Met-X dipeptidase

Met-Xaa dipeptidase (EC 3.4.13.12, methionyl dipeptidase, dipeptidase M) is an enzyme.^[1] This enzyme catalyses the following chemical reaction

This Mn²⁺-activated Escherichia coli enzyme with thiol dependence

References

↑ Brown, J.L. (1973). "Purification and properties of dipeptidase M from Escherichia coli B". J. Biol. Chem. 248: 409–416. PMID 4567782.

Met-Xaa dipeptidase at the US National Library of Medicine Medical Subject Headings (MeSH)

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

3.4.99: Unknown

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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