Phospho-N-acetylmuramoyl-pentapeptide-transferase
phospho-N-acetylmuramoyl-pentapeptide-transferase | |||||||||
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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 | ||||||||
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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
- ↑ 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 3234709. PMID 21937437.
- Heydanek MG Jr, Neuhaus FC; Neuhaus (1969). "The initial stage in peptidoglycan synthesis. IV. Solubilization of phospho-N-acetylmuramyl-pentapeptide translocase". Biochemistry. 8 (4): 1474–81. doi:10.1021/bi00832a024. PMID 5805290.
- Higashi Y, Strominger JL, Sweeley CC; Strominger; Sweeley (1967). "Structure of a lipid intermediate in cell wall peptidoglycan synthesis: a derivative of a C55 isoprenoid alcohol". Proc. Natl. Acad. Sci. U.S.A. 57 (6): 1878–84. Bibcode:1967PNAS...57.1878H. doi:10.1073/pnas.57.6.1878. PMC 224560. PMID 5231417.
- Struve WG, Sinha RK, Neuhaus FC; Sinha; Neuhaus (1966). "On the initial stage in peptidoglycan synthesis Phospho-N-acetylmuramyl-pentapeptide translocase (uridine monophosphate)". Biochemistry. 5 (1): 82–93. doi:10.1021/bi00865a012. PMID 5938956.
- van Heijenoort J (2001). "Recent advances in the formation of the bacterial peptidoglycan monomer unit". Nat. Prod. Rep. 18 (5): 503–19. doi:10.1039/a804532a. PMID 11699883.