Phospho-N-acetylmuramoyl-pentapeptide-transferase

phospho-N-acetylmuramoyl-pentapeptide-transferase
Identifiers
EC number 2.7.8.13
CAS number 9068-50-2
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 / EGO

In enzymology, a phospho-N-acetylmuramoyl-pentapeptide-transferase (EC 2.7.8.13) is an enzyme that catalyzes the chemical reaction

UDP-Mur2Ac(oyl-L-Ala-gamma-D-Glu-L-Lys-D-Ala-D-Ala) + undecaprenyl phosphate UMP + Mur2Ac(oyl-L-Ala-gamma-D-Glu-L-Lys-D-Ala-D-Ala)- diphosphoundecaprenol

Thus, the two substrates of this enzyme are UDP-Mur2Ac(oyl-L-Ala-gamma-D-Glu-L-Lys-D-Ala-D-Ala) and undecaprenyl phosphate, whereas its 3 products are UMP, Mur2Ac(oyl-L-Ala-gamma-D-Glu-L-Lys-D-Ala-D-Ala)-, and diphosphoundecaprenol.

This enzyme belongs to the family of transferases, specifically those transferring non-standard substituted phosphate groups. The systematic name of this enzyme class is UDP-MurAc(oyl-L-Ala-gamma-D-Glu-L-Lys-D-Ala-D-Ala):undecaprenyl-phos phate phospho-N-acetylmuramoyl-pentapeptide-transferase. Other names in common use include MraY transferase, UDP-MurNAc-L-Ala-D-gamma-Glu-L-Lys-D-Ala-D-Ala:C55-isoprenoid, alcohol transferase, UDP-MurNAc-Ala-gammaDGlu-Lys-DAla-DAla:undecaprenylphosphate, transferase, phospho-N-acetylmuramoyl pentapeptide translocase, phospho-MurNAc-pentapeptide transferase, phospho-NAc-muramoyl-pentapeptide translocase (UMP), phosphoacetylmuramoylpentapeptide translocase, and phosphoacetylmuramoylpentapeptidetransferase. This enzyme participates in peptidoglycan biosynthesis. It can be expressed efficiently by cell-free protein expression system.[1]

References

  1. Ma, Y; Münch, D; Schneider, T; Sahl, H. G.; Bouhss, A; Ghoshdastider, U; Wang, J; Dötsch, V; Wang, X; Bernhard, F (2011). "Preparative scale cell-free production and quality optimization of MraY homologues in different expression modes". Journal of Biological Chemistry. 286 (45): 38844–53. doi:10.1074/jbc.M111.301085. PMC 3234709Freely accessible. PMID 21937437.
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