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: 3.4.11.21

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

EC Number: 3.4.11.21

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: Undetermined; a substrate lacks a chemical formula

Enzyme Commission Primary Name: aspartyl aminopeptidase

Enzyme Commission Summary:
Release of an N-terminal aspartate or glutamate from a peptide, with a preference for aspartate. Aminoacyl-arylamides are poor substrates. This is an abundant cytosolic enzyme in mammalian cells, in peptidase family M18 of aminopeptidase I

Citations: [Kelly83, Wilk98]

Relationship Links: BRENDA:EC:3.4.11.21 , ENZYME:EC:3.4.11.21 , IUBMB-ExplorEnz:EC:3.4.11.21


References

Kelly83: Kelly JA, Neidle EL, Neidle A (1983). "An aminopeptidase from mouse brain cytosol that cleaves N-terminal acidic amino acid residues." J Neurochem 40(6);1727-34. PMID: 6854330

Wilk98: Wilk S, Wilk E, Magnusson RP (1998). "Purification, characterization, and cloning of a cytosolic aspartyl aminopeptidase." J Biol Chem 273(26);15961-70. PMID: 9632644


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 Sun Nov 23, 2014, BIOCYC14A.