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Journal articles on the topic 'GLYOXYLATE AMINOTRANSFERASE'

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Published: 11 March 2023

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1

Han, Qian, Cihan Yang, Jun Lu, Yinai Zhang, and Jianyong Li. "Metabolism of Oxalate in Humans: A Potential Role Kynurenine Aminotransferase/Glutamine Transaminase/Cysteine Conjugate Betalyase Plays in Hyperoxaluria." Current Medicinal Chemistry 26, no. 26 (October 22, 2019): 4944–63. http://dx.doi.org/10.2174/0929867326666190325095223.

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Hyperoxaluria, excessive urinary oxalate excretion, is a significant health problem worldwide. Disrupted oxalate metabolism has been implicated in hyperoxaluria and accordingly, an enzymatic disturbance in oxalate biosynthesis can result in the primary hyperoxaluria. Alanine-glyoxylate aminotransferase-1 and glyoxylate reductase, the enzymes involving glyoxylate (precursor for oxalate) metabolism, have been related to primary hyperoxalurias. Some studies suggest that other enzymes such as glycolate oxidase and alanine-glyoxylate aminotransferase-2 might be associated with primary hyperoxaluria as well, but evidence of a definitive link is not strong between the clinical cases and gene mutations. There are still some idiopathic hyperoxalurias, which require a further study for the etiologies. Some aminotransferases, particularly kynurenine aminotransferases, can convert glyoxylate to glycine. Based on biochemical and structural characteristics, expression level, and subcellular localization of some aminotransferases, a number of them appear able to catalyze the transamination of glyoxylate to glycine more efficiently than alanine glyoxylate aminotransferase-1. The aim of this minireview is to explore other undermining causes of primary hyperoxaluria and stimulate research toward achieving a comprehensive understanding of underlying mechanisms leading to the disease. Herein, we reviewed all aminotransferases in the liver for their functions in glyoxylate metabolism. Particularly, kynurenine aminotransferase-I and III were carefully discussed regarding their biochemical and structural characteristics, cellular localization, and enzyme inhibition. Kynurenine aminotransferase-III is, so far, the most efficient putative mitochondrial enzyme to transaminate glyoxylate to glycine in mammalian livers, which might be an interesting enzyme to look for in hyperoxaluria etiology of primary hyperoxaluria and should be carefully investigated for its involvement in oxalate metabolism.

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2

Orzechowski, S., J. Socha-Hanc, and A. Paszkowski. "Alanine aminotransferase and glycine aminotransferase from maize (Zea mays L.) leaves." Acta Biochimica Polonica 46, no. 2 (June 30, 1999): 447–57. http://dx.doi.org/10.18388/abp.1999_4176.

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Alanine aminotransferase (AlaAT, EC 2.6.1.2) and glycine aminotransferase (GlyAT, EC 2.6.1.4), two different enzymes catalyzing transamination reactions with L-alanine as the amino-acid substrate, were examined in maize in which alanine participates substantially in nitrogen transport. Preparative PAGE of a partially purified preparation of aminotransferases from maize leaves gave 6 fractions differing in electrophoretic mobility. The fastest migrating fraction I represents AlaAT specific for L-alanine as amino donor and 2-oxoglutarate as amino acceptor. The remaining fractions showed three aminotransferase activities: L-alanine-2-oxoglutarate, L-alanine-glyoxylate and L-glutamate-glyoxylate. By means of molecular sieving on Zorbax SE-250 two groups of enzymes were distinguished in the PAGE fractions: of about 100 kDa and 50 kDa. Molecular mass of 104 kDa was ascribed to AlaAT in fraction I, while the molecular mass of the three enzymatic activities in 3 fractions of the low electrophoretic mobility was about 50 kDa. The response of these fractions to: aminooxyacetate, 3-chloro-L-alanine and competing amino acids prompted us to suggest that five out of the six preparative PAGE fractions represented GlyAT isoforms, differing from each other by the L-glutamate-glyoxylate:L-alanine-glyoxylate:L-alanine-2-oxoglutarate activity ratio.

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3

Donini, Stefano, Manuela Ferrari, Chiara Fedeli, Marco Faini, Ilaria Lamberto, Ada Serena Marletta, Lara Mellini, et al. "Recombinant production of eight human cytosolic aminotransferases and assessment of their potential involvement in glyoxylate metabolism." Biochemical Journal 422, no. 2 (August 13, 2009): 265–72. http://dx.doi.org/10.1042/bj20090748.

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PH1 (primary hyperoxaluria type 1) is a severe inborn disorder of glyoxylate metabolism caused by a functional deficiency of the peroxisomal enzyme AGXT (alanine-glyoxylate aminotransferase), which converts glyoxylate into glycine using L-alanine as the amino-group donor. Even though pre-genomic studies indicate that other human transaminases can convert glyoxylate into glycine, in PH1 patients these enzymes are apparently unable to compensate for the lack of AGXT, perhaps due to their limited levels of expression, their localization in an inappropriate cell compartment or the scarcity of the required amino-group donor. In the present paper, we describe the cloning of eight human cytosolic aminotransferases, their recombinant expression as His6-tagged proteins and a comparative study on their ability to transaminate glyoxylate, using any standard amino acid as an amino-group donor. To selectively quantify the glycine formed, we have developed and validated an assay based on bacterial GO (glycine oxidase); this assay allows the detection of enzymes that produce glycine by transamination in the presence of mixtures of potential amino-group donors and without separation of the product from the substrates. We show that among the eight enzymes tested, only GPT (alanine transaminase) and PSAT1 (phosphoserine aminotransferase 1) can transaminate glyoxylate with good efficiency, using L-glutamate (and, for GPT, also L-alanine) as the best amino-group donor. These findings confirm that glyoxylate transamination can occur in the cytosol, in direct competition with the conversion of glyoxylate into oxalate. The potential implications for the treatment of primary hyperoxaluria are discussed.

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4

Pey, Angel L., Armando Albert, and Eduardo Salido. "Protein Homeostasis Defects of Alanine-Glyoxylate Aminotransferase: New Therapeutic Strategies in Primary Hyperoxaluria Type I." BioMed Research International 2013 (2013): 1–15. http://dx.doi.org/10.1155/2013/687658.

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Alanine-glyoxylate aminotransferase catalyzes the transamination between L-alanine and glyoxylate to produce pyruvate and glycine using pyridoxal 5′-phosphate (PLP) as cofactor. Human alanine-glyoxylate aminotransferase is a peroxisomal enzyme expressed in the hepatocytes, the main site of glyoxylate detoxification. Its deficit causes primary hyperoxaluria type I, a rare but severe inborn error of metabolism. Single amino acid changes are the main type of mutation causing this disease, and considerable effort has been dedicated to the understanding of the molecular consequences of such missense mutations. In this review, we summarize the role of protein homeostasis in the basic mechanisms of primary hyperoxaluria. Intrinsic physicochemical properties of polypeptide chains such as thermodynamic stability, folding, unfolding, and misfolding rates as well as the interaction of different folding states with protein homeostasis networks are essential to understand this disease. The view presented has important implications for the development of new therapeutic strategies based on targeting specific elements of alanine-glyoxylate aminotransferase homeostasis.

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5

IZUMI, Yoshikazu, Toyokazu YOSNIDA, and Hideaki YAMADA. "An assay for serine-glyoxylate aminotransferase." Agricultural and Biological Chemistry 54, no. 6 (1990): 1573–74. http://dx.doi.org/10.1271/bbb1961.54.1573.

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6

Izumi, Yoshikazu, Toyokazu Yoshida, and Hideaki Yamada. "An Assay for Serine-glyoxylate Aminotransferase." Agricultural and Biological Chemistry 54, no. 6 (June 1990): 1573–74. http://dx.doi.org/10.1080/00021369.1990.10870180.

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7

Han, Qian, Howard Robinson, Yi Gui Gao, Nancy Vogelaar, Scott R. Wilson, Menico Rizzi, and Jianyong Li. "Crystal Structures ofAedes aegyptiAlanine Glyoxylate Aminotransferase." Journal of Biological Chemistry 281, no. 48 (September 21, 2006): 37175–82. http://dx.doi.org/10.1074/jbc.m607032200.

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8

Rumsby, G., T. Weir, and C. T. Samuell. "A Semiautomated Alanine: Glyoxylate Aminotransferase Assay for the Tissue Diagnosis of Primary Hyperoxaluria Type 1." Annals of Clinical Biochemistry: International Journal of Laboratory Medicine 34, no. 4 (July 1997): 400–404. http://dx.doi.org/10.1177/000456329703400411.

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We have developed a sensitive assay for the measurement of alanine:glyoxylate aminotransferase (EC 2.6.1.44) activity in human liver. The assay is partly automated, and takes into consideration the sensitivity of the reaction to pH and to glyoxylate concentration. It is less subject to interference from other enzymes utilizing glyoxylate and to chemical interference from glyoxylate itself and can therefore be used without correction for cross-over by glutamate:glyoxylate aminotransferase (EC 2.6.1.4). The assay allows clear discrimination between normal and affected livers and is sufficiently sensitive to measure enzyme activity in fetal liver samples. Enzyme activity ranged from 17·9 to 38·5 μmol/h/mg protein in control livers ( n = 9) and 0·8 to 9·5 μmol/h/mg protein in 30 of 39 hyperoxaluric patients studied. Normal alanine: glyoxylate aminotransferase activity (from 22·8 to 45·5 μmol/h/mg protein) allowed exclusion of primary hyperoxaluria type 1 in the other nine hyperoxaluric patients.

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9

Takada, Y., and T. Noguchi. "Characteristics of alanine: glyoxylate aminotransferase from Saccharomyces cerevisiae, a regulatory enzyme in the glyoxylate pathway of glycine and serine biosynthesis from tricarboxylic acid-cycle intermediates." Biochemical Journal 231, no. 1 (October 1, 1985): 157–63. http://dx.doi.org/10.1042/bj2310157.

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Alanine: glyoxylate aminotransferase (EC 2.6.1.44), which is involved in the glyoxylate pathway of glycine and serine biosynthesis from tricarboxylic acid-cycle intermediates in Saccharomyces cerevisiae, was highly purified and characterized. The enzyme had Mr about 80 000, with two identical subunits. It was highly specific for L-alanine and glyoxylate and contained pyridoxal 5′-phosphate as cofactor. The apparent Km values were 2.1 mM and 0.7 mM for L-alanine and glyoxylate respectively. The activity was low (10 nmol/min per mg of protein) with glucose as sole carbon source, but was remarkably high with ethanol or acetate as carbon source (930 and 430 nmol/min per mg respectively). The transamination of glyoxylate is mainly catalysed by this enzyme in ethanol-grown cells. When glucose-grown cells were incubated in medium containing ethanol as sole carbon source, the activity markedly increased, and the increase was completely blocked by cycloheximide, suggesting that the enzyme is synthesized de novo during the incubation period. Similarity in the amino acid composition was observed, but immunological cross-reactivity was not observed among alanine: glyoxylate aminotransferases from yeast and vertebrate liver.

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10

Sakuraba, Haruhiko. "Studies on Avian Peroxisomal Alanine : Glyoxylate Aminotransferase." Journal of the Kyushu Dental Society 45, no. 3 (1991): 390–408. http://dx.doi.org/10.2504/kds.45.390.

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11

Kontani, Yasuhide, Masae Kaneko, Mariko Kikugawa, Shigeko Fujimoto, and Nanaya Tamaki. "Identity of D-3-aminoisobutyrate-pyruvate aminotransferase with alanine-glyoxylate aminotransferase 2." Biochimica et Biophysica Acta (BBA) - General Subjects 1156, no. 2 (February 1993): 161–66. http://dx.doi.org/10.1016/0304-4165(93)90131-q.

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12

COOPER, Arthur J. L., Boris F. KRASNIKOV, Etsuo OKUNO, and Thomas M. JEITNER. "l-Alanine–glyoxylate aminotransferase II of rat kidney and liver mitochondria possesses cysteine S-conjugate β-lyase activity: a contributing factor to the nephrotoxicity/hepatotoxicity of halogenated alkenes?" Biochemical Journal 376, no. 1 (November 15, 2003): 169–78. http://dx.doi.org/10.1042/bj20030988.

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Several halogenated alkenes are metabolized in part to cysteine S-conjugates, which are mitochondrial toxicants of kidney and, to a lesser extent, other organs. Toxicity is due to cysteine S-conjugate β-lyases, which convert the cysteine S-conjugate into pyruvate, ammonia and a reactive sulphur-containing fragment. A section of the human population is exposed to halogenated alkenes. To understand the health effects of such exposure, it is important to identify cysteine S-conjugate β-lyases that contribute to mitochondrial damage. Mitochondrial aspartate aminotransferase [Cooper, Bruschi, Iriarte and Martinez-Carrion (2002) Biochem. J. 368, 253–261] and mitochondrial branched-chain aminotransferase [Cooper, Bruschi, Conway and Hutson (2003) Biochem. Pharmacol. 65, 181–192] exhibit β-lyase activity toward S-(1,2-dichlorovinyl)-l-cysteine (the cysteine S-conjugate of trichloroethylene) and S-(1,1,2,2-tetrafluoroethyl)-l-cysteine (the cysteine S-conjugate of tetrafluoroethylene). Turnover leads to eventual inactivation of these enzymes. Here we report that mitochondrial l-alanine–glyoxylate aminotransferase II, which, in the rat, is most active in kidney, catalyses cysteine S-conjugate β-lyase reactions with S-(1,1,2,2-tetrafluoroethyl)-l-cysteine, S-(1,2-dichlorovinyl)-l-cysteine and S-(benzothiazolyl-l-cysteine); turnover leads to inactivation. Previous workers showed that the reactive-sulphur-containing fragment released from S-(1,1,2,2-tetrafluoroethyl)-l-cysteine and S-(1,2-dichlorovinyl)-l-cysteine is toxic by acting as a thioacylating agent – particularly of lysine residues in nearby proteins. Toxicity, however, may also involve ‘self-inactivation’ of key enzymes. The present findings suggest that alanine–glyoxylate aminotransferase II may be an important factor in the well-established targeting of rat kidney mitochondria by toxic halogenated cysteine S-conjugates. Previous reports suggest that alanine–glyoxylate aminotransferase II is absent in some humans, but present in others. Alanine–glyoxylate aminotransferase II may contribute to the bioactivation (toxification) of halogenated cysteine S-conjugates in a subset of individuals exposed to halogenated alkenes.

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13

夏, 敬明. "Introduction and Research Progress of Alanine-Glyoxylate Aminotransferase." Open Journal of Nature Science 06, no. 05 (2018): 409–15. http://dx.doi.org/10.12677/ojns.2018.65053.

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14

Wingler, A., V. J. Ann, P. J. Lea, and R. C. Leegood. "Serine: glyoxylate aminotransferase exerts no control on photosynthesis." Journal of Experimental Botany 50, no. 334 (May 1, 1999): 719–22. http://dx.doi.org/10.1093/jxb/50.334.719.

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15

Nagata, Masao, Arata Ichiyama, Tatsuya Takayama, Toshiaki Oda, Soichi Mugiya, and Seiichiro Ozono. "Assay of alanine:glyoxylate aminotransferase in human liver by its serine: glyoxylate aminotransferase activity." Biomedical Research 30, no. 5 (2009): 295–301. http://dx.doi.org/10.2220/biomedres.30.295.

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16

Holbrook, Joanna D., Graeme M. Birdsey, Ziheng Yang, Michael W. Bruford, and Christopher J. Danpure. "Molecular Adaptation of Alanine : Glyoxylate Aminotransferase Targeting in Primates." Molecular Biology and Evolution 17, no. 3 (March 1, 2000): 387–400. http://dx.doi.org/10.1093/oxfordjournals.molbev.a026318.

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17

Ikeda, Mitsunori, Hiroaki Kanouchi, and Yohsuke Minatogawa. "Characterization of Peroxisomal Targeting Signals on Alanine : Glyoxylate Aminotransferase." Biological & Pharmaceutical Bulletin 31, no. 1 (2008): 131–34. http://dx.doi.org/10.1248/bpb.31.131.

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18

Kah, A., D. Dörnemann, and H. Senger. "Isolation and Purification to Apparent Homogeneity of 4,5-Dioxovalerate Aminotransferase from Scenedesmus obliquus Mutant C-2 A′." Zeitschrift für Naturforschung C 43, no. 7-8 (August 1, 1988): 563–71. http://dx.doi.org/10.1515/znc-1988-7-813.

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In the present paper the purification of a specific 4,5-dioxovalerate transaminase from pigment mutant C-2 A′ of the unicellular green alga Scenedesmus obliquus to apparent homogeneity is described. The newly isolated enzyme ʟ-glutamate: 4,5-dioxovalerate aminotransferase is not identical with ʟ-alanine: 4,5-dioxovalerate aminotransferase (EC 2.6.1.43) and ʟ-alanine: glyoxylate aminotransferase (EC 2.6.1.44). A procedure for the purification is described and the resulting homogeneous protein is characterized by its Kᴍ-values for oxo-substrates and amino donors, its pyridoxal phosphate requirement, reversability of the catalysis, pH-optimum, isoelectric point and its molecular weight.

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19

Wingler, A. "Short communication. Serine: glyoxylate aminotransferase exerts no control on photosynthesis." Journal of Experimental Botany 50, no. 334 (May 1, 1999): 719–22. http://dx.doi.org/10.1093/jexbot/50.334.719.

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20

Rumsby, G., R. Jones, C. J. Danpure, and C. T. Samuell. "Taql polymorphism at the alanine: glyoxylate aminotransferase (AGXT) gene locus." Human Molecular Genetics 1, no. 5 (1992): 350. http://dx.doi.org/10.1093/hmg/1.5.350-a.

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21

Okuno, Etsuo, Takaya Ishikawa, Jun Kawai, and Ryo Kido. "Alanine: Glyoxylate aminotransferase activities in liver of Suncus murinus (insectivora)." Comparative Biochemistry and Physiology Part B: Comparative Biochemistry 90, no. 4 (January 1988): 773–78. http://dx.doi.org/10.1016/0305-0491(88)90333-1.

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22

Allsop, Jennifer, Patricia R. Jennings, and Christopher J. Danpure. "A new micro-assay for human liver alanine : Glyoxylate aminotransferase." Clinica Chimica Acta 170, no. 2-3 (December 1987): 187–93. http://dx.doi.org/10.1016/0009-8981(87)90127-6.

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23

Schlösser, Thomas, Cornelia Gätgens, Ulrike Weber, and K. Peter Stahmann. "Alanine : glyoxylate aminotransferase ofSaccharomyces cerevisiae–encoding geneAGX1 and metabolic significance." Yeast 21, no. 1 (January 15, 2004): 63–73. http://dx.doi.org/10.1002/yea.1058.

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24

Noguchi, T., and S. Fujiwara. "Identification of mammalian aminotransferases utilizing glyoxylate or pyruvate as amino acceptor. Peroxisomal and mitochondrial asparagine aminotransferase." Journal of Biological Chemistry 263, no. 1 (January 1988): 182–86. http://dx.doi.org/10.1016/s0021-9258(19)57376-8.

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25

Holmes, R. P., C. H. Hurst, D. G. Assimos, and H. O. Goodman. "Glucagon increases urinary oxalate excretion in the guinea pig." American Journal of Physiology-Endocrinology and Metabolism 269, no. 3 (September 1, 1995): E568—E574. http://dx.doi.org/10.1152/ajpendo.1995.269.3.e568.

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Factors that influence hepatic oxalate synthesis are poorly defined. Hormones are important regulators of hepatic metabolism and could potentially be involved. The effects of hyperglucagonemia were examined in guinea pigs injected with either saline or pharmacological doses of glucagon for 4 days. Glucagon treatment increased mean urinary oxalate excretion by 77% in male and 34% in female animals. The levels of hepatic peroxisomal enzymes involved in oxalate synthesis declined with glucagon treatment, but experiments with isolated peroxisomes indicated that oxalate synthesis in vitro was unaffected. Glucagon decreased hepatic alanine levels by 66%, lactate by 69%, and pyruvate by 73%, but glycolate and glyoxylate levels were unaffected. This decrease in alanine would substantially lower the activity of alanine-to-glyoxylate aminotransferase activity in vivo and make more glyoxylate available for oxalate synthesis. The decrease in lactate and pyruvate concentrations would stimulate the enzymatic conversion of glyoxylate to oxalate and may account for the increase in oxalate synthesis without an increase in glyoxylate concentration. These results demonstrate that hepatic oxalate synthesis is influenced by metabolic changes and that alterations in hepatic alanine, lactate, and pyruvate concentrations may be important elements.

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26

Kukreja, Anjli, Melissa Lasaro, Christian Cobaugh, Chris Forbes, Jian-Ping Tang, Xiang Gao, Cristina Martin-Higueras, et al. "Systemic Alanine Glyoxylate Aminotransferase mRNA Improves Glyoxylate Metabolism in a Mouse Model of Primary Hyperoxaluria Type 1." Nucleic Acid Therapeutics 29, no. 2 (April 2019): 104–13. http://dx.doi.org/10.1089/nat.2018.0740.

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27

Behnam, Joseph T., Emma L. Williams, Susanne Brink, Gill Rumsby, and Christopher J. Danpure. "Reconstruction of human hepatocyte glyoxylate metabolic pathways in stably transformed Chinese-hamster ovary cells." Biochemical Journal 394, no. 2 (February 10, 2006): 409–16. http://dx.doi.org/10.1042/bj20051397.

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Failure to detoxify the intermediary metabolite glyoxylate in human hepatocytes underlies the metabolic pathology of two potentially lethal hereditary calcium oxalate kidney stone diseases, PH (primary hyperoxaluria) types 1 and 2. In order to define more clearly the roles of enzymes involved in the metabolism of glyoxylate, we have established singly, doubly and triply transformed CHO (Chinese-hamster ovary) cell lines, expressing all combinations of normal human AGT (alanine:glyoxylate aminotransferase; the enzyme deficient in PH1), GR/HPR (glyoxylate/hydroxypyruvate reductase; the enzyme deficient in PH2), and GO (glycolate oxidase). We have embarked on the preliminary metabolic analysis of these transformants by studying the indirect toxicity of glycolate as a simple measure of the net intracellular production of glyoxylate. Our results show that glycolate is toxic only to those cells expressing GO and that this toxicity is diminished when AGT and/or GR/HPR are expressed in addition to GO. This finding indicates that we have been able to reconstruct the glycolate→glyoxylate, glyoxylate→glycine, and glyoxylate→glycolate metabolic pathways, catalysed by GO, AGT, and GR/HPR respectively, in cells that do not normally express them. These results are compatible with the findings in PH1 and PH2, in which AGT and GR/HPR deficiencies lead to increased oxalate synthesis, due to the failure to detoxify its immediate precursor glyoxylate. These CHO cell transformants have a potential use as a cell-based bioassay for screening small molecules that stabilize AGT or GR/HPR and might have use in the treatment of PH1 or PH2.

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28

Baker, Paul R. S., Scott D. Cramer, Martha Kennedy, Dean G. Assimos, and Ross P. Holmes. "Glycolate and glyoxylate metabolism in HepG2 cells." American Journal of Physiology-Cell Physiology 287, no. 5 (November 2004): C1359—C1365. http://dx.doi.org/10.1152/ajpcell.00238.2004.

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Oxalate synthesis in human hepatocytes is not well defined despite the clinical significance of its overproduction in diseases such as the primary hyperoxalurias. To further define these steps, the metabolism to oxalate of the oxalate precursors glycolate and glyoxylate and the possible pathways involved were examined in HepG2 cells. These cells were found to contain oxalate, glyoxylate, and glycolate as intracellular metabolites and to excrete oxalate and glycolate into the medium. Glycolate was taken up more effectively by cells than glyoxylate, but glyoxylate was more efficiently converted to oxalate. Oxalate was formed from exogenous glycolate only when cells were exposed to high concentrations. Peroxisomes in HepG2 cells, in contrast to those in human hepatocytes, were not involved in glycolate metabolism. Incubations with purified lactate dehydrogenase suggested that this enzyme was responsible for the metabolism of glycolate to oxalate in HepG2 cells. The formation of14C-labeled glycine from14C-labeled glycolate was observed only when cell membranes were permeabilized with Triton X-100. These results imply that peroxisome permeability to glycolate is restricted in these cells. Mitochondria, which produce glyoxylate from hydroxyproline metabolism, contained both alanine:glyoxylate aminotransferase (AGT)2 and glyoxylate reductase activities, which can convert glyoxylate to glycine and glycolate, respectively. Expression of AGT2 mRNA in HepG2 cells was confirmed by RT-PCR. These results indicate that HepG2 cells will be useful in clarifying the nonperoxisomal metabolism associated with oxalate synthesis in human hepatocytes.

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29

Han, Qian, Seong Ryul Kim, Haizhen Ding, and Jianyong Li. "Evolution of two alanine glyoxylate aminotransferases in mosquito." Biochemical Journal 397, no. 3 (July 13, 2006): 473–81. http://dx.doi.org/10.1042/bj20060469.

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In the mosquito, transamination of 3-HK (3-hydroxykynurenine) to XA (xanthurenic acid) is catalysed by an AGT (alanine glyoxylate aminotransferase) and is the major branch pathway of tryptophan metabolism. Interestingly, malaria parasites hijack this pathway to use XA as a chemical signal for development in the mosquito. Here, we report that the mosquito has two AGT isoenzymes. One is the previously cloned AeHKT [Aedes aegypti HKT (3-HK transaminase)] [Han, Fang and Li (2002) J. Biol. Chem. 277, 15781–15787], similar to hAGT (human AGT), which primarily catalyses 3-HK to XA in mosquitoes, and the other is a typical dipteran insect AGT. We cloned the second AGT from Ae. aegypti mosquitoes [AeAGT (Ae. aegypti AGT)], overexpressed the enzyme in baculovirus/insect cells and determined its biochemical characteristics. We also expressed hAGT for a comparative study. The new cloned AeAGT is highly substrate-specific when compared with hAGT and the previously reported AeHKT and Drosophila AGT, and is translated mainly in pupae and adults, which contrasts with AeHKT that is expressed primarily in larvae. Our results suggest that the physiological requirements of mosquitoes and the interaction between the mosquito and its host appear to be the driving force in mosquito AGT evolution.

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30

Han, Qian, and Jianyong Li. "Comparative characterization ofAedes3-hydroxykynurenine transaminase/alanine glyoxylate transaminase andDrosophilaserine pyruvate aminotransferase." FEBS Letters 527, no. 1-3 (August 28, 2002): 199–204. http://dx.doi.org/10.1016/s0014-5793(02)03229-5.

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31

Satriano, Letizia, Monika Lewinska, Colm O. Rourke, Douglas VNP Oliveira, Deepak Kumar Bhatt, Andrzej Taranta, Monika Herr, et al. "THU-491-The role of alanine glyoxylate aminotransferase in hepatocellular carcinoma." Journal of Hepatology 70, no. 1 (April 2019): e377. http://dx.doi.org/10.1016/s0618-8278(19)30738-8.

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32

McHale, N. A., E. A. Havir, and I. Zelitch. "A mutant of Nicotiana sylvestris deficient in serine glyoxylate aminotransferase activity." Theoretical and Applied Genetics 76, no. 1 (July 1988): 71–75. http://dx.doi.org/10.1007/bf00288834.

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33

Benjamin, Ido, David Kenigsbuch, Mariana Galperin, Javier A. Abrameto, and Yigal Cohen. "Cisgenic melons over expressing glyoxylate-aminotransferase are resistant to downy mildew." European Journal of Plant Pathology 125, no. 3 (May 8, 2009): 355–65. http://dx.doi.org/10.1007/s10658-009-9485-4.

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34

Dindo, Mirco, Silvia Grottelli, Giannamaria Annunziato, Giorgio Giardina, Marco Pieroni, Gioena Pampalone, Andrea Faccini, et al. "Cycloserine enantiomers are reversible inhibitors of human alanine:glyoxylate aminotransferase: implications for Primary Hyperoxaluria type 1." Biochemical Journal 476, no. 24 (December 20, 2019): 3751–68. http://dx.doi.org/10.1042/bcj20190507.

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Peroxisomal alanine:glyoxylate aminotransferase (AGT) is responsible for glyoxylate detoxification in human liver and utilizes pyridoxal 5′-phosphate (PLP) as coenzyme. The deficit of AGT leads to Primary Hyperoxaluria Type I (PH1), a rare disease characterized by calcium oxalate stones deposition in the urinary tract as a consequence of glyoxylate accumulation. Most missense mutations cause AGT misfolding, as in the case of the G41R, which induces aggregation and proteolytic degradation. We have investigated the interaction of wild-type AGT and the pathogenic G41R variant with d-cycloserine (DCS, commercialized as Seromycin), a natural product used as a second-line treatment of multidrug-resistant tuberculosis, and its synthetic enantiomer l-cycloserine (LCS). In contrast with evidences previously reported on other PLP-enzymes, both ligands are AGT reversible inhibitors showing inhibition constants in the micromolar range. While LCS undergoes half-transamination generating a ketimine intermediate and behaves as a classical competitive inhibitor, DCS displays a time-dependent binding mainly generating an oxime intermediate. Using a mammalian cellular model, we found that DCS, but not LCS, is able to promote the correct folding of the G41R variant, as revealed by its increased specific activity and expression as a soluble protein. This effect also translates into an increased glyoxylate detoxification ability of cells expressing the variant upon treatment with DCS. Overall, our findings establish that DCS could play a role as pharmacological chaperone, thus suggesting a new line of intervention against PH1 based on a drug repositioning approach. To a widest extent, this strategy could be applied to other disease-causing mutations leading to AGT misfolding.

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Horváth, V. Andy P., and Ronald J. A. Wanders. "Re-Evaluation of Conditions Required for Measurement of True Alanine:Glyoxylate Aminotransferase Activity in Human Liver: Implications for the Diagnosis of Hyperoxaluria Type I." Annals of Clinical Biochemistry: International Journal of Laboratory Medicine 31, no. 4 (July 1994): 361–66. http://dx.doi.org/10.1177/000456329403100410.

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In this paper we studied the glyoxylate-dependent transamination of L-alanine and L-glutamate in human liver homogenates in order to develop a reliable method for the determination of true alanine:glyoxylate aminotransferase activity in liver homogenates from patients suspected to suffer from hyperoxaluria type I. Measurements were made according to two protocols described in literature in control human liver homogenates which were either untreated or treated with an antiserum raised against purified alanine:glyoxylate aminotransferase. The results obtained show that enzyme activity can best be determined at pH 8.0 as compared to pH 7.4 since the former leads to a higher sensitivity of the method. Alanine:glyoxylate aminotransferase activities measured at pH 8.0 are approximately 50% higher compared to the enzyme activities measured at pH 7.4. Accordingly, it is proposed to measure alanine:glyoxylate aminotransferase activity at pH 8.0 using the newly determined correction factor as described in this paper.

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Murray, A. J. S., R. D. Blackwell, K. W. Joy, and P. J. Lea. "Photorespiratory N donors, aminotransferase specificity and photosynthesis in a mutant of barley deficient in serine: glyoxylate aminotransferase activity." Planta 172, no. 1 (September 1987): 106–13. http://dx.doi.org/10.1007/bf00403035.

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Wang, Bing-Jun, Jing-Ming Xia, Qian Wang, Jiang-Long Yu, Zhiyin Song, and Huabin Zhao. "Diet and Adaptive Evolution of Alanine-Glyoxylate Aminotransferase Mitochondrial Targeting in Birds." Molecular Biology and Evolution 37, no. 3 (November 8, 2019): 786–98. http://dx.doi.org/10.1093/molbev/msz266.

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Abstract Adaptations to different diets represent a hallmark of animal diversity. The diets of birds are highly variable, making them an excellent model system for studying adaptive evolution driven by dietary changes. To test whether molecular adaptations to diet have occurred during the evolution of birds, we examined a dietary enzyme alanine-glyoxylate aminotransferase (AGT), which tends to target mitochondria in carnivorous mammals, peroxisomes in herbivorous mammals, and both mitochondria and peroxisomes in omnivorous mammals. A total of 31 bird species were examined in this study, which included representatives of most major avian lineages. Of these, 29 have an intact mitochondrial targeting sequence (MTS) of AGT. This finding is in stark contrast to mammals, which showed a number of independent losses of the MTS. Our cell-based functional assays revealed that the efficiency of AGT mitochondrial targeting was greatly reduced in unrelated lineages of granivorous birds, yet it tended to be high in insectivorous and carnivorous lineages. Furthermore, we found that proportions of animal tissue in avian diets were positively correlated with mitochondrial targeting efficiencies that were experimentally determined, but not with those that were computationally predicted. Adaptive evolution of AGT mitochondrial targeting in birds was further supported by the detection of positive selection on MTS regions. Our study contributes to the understanding of how diet drives molecular adaptations in animals, and suggests that caution must be taken when computationally predicting protein subcellular targeting.

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Lage, Melissa D., Adrianne M. C. Pittman, Alessandro Roncador, Barbara Cellini, and Chandra L. Tucker. "Allele-specific Characterization of Alanine: Glyoxylate Aminotransferase Variants Associated with Primary Hyperoxaluria." PLoS ONE 9, no. 4 (April 9, 2014): e94338. http://dx.doi.org/10.1371/journal.pone.0094338.

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Hayashi, Sueko, Haruhiko Sakuraba, and Tomoo Noguchi. "Response of hepatic alanine: Glyoxylate aminotransferase 1 to hormone differs among mammalia." Biochemical and Biophysical Research Communications 165, no. 1 (November 1989): 372–76. http://dx.doi.org/10.1016/0006-291x(89)91080-2.

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Maul, Diana M., and Sheldon M. Schuster. "A Comparison of the cytosolic and mitochondrial forms of asparagine/glyoxylate aminotransferase." Archives of Biochemistry and Biophysics 251, no. 2 (December 1986): 577–84. http://dx.doi.org/10.1016/0003-9861(86)90366-8.

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Zhao, Chaohui Lisa, Yiang Hui, Li Juan Wang, Dongfang Yang, Evgeny Yakirevich, Shamlal Mangray, Chiung-Kuei Huang, and Shaolei Lu. "Alanine-glyoxylate aminotransferase 1 (AGXT1) is a novel marker for hepatocellular carcinomas." Human Pathology 80 (October 2018): 76–81. http://dx.doi.org/10.1016/j.humpath.2018.05.025.

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Hameed, Mohammed, Kashif Eqbal, Beena Nair, Alexander Woywodt, and Aimun Ahmed. "Late Diagnosis of Primary Hyperoxaluria by Crystals in the Bone Marrow!" Nephrology @ Point of Care 1, no. 1 (January 2015): napoc.2015.1467. http://dx.doi.org/10.5301/napoc.2015.14679.

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Primary hyperoxaluria type 1 (PH1) is a rare, inherited, autosomal recessive, metabolic disorder caused by a deficiency of peroxisomal alanine-glyoxylate aminotransferase (AGT). We describe here a case of a 57-year-old man with End Stage Renal Disease, where the late age of presentation of PH T1 due to marked heterogeneity of disease expression caused a delay in diagnosis, and we discuss the causes of the poor outcome typical of this condition

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Cellini, Barbara, Mariarita Bertoldi, Riccardo Montioli, Alessandro Paiardini, and Carla Borri Voltattorni. "Human wild-type alanine:glyoxylate aminotransferase and its naturally occurring G82E variant: functional properties and physiological implications." Biochemical Journal 408, no. 1 (October 29, 2007): 39–50. http://dx.doi.org/10.1042/bj20070637.

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Human hepatic peroxisomal AGT (alanine:glyoxylate aminotransferase) is a PLP (pyridoxal 5′-phosphate)-dependent enzyme whose deficiency causes primary hyperoxaluria Type I, a rare autosomal recessive disorder. To acquire experimental evidence for the physiological function of AGT, the Keq,overall of the reaction, the steady-state kinetic parameters of the forward and reverse reactions, and the pre-steady-state kinetics of the half-reactions of the PLP form of AGT with L-alanine or glycine and the PMP (pyridoxamine 5′-phosphate) form with pyruvate or glyoxylate have been measured. The results indicate that the enzyme is highly specific for catalysing glyoxylate to glycine processing, thereby playing a key role in glyoxylate detoxification. Analysis of the reaction course also reveals that PMP remains bound to the enzyme during the catalytic cycle and that the AGT–PMP complex displays a reactivity towards oxo acids higher than that of apoAGT in the presence of PMP. These findings are tentatively related to possible subtle rearrangements at the active site also indicated by the putative binding mode of catalytic intermediates. Additionally, the catalytic and spectroscopic features of the naturally occurring G82E variant have been analysed. Although, like the wild-type, the G82E variant is able to bind 2 mol PLP/dimer, it exhibits a significant reduced affinity for PLP and even more for PMP compared with wild-type, and an altered conformational state of the bound PLP. The striking molecular defect of the mutant, consisting in the dramatic decrease of the overall catalytic activity (∼0.1% of that of normal AGT), appears to be related to the inability to undergo an efficient transaldimination of the PLP form of the enzyme with amino acids as well as an efficient conversion of AGT–PMP into AGT–PLP. Overall, careful biochemical analyses have allowed elucidation of the mechanism of action of AGT and the way in which the disease causing G82E mutation affects it.

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Knight, John, Ross P. Holmes, Scott D. Cramer, Tatsuya Takayama, and Eduardo Salido. "Hydroxyproline metabolism in mouse models of primary hyperoxaluria." American Journal of Physiology-Renal Physiology 302, no. 6 (March 15, 2012): F688—F693. http://dx.doi.org/10.1152/ajprenal.00473.2011.

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Primary hyperoxaluria type 1 (PH1) and type 2 (PH2) are rare genetic diseases that result from deficiencies in glyoxylate metabolism. The increased oxalate synthesis that occurs can lead to kidney stone formation, deposition of calcium oxalate in the kidney and other tissues, and renal failure. Hydroxyproline (Hyp) catabolism, which occurs mainly in the liver and kidney, is a prominent source of glyoxylate and could account for a significant portion of the oxalate produced in PH. To determine the sensitivity of mouse models of PH1 and PH2 to Hyp-derived oxalate, animals were fed diets containing 1% Hyp. Urinary excretions of glycolate and oxalate were used to monitor Hyp catabolism and the kidneys were examined to assess pathological changes. Both strains of knockout (KO) mice excreted more oxalate than wild-type (WT) animals with Hyp feeding. After 4 wk of Hyp feeding, all mice deficient in glyoxylate reductase/hydroxypyruvate reductase (GRHPR KO) developed severe nephrocalcinosis in contrast to animals deficient in alanine-glyoxylate aminotransferase (AGXT KO) where nephrocalcinosis was milder and with a lower frequency. Plasma cystatin C measurements over 4-wk Hyp feeding indicated no significant loss of renal function in WT and AGXT KO animals, and significant and severe loss of renal function in GRHPR KO animals after 2 and 4 wk, respectively. These data suggest that GRHPR activity may be vital in the kidney for limiting the conversion of Hyp-derived glyoxylate to oxalate. As Hyp catabolism may make a major contribution to the oxalate produced in PH patients, Hyp feeding in these mouse models should be useful in understanding the mechanisms associated with calcium oxalate deposition in the kidney.

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Cooper, P. J., C. J. Danpure, P. J. Wise, and K. M. Guttridge. "Immunocytochemical localization of human hepatic alanine: glyoxylate aminotransferase in control subjects and patients with primary hyperoxaluria type 1." Journal of Histochemistry & Cytochemistry 36, no. 10 (October 1988): 1285–94. http://dx.doi.org/10.1177/36.10.3418107.

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Primary hyperoxaluria type 1 (PH1) is an inherited disorder of glyoxylate metabolism caused by a deficiency of the hepatic peroxisomal enzyme alanine: glyoxylate aminotransferase (AGT; EC 2.6.1.44) [FEBS Lett (1986) 201:20]. The aim of the present study was to investigate the intracellular distribution of immunoreactive AGT protein, using protein A-gold immunocytochemistry, in normal human liver and in livers of PH1 patients with (CRM+) or without (CRM-) immunologically crossreacting enzyme protein. In all CRM+ individuals, which included three controls, a PH1 heterozygote and a PH1 homozygote immunoreactive AGT protein was confined to peroxisomes, where it was randomly dispersed throughout the peroxisomal matrix with no obvious association with the peroxisomal membrane. No AGT protein could be detected in the peroxisomes or other cytoplasmic compartments in the livers of CRM- PH1 patients (homozygotes). The peroxisomal labeling density in the CRM+ PH1 patient, who was completely deficient in AGT enzyme activity, was similar to that of the controls. In addition, in the PH1 heterozygote, who had one third normal AGT enzyme activity, peroxisomal labeling density was reduced to 50% of normal.

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Ishikawa, K., E. aneko, and A. Ichiyama. "Pyridoxal 5'-Phosphate Binding of a Recombinant Rat Serine: Pyruvate/Alanine: Glyoxylate Aminotransferase." Journal of Biochemistry 119, no. 5 (May 1, 1996): 970–78. http://dx.doi.org/10.1093/oxfordjournals.jbchem.a021337.

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Liu, Yang, Huihui Xu, Xinpu Yuan, Stephen J. Rossiter, and Shuyi Zhang. "Multiple Adaptive Losses of Alanine-Glyoxylate Aminotransferase Mitochondrial Targeting in Fruit-Eating Bats." Molecular Biology and Evolution 29, no. 6 (January 19, 2012): 1507–11. http://dx.doi.org/10.1093/molbev/mss013.

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Caplin, Ben, Zhen Wang, Anna Slaviero, James Tomlinson, Laura Dowsett, Mathew Delahaye, Alan Salama, David C. Wheeler, and James Leiper. "Alanine-Glyoxylate Aminotransferase-2 Metabolizes Endogenous Methylarginines, Regulates NO, and Controls Blood Pressure." Arteriosclerosis, Thrombosis, and Vascular Biology 32, no. 12 (December 2012): 2892–900. http://dx.doi.org/10.1161/atvbaha.112.254078.

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NISHIJIMA, SAORI, KIMIO SUGAYA, MAKOTO MOROZUMI, TADASHI HATANO, and YOSHIHIDE OGAWA. "Hepatic Alanine-glyoxylate Aminotransferase Activity and Oxalate Metabolism in Vitamin B6 Deficient Rats." Journal of Urology 169, no. 2 (February 2003): 683–86. http://dx.doi.org/10.1016/s0022-5347(05)63992-4.

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Craigen, W. J. "Persistent glycolic aciduria in a healthy child with normal alanine-glyoxylate aminotransferase activity." Journal of Inherited Metabolic Disease 19, no. 6 (November 1996): 793–94. http://dx.doi.org/10.1007/bf01799176.

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