Undecaprenyldiphospho-muramoylpentapeptide beta-N-acetylglucosaminyltransferase

(Redirected from EC 2.4.1.227)

In enzymology, an undecaprenyldiphospho-muramoylpentapeptide beta-N-acetylglucosaminyltransferase (EC 2.4.1.227) is an enzyme that catalyzes the chemical reaction

undecaprenyldiphospho-muramoylpentapeptide beta-N-acetylglucosaminyltransferase
Identifiers
EC no.2.4.1.227
CAS no.60976-26-3
Databases
IntEnzIntEnz view
BRENDABRENDA entry
ExPASyNiceZyme view
KEGGKEGG entry
MetaCycmetabolic pathway
PRIAMprofile
PDB structuresRCSB PDB PDBe PDBsum
Gene OntologyAmiGO / QuickGO
Search
PMCarticles
PubMedarticles
NCBIproteins
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

edit
  1. ^ "MetaCyc EC 2.4.1.227". biocyc.org.
  2. ^ "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.