Peptidoglycan glycosyltransferase
| peptidoglycan glycosyltransferase | |||||||||
|---|---|---|---|---|---|---|---|---|---|
| Identifiers | |||||||||
| EC no. | 2.4.1.129 | ||||||||
| CAS no. | 79079-04-2 | ||||||||
| Databases | |||||||||
| IntEnz | IntEnz view | ||||||||
| BRENDA | BRENDA entry | ||||||||
| ExPASy | NiceZyme view | ||||||||
| KEGG | KEGG entry | ||||||||
| MetaCyc | metabolic pathway | ||||||||
| PRIAM | profile | ||||||||
| PDB structures | RCSB PDB PDBe PDBsum | ||||||||
| Gene Ontology | AmiGO / QuickGO | ||||||||
| |||||||||
In enzymology, a peptidoglycan glycosyltransferase (EC 2.4.1.129) is an enzyme that catalyzes the chemical reaction
- [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 4 substrates of this enzyme are
- [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)-, and
- diphosphoundecaprenol,
whereas its 3 products are
- [GlcNAc-(1->4)-Mur2Ac(oyl-L-Ala-gamma-D-Glu-L-Lys-D-Ala-D-Ala)]n+1-,
- diphosphoundecaprenol, and
- undecaprenyl diphosphate.
This enzyme belongs to the family of glycosyltransferases, specifically the hexosyltransferases. The systematic name of this enzyme class is undecaprenyldiphospho-(N-acetyl-D-glucosaminyl-(1->4)-(N-acetyl-D-mu ramoylpentapeptide):undecaprenyldiphospho-(N-acetyl-D-glucosaminyl-( 1->4)-N-acetyl-D-muramoylpentapeptide) disaccharidetransferase. Other names in common use include PG-II, bactoprenyldiphospho-N-acetylmuramoyl-(N-acetyl-D-glucosaminyl)-, pentapeptide:peptidoglycan, N-acetylmuramoyl-N-acetyl-D-glucosaminyltransferase, penicillin binding protein (3 or 1B), and peptidoglycan transglycosylase. This enzyme participates in peptidoglycan biosynthesis.
Structural studies
As of late 2007, 3 structures have been solved for this class of enzymes, with PDB accession codes 2BG1, 2UWX, and 2UWY.
References
- Taku A, Stuckey M, Fan DP (1982). "Purification of the peptidoglycan transglycosylase of Bacillus megaterium". J. Biol. Chem. 257 (9): 5018–22. PMID 6802846.
- Goffin C, Ghuysen JM (1998). "Multimodular penicillin-binding proteins: an enigmatic family of orthologs and paralogs". Microbiol. Mol. Biol. Rev. 62 (4): 1079–93. PMC 98940. PMID 9841666.
- van Heijenoort J (2001). "Formation of the glycan chains in the synthesis of bacterial peptidoglycan". Glycobiology. 11 (3): 25R–36R. doi:10.1093/glycob/11.3.25R. PMID 11320055.