Undecaprenyldiphospho-muramoylpentapeptide beta-N-acetylglucosaminyltransferase
| undecaprenyldiphospho-muramoylpentapeptide beta-N-acetylglucosaminyltransferase | |||||||||
|---|---|---|---|---|---|---|---|---|---|
| Identifiers | |||||||||
| EC no. | 2.4.1.227 | ||||||||
| CAS no. | 60976-26-3 | ||||||||
| 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, an undecaprenyldiphospho-muramoylpentapeptide beta-N-acetylglucosaminyltransferase (EC 2.4.1.227) is an enzyme that catalyzes the chemical reaction
- UDP-N-acetylglucosamine + Mur2Ac(oyl-L-Ala-gamma-D-Glu-L-Lys-D-Ala-D-Ala)-diphosphoundecaprenol UDP + GlcNAc-(1->4)-Mur2Ac(oyl-L-Ala-gamma-D-Glu-L-Lys-D-Ala-D-Ala)-diphosphoundecaprenol
The 2 substrates of this enzyme are UDP-N-acetylglucosamine and Mur2Ac(oyl-L-Ala-gamma-D-Glu-L-Lys-D-Ala-D-Ala)-diphosphoundecaprenol, whereas its 2 products are UDP and Lipid II.
This enzyme belongs to the family of glycosyltransferases, specifically the hexosyltransferases. The systematic name of this enzyme class is UDP-N-acetyl-D-glucosamine:N-acetyl-alpha-D-muramyl(oyl-L-Ala-gamma- D-Glu-L-Lys-D-Ala-D-Ala)-diphosphoundecaprenol beta-1,4-N-acetylglucosaminlytransferase. Another name in common use is MurG transferase. This enzyme participates in peptidoglycan biosynthesis.
Variant reactions producing modified cell walls include (not muturally exclusive):
- Replacement of lysine residue with meso-diaminopimelate combined with adjacent residues through its L-centre, as it is in Gram-negative and some Gram-positive organisms.[1]
- Use of mono-trans,octa-cis-decaprenyl instead of the conventional di-trans,octa-cis-undecaprenol moiety, as found in Mycobacterium.[2]
References
- ^ "MetaCyc EC 2.4.1.227". biocyc.org.
- ^ "MetaCyc EC 2.4.1.227". biocyc.org.
- van Heijenoort J (October 2001). "Recent advances in the formation of the bacterial peptidoglycan monomer unit". Natural Product Reports. 18 (5): 503–19. doi:10.1039/a804532a. PMID 11699883.
