IntEnz

EC 3.4.19.11 - γ-D-glutamyl-meso-diaminopimelate peptidase

IntEnz Enzyme Nomenclature
EC 3.4.19.11

Names

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.

Comments:

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 [3].

Links to other databases

References

1. Arminjon, F., Guinand, M., Vacheron, M.-J. and Michel, G.
   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]
2. Garnier, M., Vacheron, M.-J., Guinard, M. and Michel, G.
   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]
3. Hourdou, M.-L., Guinand, M., Vacheron, M.-J., Michel, G., Denoroy, L., Duez, C., Englebert, S., Joris, B., Weber, G. and Ghuysen, J.-M.
   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 3.4.19.11 created 1996]