Metabolic Modeling Tutorial
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BioCyc websites down
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Metabolic Modeling Tutorial
discounted EARLY registration ends Dec 31, 2014
BioCyc websites down
12/28 - 12/31
for maintenance.
Metabolic Modeling Tutorial
discounted EARLY registration ends Dec 31, 2014
BioCyc websites down
12/28 - 12/31
for maintenance.
Metabolic Modeling Tutorial
discounted EARLY registration ends Dec 31, 2014
BioCyc websites down
12/28 - 12/31
for maintenance.
Metabolic Modeling Tutorial
discounted EARLY registration ends Dec 31, 2014
BioCyc websites down
12/28 - 12/31
for maintenance.
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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 Sun Dec 21, 2014, BIOCYC14A.