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
The enzyme appears in viruses and cellular organisms
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
Synonyms endopeptidase i, gamma-d-glutamyl-meso-diaminopimelate endopeptidase, more
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REACTION
REACTION DIAGRAM
COMMENTARY
ORGANISM
UNIPROT
LITERATURE
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
Substrates: hydrolysis of substrates containing D-Glu-meso-diaminopimelic-acid with free omega-NH2 and omega-COOH groups, the presence or absence of an alpha-amide group on glutamic acid, the second residue of peptides, has no influence on the specificity. N-Substitution of N-terminal L-Ala does not modify the enzymic specificity. An amide group on glutamic acid gives an decrease of 80% of activity Products: -
Substrates: hydrolysis of substrates containing D-Glu-meso-diaminopimelic-acid with free omega-NH2 and omega-COOH groups, the presence or absence of an alpha-amide group on glutamic acid, the second residue of peptides, has no influence on the specificity. N-Substitution of N-terminal L-Ala does not modify the enzymic specificity. An amide group on glutamic acid gives an decrease of 80% of activity Products: -
Characterization of the sporulation-related gamma-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
Garnier, M.; Vacheron, M.J.; Guinand, M.; Michel, G.
Purification and partial characterization of the extracellular gamma-D-glutamyl-(L)meso-diaminopimelate endopeptidase I, from Bacillus sphaericus NCTC 9602
Morel, P.; Guinand, M.; Vacheron, M.J.; Michel, G.
Biologically active glycopeptides from Actinomadura R 39. II. Continuous preparation of glycodipeptides with immobilized endopeptidase I from Bacillus sphaericus NCTC 9602
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