Peptidoglycan glycosyltransferase (EC 2.4.1.129) is an enzyme used in the biosynthesis of peptidoglycan. It transfers a disaccharide-peptide from a donor substrate to synthesize a glycan chain.[1]
| 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 | ||||||||
| |||||||||
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.
Function
editPeptidoglycan glycosyltransferase couples Lipid II subunits to synthesize the peptidoglycan chains. Transpeptidases crosslink the carbohydrate chains to provide the framework for the cell wall.[2]
It 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 2 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)-diphosphoundecaprenol,
whereas its 2 products are
- [GlcNAc-(1->4)-Mur2Ac(oyl-L-Ala-gamma-D-Glu-L-Lys-D-Ala-D-Ala)]n+1-diphosphoundecaprenol, and
- undecaprenyl diphosphate.[3]
Structural studies
editAs of late 2007, 3 structures have been solved for this class of enzymes, with PDB accession codes 2BG1, 2UWX, and 2UWY.
References
edit- ^ Mesleh MF, Rajaratnam P, Conrad M, Chandrasekaran V, Liu CM, Pandya BA, et al. (February 2016). "Targeting Bacterial Cell Wall Peptidoglycan Synthesis by Inhibition of Glycosyltransferase Activity". Chemical Biology & Drug Design. 87 (2): 190–199. doi:10.1111/cbdd.12662. PMID 26358369.
- ^ Yuan Y, Barrett D, Zhang Y, Kahne D, Sliz P, Walker S (March 2007). "Crystal structure of a peptidoglycan glycosyltransferase suggests a model for processive glycan chain synthesis". Proceedings of the National Academy of Sciences of the United States of America. 104 (13): 5348–5353. Bibcode:2007PNAS..104.5348Y. doi:10.1073/pnas.0701160104. PMC 1817829. PMID 17360321.
- ^ "Information on EC 2.4.1.129 - peptidoglycan glycosyltransferase - BRENDA Enzyme Database". www.brenda-enzymes.org. Retrieved 2022-05-13.
