||Alanine--glyoxylate aminotransferase (family a)
||The sequences included here are close homologs of alanine-glyoxylate aminotransferase 1 from rat liver organelles, which is identical to serine-glyoxylate aminotransferase (188.8.131.52) and also to asparagine-oxo-acid aminotransferase (184.108.40.206) [Noguchi & Fujiwara (1988) JBC 263, 182].
The enzymes from Drosophila and Aedes also show alanine-glyoxylate aminotransferase activity.
We have included in this family a number of bacterial sequences, as they seem very closely related to the metazoan ones. It must be remarked, however, that for none of these bacterial enzymes activity has been tested biochemically. Even for the Nostoc (Anabaena) enzyme, whose structure has been published, functional validation is lacking.
|PLP Fold Type
| Articles on 220.127.116.11.a
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
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.
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.
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.