PXLP-K341-GPT2 transaminates PYR to form L-Ala

Stable Identifier
R-HSA-507749
Type
Reaction [transition]
Species
Homo sapiens
Compartment
Synonyms
pyruvate + glutamate <=> alanine + alpha-ketoglutarate [GPT2]
ReviewStatus
5/5
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Glutamic-pyruvate transaminase 2 (alanine aminotransferase 2) (GPT2) catalyzes the reversible reaction of pyruvate and glutamate to form alanine and 2-oxoglutarate (alpha-ketoglutarate) (Yang et al. 2002). Unpublished crystallographic data are consistent with a homodimeric structure for the enzyme with one molecule of pyridoxal phosphate associated with each monomer (PDB 3IHJ). Recent studies of organelles purified from cultured human muscle cells suggest that GPT2 is localized to mitochondria (Glinghammar et al. 2009).
Literature References
PubMed ID Title Journal Year
19360321 Detection of the mitochondrial and catalytically active alanine aminotransferase in human tissues and plasma

Hedberg, JJ, Lindblom, P, Andersson, HB, Berg, AL, Lindstrom, AK, Glinghammar, B, Cotgreave, I, Rafter, I

Int J Mol Med 2009
11863375 cDNA cloning, genomic structure, chromosomal mapping, and functional expression of a novel human alanine aminotransferase

Hansen, BC, Shuldiner, AR, Blaileanu, G, Yang, RZ, Gong, DW

Genomics 2002
Participants
Participates
Event Information
Catalyst Activity

L-alanine:2-oxoglutarate aminotransferase activity of PXLP-K341-GPT2 dimer [mitochondrial matrix]

Orthologous Events
Cross References
RHEA
Rhea
Authored
Reviewed
Created
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