Mitochondrial AGXT2 tetramer transaminates glyoxylate and alanine to glycine and pyruvate

Stable Identifier
R-HSA-904864
Type
Reaction [transition]
Species
Homo sapiens
Compartment
Synonyms
glyoxylate + alanine => glycine + pyruvate [mitochondrial matrix]
ReviewStatus
5/5
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Mitochondrial AGXT2 (alanine-glyoxylate transaminase 2) catalyzes the irreversible reaction of glyoxylate and alanine to form glycine and pyruvate (Rodionov et al. 2010). The active form of the enzyme is inferred to be a homotetramer from the properties of the homologous rat protein, which has been purified and characterized in vitro (Tamaki et al.990). Most conversion of glyoxylate to glycine in vivo appears to occur in the peroxisome, catalyzed by AGXT, and the physiological role of the AGXT2 reaction is unclear.
Literature References
PubMed ID Title Journal Year
2158891 Purification, characterization and inhibition of D-3-aminoisobutyrate aminotransferase from the rat liver

Mizota, C, Kaneko, M, Kikugawa, M, Fujimoto, S, Tamaki, N

Eur J Biochem 1990
20018850 Human alanine-glyoxylate aminotransferase 2 lowers asymmetric dimethylarginine and protects from inhibition of nitric oxide production

Lentz, SR, Rodionov, RN, Stevens, JW, Murry, DJ, Vaulman, SF

J Biol Chem 2010
Participants
Participates
Event Information
Catalyst Activity

alanine-glyoxylate transaminase activity of AGXT2 tetramer [mitochondrial matrix]

Orthologous Events
Cross References
Rhea
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