|Superclasses:||Reactions Classified By Conversion Type → Simple Reactions → Chemical Reactions|
|Reactions Classified By Substrate → Small-Molecule Reactions|
In Pathway: gluconeogenesis I
The reaction direction shown, that is, A + B ↔ C + D versus C + D ↔ A + B, is in accordance with the Enzyme Commission system.
Mass balance status: Balanced.
Enzyme Commission Primary Name for 184.108.40.206: malate dehydrogenase (oxaloacetate-decarboxylating)
Enzyme Commission Synonyms for 220.127.116.11: 'malic' enzyme (ambiguous), pyruvic-malic carboxylase (ambiguous), NAD+-specific malic enzyme, NAD+-malic enzyme, NAD+-linked malic enzyme
Enzyme Commission Primary Name for 18.104.22.168: malate dehydrogenase (decarboxylating)
Enzyme Commission Synonyms for 22.214.171.124: 'malic' enzyme, pyruvic-malic carboxylase, NAD-specific malic enzyme, NAD-malic enzyme
A reaction of the gluconeogenesis pathway.
Enzyme Commission Summary for 126.96.36.199:
There are several forms of malate dehydrogenases that differ by their use of substrate and cofactors. This NAD+-dependent enzyme can also decarboxylate both (S)-malate and oxaloacetate. cf. EC 188.8.131.52, malate dehydrogenase, EC 184.108.40.206, malate dehydrogenase (decarboxylating); and EC 220.127.116.11, malate dehydrogenase (oxaloacetate-decarboxylating) (NADP+).
Enzyme Commission Summary for 18.104.22.168:
There are several forms of malate dehydrogenases that differ by their use of substrate and cofactors. Unlike EC 22.214.171.124, this NAD+-dependent enzyme can not decarboxylate added oxaloacetate. cf. EC 126.96.36.199, malate dehydrogenase; EC 188.8.131.52, malate dehydrogenase (oxaloacetate-decarboxylating); and EC 184.108.40.206, D-malate dehydrogenase (decarboxylating).
KAUFMAN51: KAUFMAN S, KORKES S, DEL CAMPILLO A (1951). "Biosynthesis of dicarboxylic acids by carbon dioxide fixation. V. Further study of the "malic" enzyme of Lactobacillus arabinosus." J Biol Chem 192(1);301-12. PMID: 14917678
Yamaguchi79: Yamaguchi M (1979). "Studies on regulatory functions of malic enzymes. IV. Effects of sulfhydryl group modification on the catalytic function of NAD-linked malic enzyme from Escherichia coli." J Biochem (Tokyo) 86(2);325-33. PMID: 225306
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