GOT2 dimer transfers amino group from L-Cys to 2OG to form 3MPYR and Glu

Stable Identifier
R-HSA-9012597
Type
Reaction [transition]
Species
Homo sapiens
Compartment
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Hydrogen sulfide (H2S) produced endogenously has been established as the third gaseous signaling molecule, a smooth muscle relaxant and a neuroprotectant (Kimura 2011a, 2011b). Three human enzyme systems produce H2S in the brain, retina and vascular endothelial cells. 3-mercaptopyruvate sulphurtransferase (MPST, aka 3MST) in conjunction with cysteine (aspartate) aminotransferase (CAT, aka GOT2) is decribed here. The first step is the reversible transamination between L-cysteine (L-Cys) and 2-oxoglutarate (2OG, aka alpha-ketoglutarate) to form 3-methylpyruvate (3MPYR) and glutamate (Glu) catalysed by GOT2. Two forms of human aspartate aminotransferase (GOT) enzymes exist; cytosolic (GOT1) and mitochondrial (GOT2). Both are dimeric proteins requiring pyridoxal phosphate for activity. Human GOT2 (Zhou et al. 1998) possesses the same catalytic activity as its rat counterpart (Ubuka et al. 1978).

Literature References
PubMed ID Title Journal Year
9537447 Ethanol up-regulates fatty acid uptake and plasma membrane expression and export of mitochondrial aspartate aminotransferase in HepG2 cells

Zhou, SL, Gordon, RE, Bradbury, M, Stump, D, Kiang, CL, Berk, PD

Hepatology 1998
Participants
Participant Of
Catalyst Activity
Catalyst Activity
Title
L-cysteine:2-oxoglutarate aminotransferase activity of GOT2 dimer [mitochondrial matrix]
Physical Entity
Activity
Inferred From
Cross References
Rhea
Authored
Reviewed
Created