CATH Classification
| Level | CATH Code | Description |
|---|---|---|
|
1 | Mainly Alpha |
|
1.10 | Orthogonal Bundle |
|
1.10.3810 | Penicillin binding protein transpeptidase fold |
|
1.10.3810.10 | Biosynthetic peptidoglycan transglycosylase-like |
Domain Context
CATH Clusters
| Superfamily | Biosynthetic peptidoglycan transglycosylase-like |
| Functional Family | Penicillin-binding protein 1a |
Enzyme Information
| 3.4.16.4 |
Serine-type D-Ala-D-Ala carboxypeptidase.
based on mapping to UniProt O66874
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 O66874
(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)
| O66874 |
PBPA_AQUAE
Aquifex aeolicus VF5
Penicillin-binding protein 1A
|
PDB Structure
| PDB | 2OQO |
| External Links | |
| Method | X-RAY DIFFRACTION |
| Organism | Escherichia |
| Primary Citation |
Crystal structure of a peptidoglycan glycosyltransferase suggests a model for processive glycan chain synthesis.
Proc.Natl.Acad.Sci.Usa
|