CATH Classification

Domain Context

CATH Clusters

Superfamily D-Ala-D-Ala carboxypeptidase, C-terminal domain
Functional Family

Enzyme Information

3.4.16.4
Serine-type D-Ala-D-Ala carboxypeptidase.
based on mapping to UniProt P44466
Preferential cleavage: (Ac)(2)-L-Lys-D-Ala-|-D-Ala. Also transpeptidation of peptidyl-alanyl moieties that are N-acyl substituents of D-alanine.
-!- A group of bacterial enzymes, membrane-bound. -!- Inhibited by beta-lactam antibiotics, which acylate the active site serine in the enzyme. -!- Distinct from EC 3.4.17.14. -!- Belongs to peptidase families S11, S12 and S13.

UniProtKB Entries (1)

P44466
DACA_HAEIN
Haemophilus influenzae Rd KW20
D-alanyl-D-alanine carboxypeptidase DacA

PDB Structure

PDB 3A3J
External Links
Method X-RAY DIFFRACTION
Organism
Primary Citation
Crystal structures of penicillin-binding proteins 4 and 5 from Haemophilus influenzae
Kawai, F., Clarke, T.B., Roper, D.I., Han, G.-J., Hwang, K.Y., Unzai, S., Obayashi, E., Park, S.-Y., Tame, J.R.H.
J.Mol.Biol.
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