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Peptidoglycan glycosyltransferase

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(Redirected from EC 2.4.1.129)
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

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]

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

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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

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As of late 2007, 3 structures have been solved for this class of enzymes, with PDB accession codes 2BG1, 2UWX, and 2UWY.

References

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  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. Bibcode:2007PNAS..104.5348Y. 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.