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 | Penicillin-binding protein 1B |
Enzyme Information
| 3.4.16.4 |
Serine-type D-Ala-D-Ala carboxypeptidase.
based on mapping to UniProt P02919
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.
|
| 2.4.1.129 |
Peptidoglycan glycosyltransferase.
based on mapping to UniProt P02919
(GlcNAc-(1->4)-Mur2Ac(oyl-L-Ala-gamma-D-Glu-L-Lys-D-Ala-D-Ala))(n)- diphosphoundecaprenol + GlcNAc-(1->4)-Mur2Ac(oyl-L-Ala-gamma-D-Glu-L-Lys- D-Ala-D-Ala)-diphosphoundecaprenol = (GlcNAc-(1->4)-Mur2Ac(oyl-L-Ala- gamma-D-Glu-L-Lys-D-Ala-D-Ala))(n+1)-diphosphoundecaprenol + undecaprenyl diphosphate.
-!- The enzyme also works when the lysine residue is replaced by meso- 2,6-diaminoheptanedioate (meso-2,6-diaminopimelate, A2pm) combined with adjacent residues through its L-center, as it is in Gram- negative and some Gram-positive organisms. -!- The undecaprenol involved is ditrans,octacis-undecaprenol. -!- Involved in the synthesis of cell-wall peptidoglycan.
|
UniProtKB Entries (1)
| P02919 |
PBPB_ECOLI
Escherichia coli K-12
Penicillin-binding protein 1B
|
PDB Structure
| PDB | 3VMA |
| External Links | |
| Method | X-RAY DIFFRACTION |
| Organism | |
| Primary Citation |
Crystal structure of the membrane-bound bifunctional transglycosylase PBP1b from Escherichia coli.
Proc.Natl.Acad.Sci.USA
|
