CATH Classification
Level | CATH Code | Description |
---|---|---|
2 | Mainly Beta | |
2.60 | Sandwich | |
2.60.410 | Peptidoglycan synthesis regulatory factor (PBP3), Domain 2 | |
2.60.410.10 | D-Ala-D-Ala carboxypeptidase, C-terminal domain |
Domain Context
CATH Clusters
Superfamily | D-Ala-D-Ala carboxypeptidase, C-terminal domain |
Functional Family | D-alanyl-D-alanine carboxypeptidase dacA |
Enzyme Information
3.4.16.4 |
Serine-type D-Ala-D-Ala carboxypeptidase.
based on mapping to UniProt P0AEB2
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.
|
3.5.2.6 |
Beta-lactamase.
based on mapping to UniProt P0AEB2
A beta-lactam + H(2)O = a substituted beta-amino acid.
-!- Zinc is only requires in class-B enzymes. -!- A group of enzymes of varying specificity hydrolyzing beta-lactams; some act more rapidly on penicillins, some more rapidly on cephalosporins. -!- Formerly EC 3.5.2.8.
|
UniProtKB Entries (1)
P0AEB2 |
DACA_ECOLI
Escherichia coli K-12
D-alanyl-D-alanine carboxypeptidase DacA
|
PDB Structure
PDB | 3MZD |
External Links | |
Method | X-RAY DIFFRACTION |
Organism | |
Primary Citation |
Crystal structures of covalent complexes of beta-lactam antibiotics with Escherichia coli penicillin-binding protein 5: toward an understanding of antibiotic specificity
Biochemistry
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