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3.4.17.8: muramoylpentapeptide carboxypeptidase

This is an abbreviated version!
For detailed information about muramoylpentapeptide carboxypeptidase, go to the full flat file.

Word Map on EC 3.4.17.8

Reaction

cleavage of the bond UDP-N-acetylmuramoyl-L-alanyl-D-gamma-glutamyl-6-carboxy-L-lysyl-D-alanyl-/-D-alanine =

Synonyms

carboxypeptidase D-alanyl-D-alanine, carboxypeptidase I, carboxypeptidase, muramoylpentapeptide, D-alanine carboxypeptidase, D-alanine carboxypeptidase I, D-alanine-D-alanine-carboxypeptidase, D-alanyl-D-alanine carboxypeptidase, D-alanyl-D-alanine peptidase, DacC, DD-Carboxypeptidase, DD-CPase, DD-peptidase, EC 3.4.12.6, Metallo DD-peptidase, msmeg_2432, msmeg_2433, PBP 5, PBP5, PdcA, penicillin binding protein 5, penicillin-binding protein 5, UDP-N-acetylmuramoyl-tetrapeptidyl-D-alanine alanine-hydrolase, VanX, VanXYc, VanY, Zn DD-peptidase

ECTree

     3 Hydrolases
         3.4 Acting on peptide bonds (peptidases)
             3.4.17 Metallocarboxypeptidases
                3.4.17.8 muramoylpentapeptide carboxypeptidase

Crystallization

Crystallization on EC 3.4.17.8 - muramoylpentapeptide carboxypeptidase

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CRYSTALLIZATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
modeling of structure
crystal structure of recombinant protein, with deletion off the C-terminal anchor, at a 2.05 A resolution. Structure contains a shortened loop spanning residues 74 to 78 near the active site and two active-site residues, Ser101 and Lys203. An active-site flexibility may explain its carbapenemase activity