Gamma-D-Glutamyl-meso-diaminopimelate peptidase

Gamma-D-glutamyl-meso-diaminopimelate peptidase (EC 3.4.19.11, endopeptidase I, gamma-D-glutamyldiaminopimelate endopeptidase, gamma-D-glutamyl-L-meso-diaminopimelate peptidoglycan hydrolase, gamma-glutamyl-L-meso-diaminopimelyl endopeptidase, gamma-D-glutamyl-meso-diaminopimelate endopeptidase, gamma-D-glutamyl-meso-diaminopimelic peptidoglycan hydrolase, gamma-D-glutamyl-meso-diaminopimelic endopeptidase, gamma-D-glutamyl-meso-D-aminopimelic endopeptidase) is an enzyme.^[1]^[2]^[3] This enzyme catalyses the following chemical reaction

Hydrolysis of gamma-D-glutamyl bonds to the L-terminus (position 7) of meso-diaminopimelic acid (meso-A2pm) in 7-(L-Ala-gamma-D-Glu)-meso-A2pm and 7-(L-Ala-gamma-D-Glu)-7-(D-Ala)-meso-A2pm. It is required that the D-terminal amino and carboxy groups of meso-A2pm are unsubstituted

This metallopeptidase is isolate from Bacillus sphaericus.

References

↑ Arminjon, F.; Guinand, M.; Vacheron, M.-J.; Michel, G. (1977). "Specificity profiles of the membrane-bound γ-D-glutamyl-(L)meso-diaminopimelate endopeptidase and LD-carboxypeptidase from Bacillus sphaericus 9602". Eur. J. Biochem. 73: 557–565. doi:10.1111/j.1432-1033.1977.tb11351.x. PMID 849747.
↑ Garnier, M.; Vacheron, M.-J.; Guinard, M.; Michel, G. (1985). "Purification and partial characterization of the extracellular γ-D-glutamyl-(L)meso-diaminopimelate endopeptidase I, from Bacillus sphaericus NCTC 9602". Eur. J. Biochem. 148: 539–543. doi:10.1111/j.1432-1033.1985.tb08873.x. PMID 3922755.
↑ Hourdou, M.-L.; Guinand, M.; Vacheron, M.-J.; Michel, G.; Denoroy, L.; Duez, C.; Englebert, S.; Joris, B.; Weber, G.; Ghuysen, J.-M. (1993). "Characterization of the sporulation-related γ-D-glutamyl-(L)meso-diaminopimelic-acid-hydrolysing peptidase I of Bacillus sphaericus NCTC 9602 as a member of the metallo(zinc) carboxypeptidase A family. Modular design of the protein". Biochem. J. 292: 563–570. PMID 8503890.

External links

Gamma-D-glutamyl-meso-diaminopimelate peptidase 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

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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