Biology: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 / QuickGO | ||||||||
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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 [math]\displaystyle{ \rightleftharpoons }[/math] 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 2 products are UMP and Mur2Ac(oyl-L-Ala-gamma-D-Glu-L-Lys-D-Ala-D-Ala)-diphosphoundecaprenol.
This enzyme participates in peptidoglycan biosynthesis. It can be expressed efficiently by a cell-free protein expression system.[1]
Nomenclature
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-phosphate 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.
References
- ↑ "Preparative scale cell-free production and quality optimization of MraY homologues in different expression modes". The Journal of Biological Chemistry 286 (45): 38844–53. November 2011. doi:10.1074/jbc.M111.301085. PMID 21937437.
Further reading
- "The initial stage in peptidoglycan synthesis. IV. Solubilization of phospho-N-acetylmuramyl-pentapeptide translocase". Biochemistry 8 (4): 1474–81. April 1969. doi:10.1021/bi00832a024. PMID 5805290.
- "Structure of a lipid intermediate in cell wall peptidoglycan synthesis: a derivative of a C55 isoprenoid alcohol". Proceedings of the National Academy of Sciences of the United States of America 57 (6): 1878–84. June 1967. doi:10.1073/pnas.57.6.1878. PMID 5231417. Bibcode: 1967PNAS...57.1878H.
- "On the initial stage in peptidoglycan synthesis. Phospho-N-acetylmuramyl-pentapeptide translocase (uridine monophosphate)". Biochemistry 5 (1): 82–93. January 1966. doi:10.1021/bi00865a012. PMID 5938956.
- "Recent advances in the formation of the bacterial peptidoglycan monomer unit". Natural Product Reports 18 (5): 503–19. October 2001. doi:10.1039/a804532a. PMID 11699883.
![]() | Original source: https://en.wikipedia.org/wiki/Phospho-N-acetylmuramoyl-pentapeptide-transferase.
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