B6db activities : 2_6_1

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	2.6.1.44
Description	Alanine--glyoxylate aminotransferase
Alternative names	L-alanine-glyoxylate transaminase; L-alanine-glycine transaminase; AGT; AGXT; serine-glyoxylate aminotransferase (ambiguous); 3-hydroxykynurenine transaminase (ambiguous);
Catalyzed reaction	L-alanine + glyoxylate = pyruvate + glycine.
Cofactor	Pyridoxal-phosphate.
Comments	-!- With one component of the animal enzyme, 2-oxobutanoate can replace glyoxylate. A second component also catalyzes the reaction of EC 2.6.1.51.
	The eukariotic sequences included in family a are close homologs of alanine:glyoxylate aminotransferase 1 from rat liver organelles, which in turn is identical to serine-pyruvate aminotransferase (2.6.1.51) and asparagine-oxo-acid aminotransferase (2.6.1.14)[Noguchi & Fujiwara (1988) JBC 263, 182]. The so-called alanine:glyoxylate aminotransferase 2 (AGXT2) from rat liver appears to be identical to (D)-3-amino-2-methylpropanoate aminotransferase (2.6.1.40) and aminolevulinate aminotransferase (2.6.1.43). Sequences of AGXT2 close homologs (which are very different from those in family a) are listed under 2.6.1.40. The archaeal sequences included in family b are not closely related to the eukariotic enzymes with alanine-glyoxylate aminotransferase activity.
Diseases	Primary hyperoxaluria type 1
Prosite	PROSITE; PS00600;
PDB	1H0C; 2YOB; 3ZRR; 2ZC0;
Organisms	-Eubacteria -Archea -Plants -Fungi -Metazoa -Human
Family	2.6.1.44_a (0) 2.6.1.44_b (0)

Links	Enzyme (activities) 2.6.1.44 BRENDA (activities) 2.6.1.44 KEGG (pathways) 2.6.1.44 PLPMDB (PLP mutants) 2.6.1.44

References	Wu D, Feng M1, Wang ZX, Qiao K, Tachibana H, Cheng XJ (2018) Molecular and biochemical characterization of key enzymes in the cysteine and serine metabolic pathways of Acanthamoeba castellanii Parasit Vectors 11 604. Sayer C, Bommer M, Isupov M, Ward J, Littlechild J (2012) Crystal structure and substrate specificity of the thermophilic serine:pyruvate aminotransferase from Sulfolobus solfataricus Acta Crystallogr D Biol Crystallogr 68 763-72. Littlechild,J.A. (2011) Thermophilic archaeal enzymes and applications in biocatalysis Biochem Soc Trans 39 155-8. Sakuraba H, Yoneda K, Takeuchi K, Tsuge H, Katunuma N, Ohshima T. (2008) Structure of an archaeal alanine:glyoxylate aminotransferase Acta Crystallogr D Biol Crystallogr 64 696-9. Han GW, Schwarzenbacher R, Page R et al. (2005) Crystal structure of an alanine-glyoxylate aminotransferase from Anabaena sp. at 1.70 A resolution reveals a noncovalently linked PLP cofactor. Proteins 58 971-75. Sakuraba, H.; Kawakami, R.; Takahashi, H.; Ohshima, T. (2004) Novel archaeal alanine:glyoxylate aminotransferase from Thermococcus litoralis J Bacteriol 186 15292154. Zhang, X.; Roe, S.M.; Hou, Y.; Bartlam, M.; Rao, Z.; Pearl, L.H.; Danpure, C. J. (2003) Crystal structure of alanine:glyoxylate aminotransferase and the relationship between genotype and enzymatic phenotype in primary hyperoxaluria type 1 J Mol Biol 331 643-52. Han, Q.; Fang, J.; Li, J. (2002) 3-Hydroxykynurenine transaminase identity with alanine glyoxylate transaminase. A probable detoxification protein in Aedes aegypti J Biol Chem 277 15781-7. Han, Q.; Li, J. (2002) Comparative characterization of Aedes 3-hydroxykynurenine transaminase/alanine glyoxylate transaminase and Drosophila serine pyruvate aminotransferase FEBS Lett 527 199-204. Lumb, M. J.; Danpure, C. J. (2000) Functional synergism between the most common polymorphism in human alanine:glyoxylate aminotransferase and four of the most common disease- causing mutations J Biol Chem 275 36415-22. Oda, T.; Miyajima, H.; Suzuki, Y.; Ito, T.; Yokota, S.; Hoshino, M.; Ichiyama, A. (1989) Purification and characterization of the active serine: pyruvate aminotransferase of rat liver mitochondria expressed in Escherichia coli J Biochem (Tokyo) 106 460-7. Articles on 2.6.1.44

last changed	2019/09/19 12:23

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