Reactome | alpha-ketoglutarate + NH4+ + NAD(P)H + H+ <=> glutamate + NAD(P)+ (GLUD1,2)

alpha-ketoglutarate + NH4+ + NAD(P)H + H+ <=> glutamate + NAD(P)+ (GLUD1,2)

Stable Identifier

R-HSA-70589

Type

Reaction [transition]

Species

Homo sapiens

Compartment

mitochondrial matrix

Synonyms

2-oxoglutarate + H(+) + NADH + NH4(+) => H2O + L-glutamate + NAD(+), 2-oxoglutarate + H(+) + NADPH + NH4(+) => H2O + L-glutamate + NADP(+)

ReviewStatus

5/5

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alpha-ketoglutarate + NH4+ + NAD(P)H + H+ <=> glutamate + NAD(P)+ (GLUD1,2)

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Mitochondrial glutamate dehydrogenase 1 (GLUD1) catalyzes the reversible reaction of 2-oxoglutarate, NAD(P)H + H+, and ammonia to form glutamate and NAD(P)+ (Fang et al. 2002). Mature GLUD1 protein lacks the 53 aminoterminal residues of the nascent protein (Julliard and Smith 1979), which function as a mitochondrial import signal. The active form of the enzyme is a hexamer, allosterically activated by ADP and inhibited by GTP (Fang et al. 2002; Smith et al. 2002). GLUD2 is inferred to catalyze the same reaction based on its structural similarity to GLUD1.

Literature References

PubMed ID	Title	Journal	Year
429360	Partial amino acid sequence of the glutamate dehydrogenase of human liver and a revision of the sequence of the bovine enzyme Julliard, JH, Smith, EL	J Biol Chem	1979
11903050	Expression, purification and characterization of human glutamate dehydrogenase (GDH) allosteric regulatory mutations Smith, TJ, MacMullen, CM, Hsu, BY, Fang, J, Poncz, M, Stanley, CA	Biochem J	2002
12054821	The structure of apo human glutamate dehydrogenase details subunit communication and allostery Smith, TJ, Wu, J, Schmidt, T, Fang, J, Stanley, CA, Siuzdak, G	J Mol Biol	2002