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
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MetaCyc Reaction: 3.5.1.83

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

EC Number: 3.5.1.83

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: N-acyl-D-aspartate deacylase

Enzyme Commission Synonyms: N-acyl-D-aspartate amidohydrolase

Standard Gibbs Free Energy (ΔrG in kcal/mol): 41.245605 Inferred by computational analysis [Latendresse13]

Enzyme Commission Summary:
The enzyme from Alcaligenes xylosoxydans subsp. xylosoxydans is specific for N-acyl-D-aspartate. Requires zinc.

Citations: [Moriguchi93]

Unification Links: KEGG:R02182 , Rhea:18285

Relationship Links: BRENDA:EC:3.5.1.83 , ENZYME:EC:3.5.1.83 , IUBMB-ExplorEnz:EC:3.5.1.83


References

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

Moriguchi93: Moriguchi M, Sakai K, Katsuno Y, Maki T, Wakayama M (1993). "Purification and characterization of novel N-acyl-D-aspartate amidohydrolase from Alcaligenes xylosoxydans subsp. xylosoxydans A-6." Biosci Biotechnol Biochem 57(7);1145-8. PMID: 7763985


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 Nov 27, 2014, BIOCYC13A.