Peptidoglycan glycosyltransferase

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
IntEnzIntEnz view
BRENDABRENDA entry
ExPASyNiceZyme view
KEGGKEGG entry
MetaCycmetabolic pathway
PRIAMprofile
PDB structuresRCSB PDB PDBe PDBsum
Gene OntologyAmiGO / QuickGO
Search
PMCarticles
PubMedarticles
NCBIproteins

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

Peptidoglycan 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

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

  1. 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.
  2. 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. doi:10.1073/pnas.0701160104. PMC 1817829. PMID 17360321.
  3. "Information on EC 2.4.1.129 - peptidoglycan glycosyltransferase - BRENDA Enzyme Database". www.brenda-enzymes.org. Retrieved 2022-05-13.


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