EC 126.96.36.199 - γ-D-glutamyl-meso-diaminopimelate peptidase
IntEnz Enzyme Nomenclature
γ-D-glutamyl-meso-diaminopimelic peptidoglycan hydrolase
γ-D-glutamyl-L-meso-diaminopimelate peptidoglycan hydrolase
- 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.
A 45-kDa metallopeptidase from Bacillus sphaericus, the substrates being components of the bacterial spore wall. A member of peptidase family M14 (carboxypeptidase A family). Endopeptidase II has similar activity, but differs in cellular location, molecular mass and catalytic mechanism .
Links to other databases
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 (1977). [PMID: 849747]
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 (1985). [PMID: 3922755]
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 (1993). [PMID: 8503890]
[EC 188.8.131.52 created 1996]