MetaCyc Reaction:

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

EC Number:

Enzymes and Genes:

Escherichia coli K-12 substr. MG1655: methionine aminopeptidaseInferred from experiment: map

The direction shown, i.e. which substrates are on the left and right sides, is in accordance with the direction in which it was curated.

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: methionyl aminopeptidase

Enzyme Commission Synonyms: methionine aminopeptidase, peptidase M, L-methionine aminopeptidase, MAP

Taxonomic Range: Metazoa, Viridiplantae, Bacteria , Fungi, Archaea

Standard Gibbs Free Energy (ΔrG in kcal/mol): 95.1682Inferred by computational analysis [Latendresse13]

Enzyme Commission Summary:
This enzyme catalyzes release of N-terminal amino acids, preferentially methionine, from peptides and arylamides.

Membrane-bound enzyme present in both prokaryotes and eukaryotes. Type example of peptidase family M24. Releases methionine from nascent peptides.

Citations: [1, Freitas85, Yoshida72 , Tsunasawa85, BenBassat87]

Gene-Reaction Schematic

Gene-Reaction Schematic

Relationship Links: BRENDA:EC:, ENZYME:EC:, IUBMB-ExplorEnz:EC:, UniProt:RELATED-TO:P0A1X6, UniProt:RELATED-TO:P0AE18, UniProt:RELATED-TO:P19994, UniProt:RELATED-TO:P22624, UniProt:RELATED-TO:P28617, UniProt:RELATED-TO:P38062, UniProt:RELATED-TO:P41392, UniProt:RELATED-TO:P44421, UniProt:RELATED-TO:P47418, UniProt:RELATED-TO:P50579, UniProt:RELATED-TO:P53579, UniProt:RELATED-TO:P53580, UniProt:RELATED-TO:P53581, UniProt:RELATED-TO:P56218, UniProt:RELATED-TO:P95963, UniProt:RELATED-TO:Q9FV49, UniProt:RELATED-TO:Q9JWK1, UniProt:RELATED-TO:Q9PM25, UniProt:RELATED-TO:Q9RKR2, UniProt:RELATED-TO:Q9UYT4, UniProt:RELATED-TO:Q9Z9J4, UniProt:RELATED-TO:Q01662, UniProt:RELATED-TO:Q58725, UniProt:RELATED-TO:Q59509


BenBassat87: Ben-Bassat A, Bauer K, Chang SY, Myambo K, Boosman A, Chang S (1987). "Processing of the initiation methionine from proteins: properties of the Escherichia coli methionine aminopeptidase and its gene structure." J Bacteriol 169(2);751-7. PMID: 3027045

Freitas85: Freitas JO, Termignoni C, Guimaraes JA (1985). "Microsomal methionine aminopeptidase: properties of the detergent-solubilized enzyme." Int J Biochem 17(12);1285-91. PMID: 3937747

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

Tsunasawa85: Tsunasawa S, Stewart JW, Sherman F (1985). "Amino-terminal processing of mutant forms of yeast iso-1-cytochrome c. The specificities of methionine aminopeptidase and acetyltransferase." J Biol Chem 260(9);5382-91. PMID: 2985590

Yoshida72: Yoshida A, Lin M (1972). "NH 2 -terminal formylmethionine- and NH 2 -terminal methionine-cleaving enzymes in rabbits." J Biol Chem 247(3);952-7. PMID: 4110013

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
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