CATH Classification
| Level | CATH Code | Description |
|---|---|---|
|
3 | Alpha Beta |
|
3.40 | 3-Layer(aba) Sandwich |
|
3.40.710 | Beta-lactamase |
|
3.40.710.10 | DD-peptidase/beta-lactamase superfamily |
Domain Context
CATH Clusters
| Superfamily | DD-peptidase/beta-lactamase superfamily |
| Functional Family | D-alanyl-D-alanine serine-type carboxypeptidase |
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 | 1Z6F |
| External Links | |
| Method | X-RAY DIFFRACTION |
| Organism | Escherichia |
| Primary Citation |
Crystal Structure of Escherichia coli Penicillin-Binding Protein 5 Bound to a Tripeptide Boronic Acid Inhibitor: A Role for Ser-110 in Deacylation.
Biochemistry
|
