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 | |||||||||
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 | ||||||||
|
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 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.
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
- Mesleh, Michael F.; Rajaratnam, Premraj; Conrad, Mary; Chandrasekaran, Vasu; Liu, Christopher M.; Pandya, Bhaumik A.; Hwang, You Seok; Rye, Peter T.; Muldoon, Craig; Becker, Bernd; Zuegg, Johannes (11 September 2015). "Targeting Bacterial Cell Wall Peptidoglycan Synthesis by Inhibition of Glycosyltransferase Activity". Chemical Biology & Drug Design. 87 (2): 190–199. doi:10.1111/cbdd.12662. ISSN 1747-0285. PMID 26358369.
- 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. doi:10.1128/MMBR.62.4.1079-1093.1998. 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.