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discounted EARLY registration ends Dec 31, 2014
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Metabolic Modeling Tutorial
discounted EARLY registration ends Dec 31, 2014
BioCyc websites down
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Metabolic Modeling Tutorial
discounted EARLY registration ends Dec 31, 2014
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Metabolic Modeling Tutorial
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Escherichia coli K-12 substr. MG1655 Reaction: 1.1.1.38/1.1.1.39

Superclasses: Reactions Classified By Conversion Type Simple Reactions Chemical Reactions
Reactions Classified By Substrate Small-Molecule Reactions

EC Number: 1.1.1.38 , 1.1.1.39

Enzymes and Genes:
malate dehydrogenase, NAD-requiring Inferred from experiment : maeA

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 1.1.1.38: malate dehydrogenase (oxaloacetate-decarboxylating)

Enzyme Commission Synonyms for 1.1.1.38: 'malic' enzyme (ambiguous), pyruvic-malic carboxylase (ambiguous), NAD+-specific malic enzyme, NAD+-malic enzyme, NAD+-linked malic enzyme

Enzyme Commission Primary Name for 1.1.1.39: malate dehydrogenase (decarboxylating)

Enzyme Commission Synonyms for 1.1.1.39: 'malic' enzyme, pyruvic-malic carboxylase, NAD-specific malic enzyme, NAD-malic enzyme

Summary:
A reaction of the gluconeogenesis pathway.

Enzyme Commission Summary for 1.1.1.38:
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 1.1.1.37, malate dehydrogenase, EC 1.1.1.39, malate dehydrogenase (decarboxylating); and EC 1.1.1.40, malate dehydrogenase (oxaloacetate-decarboxylating) (NADP+).

Enzyme Commission Summary for 1.1.1.39:
There are several forms of malate dehydrogenases that differ by their use of substrate and cofactors. Unlike EC 1.1.1.38, this NAD+-dependent enzyme can not decarboxylate added oxaloacetate. cf. EC 1.1.1.37, malate dehydrogenase; EC 1.1.1.38, malate dehydrogenase (oxaloacetate-decarboxylating); and EC 1.1.1.83, D-malate dehydrogenase (decarboxylating).

Citations: [KAUFMAN51, Yamaguchi79, Saz57]

Gene-Reaction Schematic: ?

Relationship Links: BRENDA:EC:1.1.1.38 , BRENDA:EC:1.1.1.39 , ENZYME:EC:1.1.1.38 , ENZYME:EC:1.1.1.39 , IUBMB-ExplorEnz:EC:1.1.1.38 , IUBMB-ExplorEnz:EC:1.1.1.39


References

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

Saz57: Saz HJ, Hubbard JA (1957). "The oxidative decarboxylation of malate by Ascaris lumbricoides." J Biol Chem 225(2);921-33. PMID: 13416294

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


Report Errors or Provide Feedback
Please cite the following article in publications resulting from the use of EcoCyc: Nucleic Acids Research 41:D605-12 2013
Page generated by SRI International Pathway Tools version 18.5 on Sat Dec 20, 2014, BIOCYC14A.