhibitory action upon histidine, lysine, and ornithine decarboxylases. Of the spices used, cloves, cinnamon, sage, nutmeg, and allspice were very effective in inhibiting the decarboxylases. Among the components of those spices, cinnamaldehyde and eugenol were found to be effective inhibitors.
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4

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

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Анотація:
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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5

de las RIVAS, BLANCA, ÁNGELA MARCOBAL, ALFONSO V. CARRASCOSA, and ROSARIO MUÑOZ. "PCR Detection of Foodborne Bacteria Producing the Biogenic Amines Histamine, Tyramine, Putrescine, and Cadaverine." Journal of Food Protection 69, no. 10 (October 1, 2006): 2509–14. http://dx.doi.org/10.4315/0362-028x-69.10.2509.

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Анотація:
This study describes an easy PCR method for the detection of foodborne bacteria that potentially produce histamine, tyramine, putrescine, and cadaverine. Synthetic oligonucleotide pairs for the specific detection of the gene coding for each group of bacterial histidine, tyrosine, ornithine, or lysine decarboxylases were designed. Under the conditions used in this study, the assay yielded fragments of 372 and 531 bp from histidine decarboxylase–encoding genes, a 825-bp fragment from tyrosine decarboxylases, fragments of 624 and 1,440 bp from ornithine decarboxylases, and 1,098- and 1,185-bp fragments from lysine decarboxylases. This is the first PCR method for detection of cadaverine-producing bacteria. The method was successfully applied to several biogenic amine–producing bacterial strains.
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6

Sköldberg, Filip, Fredrik Rorsman, Jaakko Perheentupa, Mona Landin-Olsson, Eystein S. Husebye, Jan Gustafsson, and 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, no. 4 (April 1, 2004): 1636–40. http://dx.doi.org/10.1210/jc.2003-031161.

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Анотація:
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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7

Burdychová, Radka. "Identification and typization of bacteria of the genus Enterococcus supposed to be used for the production of functional foods." Acta Universitatis Agriculturae et Silviculturae Mendelianae Brunensis 55, no. 2 (2007): 9–14. http://dx.doi.org/10.11118/actaun200755020009.

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In this study, the species identification of 12 probiotic strains of the genusEnterococcusfrom Culture Collection of Dairy Microorganisms Lactoflora (CCDM, Milcom, Tábor, Czech Republic) were done using PCR described by DUTKA-MALEN et al. (1995). All strains were classified to be of the genusEnterococcusand speciesE. faecium.These strains are supposed to be used as probiotics for the production of functional foods. According to the fact thatE. faeciumwas described to have decarboxylase activity responsible for biogenic amine production in fermented products, the presence of genes coding for microbial tyrosine and histidine decarboxylase was screened in all strains using PCR described by COTON et al. (2004). Whereas the presence of DNA sequences for histidine decarboxylase was not detected in any strain, specific DNA sequences coding for tyrosine decarboxylases were detected in all tested strains. When applying as starter probiotic cultures to fermented milk products, the production of biogenic amine tyramine have to be observed during both fermentation and storage.
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8

Pak, Won-Min, Koth-Bong-Woo-Ri Kim, Min-Ji Kim, Ji-Hye Park, Nan-Young Bae, Sun-Hee Park, and Dong-Hyun Ahn. "Effects of Thermal Treatments on Inactivation of Histidine Decarboxylase from Morganella morganii and Photobacterium phosphoreum." Journal of the Korean Society of Food Science and Nutrition 45, no. 3 (March 31, 2016): 396–401. http://dx.doi.org/10.3746/jkfn.2016.45.3.396.

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9

COSTANTINI, ANTONELLA, MANUELA CERSOSIMO, VINCENZO DEL PRETE, and EMILIA GARCIA-MORUNO. "Production of Biogenic Amines by Lactic Acid Bacteria: Screening by PCR, Thin-Layer Chromatography, and High-Performance Liquid Chromatography of Strains Isolated from Wine and Must." Journal of Food Protection 69, no. 2 (February 1, 2006): 391–96. http://dx.doi.org/10.4315/0362-028x-69.2.391.

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Biogenic amines are frequently found in wine and other fermented food. We investigated the ability of 133 strains of lactic acid bacteria isolated from musts and wines of different origins to produce histamine, tyramine, and putrescine. We detected the genes responsible for encoding the corresponding amino acid decarboxylases through PCR assays using two primer sets for every gene: histidine decarboxylase (hdc), tyrosine decarboxylase (tdc), and ornithine decarboxylase (odc); these primers were taken from the literature or designed by us. Only one strain of Lactobacillus hilgardii was shown to possess the hdc gene, whereas four strains of Lactobacillus brevis had the tdc gene. None of the Oenococcus oeni strains, the main agents of malolactic fermentation, was a biogenic amine producer. All PCR amplicon band–positive results were confirmed by thin-layer chromatography and high-performance liquid chromatography analyses.
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10

FLEMING, John V., Francisca SÁNCHEZ-JIMÉNEZ, Aurelio A. MOYA-GARCÍA, Michael R. LANGLOIS, and Timothy C. WANG. "Mapping of catalytically important residues in the rat l-histidine decarboxylase enzyme using bioinformatic and site-directed mutagenesis approaches." Biochemical Journal 379, no. 2 (April 15, 2004): 253–61. http://dx.doi.org/10.1042/bj20031525.

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Анотація:
HDC (l-histidine decarboxylase), the enzyme responsible for the catalytic production of histamine from l-histidine, belongs to an evolutionarily conserved family of vitamin B6-dependent enzymes known as the group II decarboxylases. Yet despite the obvious importance of histamine, mammalian HDC enzymes remain poorly characterized at both the biochemical and structural levels. By comparison with the recently described crystal structure of the homologous enzyme l-DOPA decarboxylase, we have been able to identify a number of conserved domains and motifs that are important also for HDC catalysis. This includes residues that were proposed to mediate events within the active site, and HDC proteins carrying mutations in these residues were inactive when expressed in reticulocyte cell lysates reactions. Our studies also suggest that a significant change in quartenary structure occurs during catalysis. This involves a protease sensitive loop, and incubating recombinant HDC with an l-histidine substrate analogue altered enzyme structure so that the loop was no longer exposed for tryptic proteolysis. In total, 27 mutant proteins were used to test the proposed importance of 34 different amino acid residues. This is the most extensive mutagenesis study yet to identify catalytically important residues in a mammalian HDC protein sequence and it provides a number of novel insights into the mechanism of histamine biosynthesis.
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11

WADA, HIROSHI, MASATO TAKETOSHI, IKUO IMAMURA, TATSUYA TANAKA, YOSHIYUKI HORIO, YOSHITAKA TAGUCHI, and HIROYUKI FUKUI. "Mammalian Histidine Decarboxylase and DOPA Decarboxylase." Annals of the New York Academy of Sciences 585, no. 1 Vitamin B6 (May 1990): 145–61. http://dx.doi.org/10.1111/j.1749-6632.1990.tb28050.x.

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12

Brosnan, Margaret E., and John T. Brosnan. "Histidine Metabolism and Function." Journal of Nutrition 150, Supplement_1 (October 1, 2020): 2570S—2575S. http://dx.doi.org/10.1093/jn/nxaa079.

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Анотація:
ABSTRACT Histidine is a dietary essential amino acid because it cannot be synthesized in humans. The WHO/FAO requirement for adults for histidine is 10 mg · kg body weight−1 · d−1. Histidine is required for synthesis of proteins. It plays particularly important roles in the active site of enzymes, such as serine proteases (e.g., trypsin) where it is a member of the catalytic triad. Excess histidine may be converted to trans-urocanate by histidine ammonia lyase (histidase) in liver and skin. UV light in skin converts the trans form to cis-urocanate which plays an important protective role in skin. Liver is capable of complete catabolism of histidine by a pathway which requires folic acid for the last step, in which glutamate formiminotransferase converts the intermediate N-formiminoglutamate to glutamate, 5,10 methenyl-tetrahydrofolate, and ammonia. Inborn errors have been recognized in all of the catabolic enzymes of histidine. Histidine is required as a precursor of carnosine in human muscle and parts of the brain where carnosine appears to play an important role as a buffer and antioxidant. It is synthesized in the tissue by carnosine synthase from histidine and β-alanine, at the expense of ATP hydrolysis. Histidine can be decarboxylated to histamine by histidine decarboxylase. This reaction occurs in the enterochromaffin-like cells of the stomach, in the mast cells of the immune system, and in various regions of the brain where histamine may serve as a neurotransmitter.
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13

ROIG-SAGUÉS, ARTUR X., MANUELA HERNÁNDEZ-HERRERO, JOSE J. RODRÍGUEZ-JEREZ, EMILIO I. LÓPEZ-SABATER, and MARIA T. MORA-VENTURA. "Histidine Decarboxylase Activity of Enterobacter cloacae S15/19 during the Production of Ripened Sausages and Its Influence on the Formation of Cadaverine." Journal of Food Protection 60, no. 4 (April 1, 1997): 430–32. http://dx.doi.org/10.4315/0362-028x-60.4.430.

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The histidine decarboxylase activity of Enterobacter cloacae S15/19 was studied during the production process of salchichón, a Spanish ripened sausage. Counts of fecal coliform and histidine decarboxylase bacteria decreased during the production process, showing a good correlation in both inoculated and control samples. In the samples inoculated with Enterobacter cloacae S15/19, fecal coliforms were undetectable the last day of the survey, while the population of histidine decarboxylase bacteria was over 2 log MPN/g. Despite the fact that inoculation with Enterobacter cloacae S15/19 increased histidine decarboxylase bacteria counts, no differences were observed in the histamine concentration reached, which was undetectable in most of the control and inoculated samples. In contrast, cadaverine concentration increased significantly (P < 0.01) in the inoculated samples, suggesting that cadaverine could be used as a hygienic-quality indicator of the raw materials employed in sausage processing.
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14

Gallagher, T., E. E. Snell, and M. L. Hackert. "Pyruvoyl-dependent Histidine Decarboxylase." Journal of Biological Chemistry 264, no. 21 (July 1989): 12737–43. http://dx.doi.org/10.1016/s0021-9258(18)63917-1.

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15

Lucas, Patrick M., Wout A. M. Wolken, Olivier Claisse, Juke S. Lolkema, and Aline Lonvaud-Funel. "Histamine-Producing Pathway Encoded on an Unstable Plasmid in Lactobacillus hilgardii 0006." Applied and Environmental Microbiology 71, no. 3 (March 2005): 1417–24. http://dx.doi.org/10.1128/aem.71.3.1417-1424.2005.

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ABSTRACT Histamine production from histidine in fermented food products by lactic acid bacteria results in food spoilage and is harmful to consumers. We have isolated a histamine-producing lactic acid bacterium, Lactobacillus hilgardii strain IOEB 0006, which could retain or lose the ability to produce histamine depending on culture conditions. The hdcA gene, coding for the histidine decarboxylase of L. hilgardii IOEB 0006, was located on an 80-kb plasmid that proved to be unstable. Sequencing of the hdcA locus disclosed a four-gene cluster encoding the histidine decarboxylase, a protein of unknown function, a histidyl-tRNA synthetase, and a protein, which we named HdcP, showing similarities to integral membrane transporters driving substrate/product exchange. The gene coding for HdcP was cloned downstream of a sequence specifying a histidine tag and expressed in Lactococcus lactis. The recombinant HdcP could drive the uptake of histidine into the cell and the exchange of histidine and histamine. The combination of HdcP and the histidine decarboxylase forms a typical bacterial decarboxylation pathway that may generate metabolic energy or be involved in the acid stress response. Analyses of sequences present in databases suggest that the other two proteins have dispensable functions. These results describe for the first time the genes encoding a histamine-producing pathway and provide clues to the parsimonious distribution and the instability of histamine-producing lactic acid bacteria.
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16

Tanaka, S., and A. Ichikawa. "Intracellular localization of histidine decarboxylase." Inflammation Research 50, S2 (April 2001): 98–99. http://dx.doi.org/10.1007/pl00022423.

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17

Schayer, Richard W. "HISTIDINE DECARBOXYLASE IN MAST CELLS." Annals of the New York Academy of Sciences 103, no. 1 (December 15, 2006): 164–78. http://dx.doi.org/10.1111/j.1749-6632.1963.tb53696.x.

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18

Prozorovskii, V. N., A. E. Alekseeva, and O. G. Grebenshchikov. "Primary structure of histidine decarboxylase." Bulletin of Experimental Biology and Medicine 107, no. 1 (January 1989): 41–44. http://dx.doi.org/10.1007/bf00837053.

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19

Wauters, G., V. Avesani, J. Charlier, M. Janssens, and M. Delmee. "Histidine Decarboxylase in Enterobacteriaceae Revisited." Journal of Clinical Microbiology 42, no. 12 (December 1, 2004): 5923–24. http://dx.doi.org/10.1128/jcm.42.12.5923-5924.2004.

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20

FLEMING, John V., Ignacio FAJARDO, Michael R. LANGLOIS, Francisca SÁNCHEZ-JIMÉNEZ, and Timothy C. WANG. "The C-terminus of rat L-histidine decarboxylase specifically inhibits enzymic activity and disrupts pyridoxal phosphate-dependent interactions with L-histidine substrate analogues." Biochemical Journal 381, no. 3 (July 27, 2004): 769–78. http://dx.doi.org/10.1042/bj20031553.

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Анотація:
Full-length rat HDC (L-histidine decarboxylase) translated in reticulocyte cell lysate reactions is inactive, whereas C-terminally truncated isoforms are capable of histamine biosynthesis. C-terminal processing of the ∼74 kDa full-length protein occurs naturally in vivo, with the production of multiple truncated isoforms. The minimal C-terminal truncation required for the acquisition of catalytic competence has yet to be defined, however, and it remains unclear as to why truncation is needed. Here we show that ∼74 kDa HDC monomers can form dimers, which is the conformation in which the enzyme is thought to be catalytically active. Nevertheless, the resulting dimer is unable to establish pyridoxal phosphate-dependent interactions with an L-histidine substrate analogue. Protein sequences localized to between amino acids 617 and 633 specifically mediate this inhibition. Removing this region or replacing the entire C-terminus with non-HDC protein sequences permitted interactions with the substrate analogue to be re-established. This corresponded exactly with the acquisition of catalytic competence, and the ability to decarboxylate natural L-histidine substrate. These studies suggested that the ∼74 kDa full-length isoform is deficient in substrate binding, and demonstrated that C-terminally truncated isoforms with molecular masses between ∼70 kDa and ∼58 kDa have gradually increasing specific activities. The physiological relevance of our results is discussed in the context of differential expression of HDC isoforms in vivo.
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21

Arnould, J. M. "Mise en évidence in vitro de la biosynthèse d'histamine à partir de carnosine par le rein de souris gravide." Canadian Journal of Physiology and Pharmacology 65, no. 1 (January 1, 1987): 70–74. http://dx.doi.org/10.1139/y87-013.

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Анотація:
Kidneys of pregnant mice synthesize histamine when incubated in the presence of carnosine, manganese, and pyridoxal phosphate. Intensity of biosynthesis increases linearly with the amount of enzyme and the incubation time. The reaction can only be catalysed by two enzymes that are located in kidneys and act in succession: carnosinase, which hydrolyzes carnosine into its two moieties, and histidine decarboxylase, which transforms histidine, a product of carnosine degradation, into histamine. The biosynthesis of histamine from carnosine seems to increase with the progress of pregnancy. In nonpregnant mice, kidneys do not effect this biosynthesis. The above results directly demonstrate that carnosine may be used for histamine synthesis when the activity of histidine decarboxylase is high, as in pregnant mouse kidney. Vertebrate carnosine, its role still enigmatic, might thus be mainly a potential histidine reservoir that would be mobilized any time there is a significant requirement for histidine, such as for histamine biosynthesis.
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22

Suzuki, S., and K. Nakano. "LPS-caused secretion of corticosterone is mediated by histamine through histidine decarboxylase." American Journal of Physiology-Endocrinology and Metabolism 250, no. 3 (March 1, 1986): E243—E247. http://dx.doi.org/10.1152/ajpendo.1986.250.3.e243.

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Escherichia coli lipopolysaccharide (LPS) induced strong time- and dose-dependent secretion of corticosterone (CS) in C3H/HeN mice. In contrast, C3H/HeJ mice were very insensitive to LPS; 100,000 times more LPS was required with C3H/HeJ mice for producing a similar degree of CS secretion as that of C3H/HeN mice. However, C3H/HeJ mice could efficiently respond to other types of stressors, immobilization stress or injection of histamine, a possible mediator of LPS-induced CS secretion (28), leading to a striking increase in the serum levels of CS. Adoptive transfer of spleen cells from C3H/HeN mice converted x-irradiated C3H/HeJ mice to the donor phenotype. Injection of LPS produced a large increase in the activity of histidine decarboxylase (EC 4.1.1.22) in the spleen, lung, and liver of C3H/HeN mice, whereas C3H/HeJ mice were far less responsive. Transfer of spleen cells from the C3H/HeN mice made C3H/HeJ mice sensitive to LPS, leading to an increase in histidine decarboxylase activity in the spleen. There was a statistically significant relationship between the activity of splenic histidine decarboxylase and the serum levels of CS. These results suggest that the LPS-induced secretion of CS is mediated by histamine through induction of histidine decarboxylase in the spleen, lung, and liver. This may be significant in relation to the host-defense mechanism against endotoxemia.
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23

Yamani, Mohammed I., and Friedrich Untermann. "Development of a histidine decarboxylase medium and its application to detect other amino acid decarboxylases." International Journal of Food Microbiology 2, no. 5 (September 1985): 273–78. http://dx.doi.org/10.1016/0168-1605(85)90040-6.

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24

ENGEL, Nora, María Teresa OLMO, Catherine S. COLEMAN, Miguel Angel MEDINA, Anthony E. PEGG, and Francisca SÁNCHEZ-JIMÉNEZ. "Experimental evidence for structure-activity features in common between mammalian histidine decarboxylase and ornithine decarboxylase." Biochemical Journal 320, no. 2 (December 1, 1996): 365–68. http://dx.doi.org/10.1042/bj3200365.

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Анотація:
Common protein motifs between histidine decarboxylase (HDC) and ornithine decarboxylase (ODC) were detected by computational analysis. Mutants were generated and expressed in vitro. In both enzymes, terminal PEST-region-containing fragments are not essential for decarboxylation (PEST regions are sequence fragments enriched in proline, glutamic acid, serine and threonine residues in a hydrophilic fragment flanked by cationic amino acids). The substitution of a very well conserved histidine residue by alanine causes a severalfold increase of the apparent Km values for the respective substrates.
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25

Kitano, Masayuki, Maria Bernsand, Yosuke Kishimoto, Per Norlén, Rolf Håkanson, Yoko Haenuki, Masatoshi Kudo, and Junichi Hasegawa. "Ischemia of rat stomach mobilizes ECL cell histamine." American Journal of Physiology-Gastrointestinal and Liver Physiology 288, no. 5 (May 2005): G1084—G1090. http://dx.doi.org/10.1152/ajpgi.00004.2004.

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Microdialysis was used to study how ischemia-evoked gastric mucosal injury affects rat stomach histamine, which resides in enterochromaffin-like (ECL) cells and mast cells. A microdialysis probe was inserted into the gastric submucosa, and the celiac artery was clamped (30 min), followed by removal of the clamp. Microdialysate histamine was determined by enzyme-linked immunosorbent assay. In addition, we studied the long-term effects of ischemia on the oxyntic mucosal histidine decarboxylase activity in omeprazole-treated rats. Gastric mucosal lesions induced by the ischemia were enlarged on removal of the clamp. The microdialysate histamine concentration increased immediately on clamping (50-fold rise within 30 min) and declined promptly after the clamp was removed. In contrast, histidine decarboxylase activity of the ECL cells was lowered by the ischemia and returned to preischemic values 9 days later. Mast cell-deficient rats responded to ischemia-reperfusion much like wild-type rats with respect to histamine mobilization. Pretreatment with the irreversible inhibitor of histidine decarboxylase, α-fluoromethylhistidine, which is known to eliminate histamine from ECL cells, prevented the rise in microdialysate histamine. Pharmacological blockade of acid secretion (cimetidine or omeprazole) prevented the lesions induced by ischemia-reperfusion insult but not the mobilization of histamine. In conclusion, ischemia of the celiac artery mobilizes large amounts of histamine from ECL cells, which occurs independently of the gross mucosal lesions. The prompt reduction of the mucosal histidine decarboxylase activity in response to ischemia probably reflects ECL cell damage. The lesions develop not because of mobilization of histamine per se but because of ischemia plus reperfusion plus gastric acid.
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26

Gullian Klanian, Mariel, Mariana Delgadillo Díaz, and Maria Sánchez Solís. "Molecular Characterization of Histamine-Producing Psychrotrophic Bacteria Isolated from Red Octopus (Octopus maya) in Refrigerated Storage." High-Throughput 7, no. 3 (September 4, 2018): 25. http://dx.doi.org/10.3390/ht7030025.

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The present study aimed at determining the histamine production capacity of Gram (+) and Gram (−) bacteria isolated from Octopus maya, along with identifying the presence of amino acid decarboxylase genes. Of the total 80 psychrotrophic microorganisms, 32 strains were identified as histamine-forming bacteria. The recombinant DNA technique was used for genotypic identification of histidine (hdc), ornithine (odc), and lysine decarboxylases (ldc) genes. Thirty-two strains were able to produce 60–100 ppm in trypticase soy broth with 1.0% l-histidine after 6 h at 20 °C. NR6B showed 98% homology with Hafnia alvei. NR73 represented 18.8% of the total isolates and showed 98% homology with Enterobacter xianfengensis and Enterobacter cloacae. NR6A represented 6% of the total isolates, which were identified as Lactococcus sp. The hdc gen from NR6B showed 100% identity with hdc from Morganella morganii; ldc showed 97.7% identity with ldc from Citrobacter freundii. The Odc gene was detected only in NR73 and showed 100% identity with Enterobacter sp. All the isolated were identified as weak histamine–former. The ingestion of a food containing small amounts of histamine has little effect on humans; however, the formation of biogenic amines is often considered as an indicator of hygienic quality; this emphasizes the importance of improving good management practices and storage.
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27

Ran, Tingting, Yanyan Gao, May Marsh, Wenjun Zhu, Meitian Wang, Xiang Mao, Langlai Xu, Dongqing Xu, and Weiwu Wang. "Crystal structures of Cg1458 reveal a catalytic lid domain and a common catalytic mechanism for the FAH family." Biochemical Journal 449, no. 1 (December 7, 2012): 51–60. http://dx.doi.org/10.1042/bj20120913.

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Анотація:
Cg1458 was recently characterized as a novel soluble oxaloacetate decarboxylase. However, sequence alignment identified that Cg1458 has no similarity with other oxaloacetate decarboxylases and instead belongs to the FAH (fumarylacetoacetate hydrolase) family. Differences in the function of Cg1458 and other FAH proteins may suggest a different catalytic mechanism. To help elucidate the catalytic mechanism of Cg1458, crystal structures of Cg1458 in both the open and closed conformations have been determined for the first time up to a resolution of 1.9 Å (1 Å=0.1 nm) and 2.0 Å respectively. Comparison of both structures and detailed biochemical studies confirmed the presence of a catalytic lid domain which is missing in the native enzyme structure. In this lid domain, a glutamic acid–histidine dyad was found to be critical in mediating enzymatic catalysis. On the basis of structural modelling and comparison, as well as large-scale sequence alignment studies, we further determined that the catalytic mechanism of Cg1458 is actually through a glutamic acid–histidine–water triad, and this catalytic triad is common among FAH family proteins that catalyse the cleavage of the C–C bond of the substrate. Two sequence motifs, HxxE and Hxx…xxE have been identified as the basis for this mechanism.
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28

Alston, Theodore A., and Robert H. Abeles. "Reaction of Lactobacillus histidine decarboxylase with L-histidine methyl ester." Biochemistry 26, no. 13 (June 30, 1987): 4082–85. http://dx.doi.org/10.1021/bi00387a051.

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29

Rönnberg, Elin, Gabriela Calounova, and Gunnar Pejler. "Mast cells express tyrosine hydroxylase and store dopamine in a serglycin-dependent manner." Biological Chemistry 393, no. 1-2 (January 1, 2012): 107–12. http://dx.doi.org/10.1515/bc-2011-220.

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AbstractHere we show that mast cells contain dopamine and that mast cell activation causes dopamine depletion, indicating its presence within secretory granules. Dopamine storage increased during mast cell maturation from bone marrow precursors, and was dependent on the presence of serglycin. Moreover, the expression of tyrosine hydroxylase, the key enzyme in dopamine biosynthesis, was induced during mast cell maturation; histidine decarboxylase and tryptophan hydroxylase 1 were also induced. Mast cell activation caused a robust induction of histidine decarboxylase, but no stimulation of tyrosine hydroxylase or tryptophan hydroxylase 1 expression. The present study points toward a possible role of dopamine in mast cell function.
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30

Ercan-Sencicek, A. Gulhan, Althea A. Stillman, Ananda K. Ghosh, Kaya Bilguvar, Brian J. O'Roak, Christopher E. Mason, Thomas Abbott, et al. "L-Histidine Decarboxylase and Tourette's Syndrome." New England Journal of Medicine 362, no. 20 (May 20, 2010): 1901–8. http://dx.doi.org/10.1056/nejmoa0907006.

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31

Stockman, J. A. "l-Histidine Decarboxylase and Tourette's Syndrome." Yearbook of Pediatrics 2012 (January 2012): 369–70. http://dx.doi.org/10.1016/j.yped.2010.12.032.

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32

YATSUNAMI, Kimio, Tetsuya FUKUI, and Atsushi ICHIKAWA. "Molecular Biology of L-Histidine Decarboxylase." YAKUGAKU ZASSHI 114, no. 11 (1994): 803–22. http://dx.doi.org/10.1248/yakushi1947.114.11_803.

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33

Darvas, Zsuzsa, Hargita Hegyesi, Valéria László, Márta Bencsáth, András Falus, Mary Haak-Frendscho, Sarolta Kárpáti, et al. "Histidine Decarboxylase Expression in Human Melanoma." Journal of Investigative Dermatology 115, no. 3 (September 2000): 345–52. http://dx.doi.org/10.1046/j.1523-1747.2000.00054.x.

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34

Huynh, Q. K., and E. E. Snell. "Pyruvoyl-dependent histidine decarboxylases. Preparation and amino acid sequences of the beta chains of histidine decarboxylase from Clostridium perfringens and Lactobacillus buchneri." Journal of Biological Chemistry 260, no. 5 (March 1985): 2798–803. http://dx.doi.org/10.1016/s0021-9258(18)89433-9.

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35

Abe, Keietsu, Fumito Ohnishi, Kyoko Yagi, Tasuku Nakajima, Takeshi Higuchi, Motoaki Sano, Masayuki Machida, Rafiquel I. Sarker, and Peter C. Maloney. "Plasmid-Encoded asp Operon Confers a Proton Motive Metabolic Cycle Catalyzed by an Aspartate-Alanine Exchange Reaction." Journal of Bacteriology 184, no. 11 (June 1, 2002): 2906–13. http://dx.doi.org/10.1128/jb.184.11.2906-2913.2002.

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ABSTRACT Tetragenococcus halophila D10 catalyzes the decarboxylation of l-aspartate with nearly stoichiometric release of l-alanine and CO2. This trait is encoded on a 25-kb plasmid, pD1. We found in this plasmid a putative asp operon consisting of two genes, which we designated aspD and aspT, encoding an l-aspartate-β-decarboxylase (AspD) and an aspartate-alanine antiporter (AspT), respectively, and determined the nucleotide sequences. The sequence analysis revealed that the genes of the asp operon in pD1 were in the following order: promoter → aspD → aspT. The deduced amino acid sequence of AspD showed similarity to the sequences of two known l-aspartate-β-decarboxylases from Pseudomonas dacunhae and Alcaligenes faecalis. Hydropathy analyses suggested that the aspT gene product encodes a hydrophobic protein with multiple membrane-spanning regions. The operon was subcloned into the Escherichia coli expression vector pTrc99A, and the two genes were cotranscribed in the resulting plasmid, pTrcAsp. Expression of the asp operon in E. coli coincided with appearance of the capacity to catalyze the decarboxylation of aspartate to alanine. Histidine-tagged AspD (AspDHis) was also expressed in E. coli and purified from cell extracts. The purified AspDHis clearly exhibited activity of l-aspartate-β-decarboxylase. Recombinant AspT was solubilized from E. coli membranes and reconstituted in proteoliposomes. The reconstituted AspT catalyzed self-exchange of aspartate and electrogenic heterologous exchange of aspartate with alanine. Thus, the asp operon confers a proton motive metabolic cycle consisting of the electrogenic aspartate-alanine antiporter and the aspartate decarboxylase, which keeps intracellular levels of alanine, the countersubstrate for aspartate, high.
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36

Araki, Masataka, Mitsuo Nakamura, Seiichi Takenoshita, Hirokazu Shoda, Yukio Nagamachi, and Shigeru Matsuzaki. "Effects of dexamethasone on the activity of histidine decarboxylase, ornithine decarboxylase, and DOPA decarboxylase in rat oxyntic mucosa." Canadian Journal of Physiology and Pharmacology 69, no. 1 (January 1, 1991): 37–42. http://dx.doi.org/10.1139/y91-006.

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Since accelerated turnover of histamine in oxyntic mucosa may be an important factor in the pathogenesis of peptic ulcers, the effect of dexamethasone and other glucocorticoids on the activity of gastric histidine decarboxylase (HDC) was studied in the rat. The activity of HDC in rat oxyntic mucosa increased significantly after dexamethasone was injected s.c. to rats at doses larger than 0.4 mg/kg body weight. The maximum response of the HDC activity to dexamethasone (4 mg/kg) was observed 8 h after the treatment. The activity of ornithine decarboxylase (ODC) increased at 4 h, while that of DOPA decarboxylase showed no significant change throughout the 16-h period following a single injection of dexamethasone. The mucosal levels of histamine, putrescine, and spermidine rose significantly after the steroid treatment, while the spermine levels remained nearly constant. There was no sex difference in these responses to dexamethasone. Betamethasone showed nearly the same effects as dexamethasone on the decarboxylase activities and the mucosal levels of diamines. Serum gastrin levels showed no significant change for the first 4 h and then rose significantly 8 and 16 h after dexamethasone treatment. Pentagastrin (0.5 mg/kg) increased the HDC activity, while it showed no significant effect on either the mucosal ODC activity or levels of polyamines and histamine. These data suggest that dexamethasone influences the metabolism of histamine and polyamines in rat oxyntic mucosa both directly and via stimulation of gastrin release.Key words: dexamethasone, betamethasone, oxyntic mucosa, histidine decarboxylase, ornithine decarboxylase, DOPA decarboxylase.
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37

Kučerová, K., H. Svobodová, Š. Tůma, I. Ondráčková, and M. Plocková. "Production of biogenic amines by Enterococci." Czech Journal of Food Sciences 27, Special Issue 2 (January 3, 2010): 50–55. http://dx.doi.org/10.17221/673-cjfs.

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Enterococci were presented in all tested samples of raw cow milk (six samples) at the level 10<sup>3</sup>&ndash;10<sup>5</sup> CFU/ml, fresh cheeses (five samples) at the level 10<sup>2</sup>&ndash;10<sup>6</sup> CFU/g and semi-hard cheeses (five samples) at the level 10<sup>3</sup>&ndash;10<sup>5</sup> CFU/g. All 33 isolated Enterococcus strains were screened for decarboxylase activity by usage differential growth medium and 20 of them possessed tyrosine decarboxylase activity. A collection of eight strains with the strongest decarboxylase activity were identified by species specific PCR as E. faecium (Z3, Z4, Br4 and 6/4D strains) and E. faecalis (Ž4, 3/3C and 4/1A strains). Enterococcus spp. Z1 strain was not identified at the species level by used methods, but the genus was confirmed by PCR method. Their tyrosin decarboxylase activity was confirmed by TLC and detection of tdc gene. Z1, Z3 and Z4 strains showed also histidine decarboxylase activity on the differential growth medium with histidine, but this activity was evaluated by TLC as a false positive reaction of medium.
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38

Olmo, M. T., F. Sanchez-Jimenez, M. A. Medina, and H. Hayashi. "Spectroscopic Analysis of Recombinant Rat Histidine Decarboxylase." Journal of Biochemistry 132, no. 3 (September 1, 2002): 433–39. http://dx.doi.org/10.1093/oxfordjournals.jbchem.a003240.

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39

Rollan, G. C., E. Coton, and A. Lonvaud-Funel. "Histidine decarboxylase activity of Leuconostoc oenos 9204." Food Microbiology 12 (February 1995): 455–61. http://dx.doi.org/10.1016/s0740-0020(95)80130-8.

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40

Yatsunami, K., H. Ohtsu, M. Tsuchikawa, T. Higuchi, K. Ishibashi, A. Shida, Y. Shima, S. Nakagawa, K. Yamauchi, and M. Yamamoto. "Structure of the L-histidine decarboxylase gene." Journal of Biological Chemistry 269, no. 2 (January 1994): 1554–59. http://dx.doi.org/10.1016/s0021-9258(17)42292-7.

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41

Moya-Garcia, Aurelio A., Miguel Ángel Medina, and Francisca Sánchez-Jiménez. "Mammalian histidine decarboxylase: from structure to function." BioEssays 27, no. 1 (December 20, 2004): 57–63. http://dx.doi.org/10.1002/bies.20174.

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42

Sneha Bhatt, Gletta Anjaly C.T, and Shlini P. "Pharmacokinetic properties of inhibitors to Histidine Decarboxylase isolated from fennel." International Journal of Research in Pharmaceutical Sciences 11, no. 4 (November 17, 2020): 6707–14. http://dx.doi.org/10.26452/ijrps.v11i4.3597.

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Анотація:
Histamine release is involved in developing wakefulness and activation of cortex. The purpose of the study was to find an alternative to these antihistamines by inhibiting the enzyme histidine decarboxylase which is responsible for the production of histamine. Histamine brings about the allergic response due to mast cell degranulation. It is also necessary that the enzyme is not completely inhibited as it plays a role as a neurotransmitter and also regulates gastric acid secretion. In the present study, the methanolic extract of commercially available fennel seeds were examined for its inhibitory activity on the purified extract of bacterial histidine decarboxylase. The methanolic extract of fennel was analyzed to check the presence of various phytochemical constituents. The spice extract was quantified to estimate the presence of flavonoids. The extract was subjected to purification by thin layer chromatography and HPLC in order to isolate and identify the flavonoids present in spice extract. The HPLC results with reference to the standard indicated the presence of ellagic acid and quercetin. The spice extracts were subjected to inhibitory studies at increasing concentrations. The fennel extract at concentration of 0.625 moles was found to be inhibiting histidine decarboxylase which was determined using the Dixon plot. The identified flavonoids were then subjected to software’s like Molinspiration and Swiss ADME in order to study the molecular properties, drug likeliness and pharmacokinetics.
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43

Rossi, Franca, Fausto Gardini, Lucia Rizzotti, Federica La Gioia, Giulia Tabanelli, and Sandra Torriani. "Quantitative Analysis of Histidine Decarboxylase Gene (hdcA) Transcription and Histamine Production by Streptococcus thermophilus PRI60 under Conditions Relevant to Cheese Making." Applied and Environmental Microbiology 77, no. 8 (March 4, 2011): 2817–22. http://dx.doi.org/10.1128/aem.02531-10.

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ABSTRACTThis study evaluated the influence of parameters relevant for cheese making on histamine formation byStreptococcus thermophilus. Strains possessing a histidine decarboxylase (hdcA) gene represented 6% of the dairy isolates screened. The most histaminogenic,S. thermophilusPRI60, exhibited in skim milk a high basal level of expression ofhdcA, upregulation in the presence of free histidine and salt, and repression after thermization. HdcA activity persisted in cell extracts, indicating that histamine might accumulate after cell lysis in cheese.
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44

Ding, X. Q., D. Chen, E. Rosengren, L. Persson, and R. Hakanson. "Comparison between activation of ornithine decarboxylase and histidine decarboxylase in rat stomach." American Journal of Physiology-Gastrointestinal and Liver Physiology 270, no. 3 (March 1, 1996): G476—G486. http://dx.doi.org/10.1152/ajpgi.1996.270.3.g476.

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We compared the responses of rat stomach ornithine decarboxylase (ODC) and histidine decarboxylase (HDC) to food intake, oral treatment with antisecretagogues, NaHCO3, and hypertonic NaCl, antrectomy, intravenous infusion of gastrin-17, the selective cholecystokinin (CCK)-B/gastrin receptor antagonist L-365,260, and the somatostatin analogue RC-160. The serum gastrin concentration and oxyntic mucosal ODC and HDC activities were higher in freely fed rats than in fasted rats. Food intake in fasted rats raised the serum gastrin concentration and the ODC and HDC activities. Ranitidine, omeprazole, and NaHCO3 raised the serum gastrin concentration and activated ODC and HDC. Hypertonic NaCl raised the ODC activity 200-fold, whereas circulating gastrin and HDC activity were increased only moderately. Infusion of gastrin-17 activated HDC but not ODC. L-365,260 prevented the activation of HDC but not of ODC in response to food intake and treatment with omeprazole, NaHCO3, or hypertonic NaCl. Antrectomy prevented the food- and omeprazole-evoked rise in oxyntic mucosal HDC activity but not the rise in ODC activity. RC-160 suppressed HDC activity after food intake and treatment with omeprazole, NaHCO3, or NaCl. In contrast, RC-160 suppressed omeprazole- and NaHCO3-evoked ODC activation but not that evoked by food intake or NaCl. The results support the view that HDC in the oxyntic mucosa is activated by gastrin and suppressed by somatostatin. The induction of ODC is not mediated by gastrin; ODC activation appears to be related to acid inhibition per se or to mucosal maintenance and repair; somatostatin, or rather the lack of it, might contribute to the induction of ODC after acid blockade. The mechanism behind the activation of rat stomach ODC seems to differ depending on the type of stimulus.
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45

MARCOBAL, ÁNGELA, BLANCA de las RIVAS, M. VICTORIA MORENO-ARRIBAS, and ROSARIO MUÑOZ. "Multiplex PCR Method for the Simultaneous Detection of Histamine-, Tyramine-, and Putrescine-Producing Lactic Acid Bacteria in Foods." Journal of Food Protection 68, no. 4 (April 1, 2005): 874–78. http://dx.doi.org/10.4315/0362-028x-68.4.874.

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In a screening of primers, we have selected three pairs of primers for a multiplex PCR assay for the simultaneous detection of lactic acid bacteria (LAB) strains, which potentially produce histamine, tyramine, and putrescine on fermented foods. These primers were based on sequences from histidine, tyrosine, and ornithine decarboxylases from LAB. Under the optimized conditions, the assay yielded a 367-bp DNA fragment from histidine decarboxylases, a 924-bp fragment from tyrosine decarboxylases, and a 1,446-bp fragment from ornithine decarboxylases. When the DNAs of several target organisms were included in the same reaction, two or three corresponding amplicons of different sizes were observed. This assay was useful for the detection of amine-producing bacteria in control collection strains and in a LAB collection. No amplification was observed with DNA from nonproducing LAB strains. This article is the first describing a multiplex PCR approach for the simultaneous detection of potentially amine-producing LAB in foods. It can be easily incorporated into the routine screening for the accurate selection of starter LAB and in food control laboratories.
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46

Middleton, Richard J., S. A. M. Martin, and Grahame Bulfield. "A new regulatory gene in the histidine decarboxylase gene complex determines the responsiveness of the mouse kidney enzyme to testosterone." Genetical Research 49, no. 1 (February 1987): 61–67. http://dx.doi.org/10.1017/s0016672300026744.

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SummaryThe level of histidine decarboxylase in mouse kidney normally differs between the sexes with females higher than males. In a strain derived from feral Danish mice (DAN), however, both males and females have the same, high, HDC activity due to the males being insensitive to repression by testosterone. Genetic analysis indicates that this insensitivity is caused by a variant allele of a new gene in the histidine decarboxylase gene complex, Hdc-a; the Hdc-ab allele in C57BL/10 confers high sensitivity to testosterone whereas the Hdc-aw allele in the DAN strain confers low sensitivity. In addition, the DAN strain has a novel haplotype for the other three known elements of [Hdc]: the allele Hdc-sd of the structural gene, the Hdc-cd allele of the gene determining enzyme concentration, and the oestrogen-inducible allele Hdc-eb.
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47

ICHIKAWA, Atsushi, Yukihiko SUGIMOTO, and Satoshi TANAKA. "Molecular biology of histidine decarboxylase and prostaglandin receptors." Proceedings of the Japan Academy, Series B 86, no. 8 (2010): 848–66. http://dx.doi.org/10.2183/pjab.86.848.

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48

Thiebaut, R., B. Garzon, P. Millet, E. Moreau, R. Ducroc, and J. P. Geloso. "Development of Gastric Histidine Decarboxylase in the Rat." Journal of Pediatric Gastroenterology and Nutrition 4, no. 3 (June 1985): 482–88. http://dx.doi.org/10.1097/00005176-198506000-00027.

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49

Nitta, Yoko, Hiroe Kikuzaki, and Hiroshi Ueno. "Food Components Inhibiting Recombinant Human Histidine Decarboxylase Activity." Journal of Agricultural and Food Chemistry 55, no. 2 (January 2007): 299–304. http://dx.doi.org/10.1021/jf062392k.

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50

MATSUMOTO, NAOKI, NAOKI AGATA, HIROSHI KUBOKI, HIRONOBU IINUMA, TSUTOMU SAWA, TOMIO TAKEUCHI, and KAZUO UMEZAWA. "Inhibition of Rat Embryo Histidine Decarboxylase by Epoxyquinomicins." Journal of Antibiotics 53, no. 6 (2000): 637–39. http://dx.doi.org/10.7164/antibiotics.53.637.

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