Metabolic Modeling Tutorial
discounted EARLY registration ends Dec 31, 2014
Metabolic Modeling Tutorial
discounted EARLY registration ends Dec 31, 2014
Metabolic Modeling Tutorial
discounted EARLY registration ends Dec 31, 2014
Metabolic Modeling Tutorial
discounted EARLY registration ends Dec 31, 2014
Metabolic Modeling Tutorial
discounted EARLY registration ends Dec 31, 2014
twitter

MetaCyc Reaction: 1.4.1.21

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

EC Number: 1.4.1.21

The reaction direction shown, that is, A + B ↔ C + D versus C + D ↔ A + B, is in accordance with the Enzyme Commission system.

Most BioCyc compounds have been protonated to a reference pH value of 7.3, and some reactions have been computationally balanced for hydrogen by adding free protons. 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

Standard Gibbs Free Energy (ΔrG in kcal/mol): -3.2305908 Inferred 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, Yang03]

Unification Links: KEGG:R07165

Relationship Links: BRENDA:EC:1.4.1.21 , ENZYME:EC:1.4.1.21 , IUBMB-ExplorEnz:EC:1.4.1.21 , Rhea:RELATED-TO:11787 , Rhea:RELATED-TO:11791


References

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

Yang03: 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


Report Errors or Provide Feedback
Please cite the following article in publications resulting from the use of MetaCyc: Caspi et al, Nucleic Acids Research 42:D459-D471 2014
Page generated by SRI International Pathway Tools version 18.5 on Thu Dec 18, 2014, BIOCYC13A.