MetaCyc Reaction:

Superclasses: Reactions Classified By Conversion TypeSimple ReactionsChemical Reactions
Reactions Classified By SubstrateSmall-Molecule Reactions

EC Number:

The direction shown, i.e. which substrates are on the left and right sides, is in accordance with the Enzyme Commission system.

Most BioCyc compounds have been protonated to a reference pH value of 7.3. Please see the PGDB Concepts Guide for more information.

Mass balance status: Balanced.

Enzyme Commission Primary Name: aspartate dehydrogenase

Enzyme Commission Synonyms: NAD-dependent aspartate dehydrogenase, NADH2-dependent aspartate dehydrogenase, NADP+-dependent aspartate dehydrogenase

Taxonomic Range: Metazoa, Bacteria , Archaea

Standard Gibbs Free Energy (ΔrG in kcal/mol): -3.2305908Inferred by computational analysis [Latendresse13]

Enzyme Commission Summary:
Catalyzes the first step in NAD biosynthesis from aspartate. Strictly specific for L-aspartate as substrate. Has a higher affinity for NAD(+) than NADP(+).

Citations: [Okamura98, Yang03a]

Unification Links: KEGG:R07165

Relationship Links: BRENDA:EC:, ENZYME:EC:, IUBMB-ExplorEnz:EC:, Rhea:RELATED-TO:11787, Rhea:RELATED-TO:11791


Latendresse13: Latendresse M. (2013). "Computing Gibbs Free Energy of Compounds and Reactions in MetaCyc."

Okamura98: Okamura T, Noda H, Fukuda S, Ohsugi M (1998). "Aspartate dehydrogenase in vitamin B12-producing Klebsiella pneumoniae IFO 13541." J Nutr Sci Vitaminol (Tokyo) 44(4);483-90. PMID: 9819709

Yang03a: Yang Z, Savchenko A, Yakunin A, Zhang R, Edwards A, Arrowsmith C, Tong L (2003). "Aspartate dehydrogenase, a novel enzyme identified from structural and functional studies of TM1643." J Biol Chem 278(10);8804-8. PMID: 12496312

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Please cite the following article in publications resulting from the use of MetaCyc: Caspi et al, Nucleic Acids Research 42:D459-D471 2014
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