Methionyl aminopeptidase

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Methionyl aminopeptidase (EC 3.4.11.18, methionine aminopeptidase, peptidase M, L-methionine aminopeptidase, MAP) is an enzyme.^[1]^[2]^[3]^[4]^[5] This enzyme catalyses the following chemical reaction

Release of N-terminal amino acids, preferentially methionine, from peptides and arylamides

This membrane-bound enzyme is present in both prokaryotes and eukaryotes.

References

↑ Yoshida A, Lin M (1972). "NH₂-terminal formylmethionine- and NH₂-terminal methionine-cleaving enzymes in rabbits". J. Biol. Chem. 247: 952–957. PMID 4110013.
↑ Tsunasawa S, Stewart JW, Sherman F (1985). "Acylamino acid-releasing enzyme from rat liver". J. Biol. Chem. 260: 5832–5391. PMID 2985590.
↑ Freitas JO, Termignoni C, Guimarães JA (1985). "Methionine aminopeptidase associated with liver mitochondria and microsomes". Int. J. Biochem. 17: 1285–1291. PMID 3937747.
↑ Ben-Bassat A, Bauer K, Chang SY, Myambo K, Boosman A, Chang S (1987). "Processing of the initiation methionine from proteins: properties of Escherichia coli methionine aminopeptidase and its gene structure". J. Bacteriol. 169: 751–757. PMID 3027045.
↑ Roderick SL, Matthews BW (1988). "Crystallization of methionine aminopeptidase from Escherichia coli". J. Biol. Chem. 263: 16531–16531. PMID 3141408.

External links

Methionyl aminopeptidase at the US National Library of Medicine Medical Subject Headings (MeSH)

Hydrolase: proteases (EC 3.4)

3.4.11-19: Exopeptidase

3.4.11	Aminopeptidase Alanine Arginyl Aspartyl Cystinyl Leucyl Glutamyl Methionyl 1 2 O

3.4.13	Dipeptidase 1 2 3

3.4.14	Dipeptidyl peptidase Cathepsin C Dipeptidyl peptidase-4 Tripeptidyl peptidase Tripeptidyl peptidase I Tripeptidyl peptidase II

3.4.15	Angiotensin-converting enzyme

3.4.16	Serine type carboxypeptidases: Cathepsin A DD-transpeptidase

3.4.17	Metalloexopeptidases Carboxypeptidase A A2 B C E Glutamate II

Other/ungrouped	Metalloexopeptidase

3.4.21-25: Endopeptidase

Other/ungrouped: Amyloid precursor protein secretase

3.4.99: Unknown

Staphylokinase

Proteins: enzymes

Activity	Active site Binding site Catalytic triad Oxyanion hole Enzyme promiscuity Catalytically perfect enzyme Coenzyme Cofactor Enzyme catalysis Enzyme kinetics Lineweaver–Burk plot Michaelis–Menten kinetics

Regulation	Allosteric regulation Cooperativity Enzyme inhibitor

Classification	EC number Enzyme superfamily Enzyme family List of enzymes

Types	EC1 Oxidoreductases(list) EC2 Transferases(list) EC3 Hydrolases(list) EC4 Lyases(list) EC5 Isomerases(list) EC6 Ligases(list)

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