Metabolic Modeling Tutorial
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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: 3.4.11.18

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

EC Number: 3.4.11.18

Enzymes and Genes:
methionine aminopeptidase Inferred from experiment : map ( Escherichia coli K-12 substr. MG1655 )

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: methionyl aminopeptidase

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

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: ?

Relationship Links: BRENDA:EC:3.4.11.18 , ENZYME:EC:3.4.11.18 , IUBMB-ExplorEnz:EC:3.4.11.18 , 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


References

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

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
Page generated by SRI International Pathway Tools version 18.5 on Tue Nov 25, 2014, BIOCYC13A.