Phospho-N-acetylmuramoyl-pentapeptide-transferase
| phospho-N-acetylmuramoyl-pentapeptide-transferase | |||||||||
|---|---|---|---|---|---|---|---|---|---|
| Identifiers | |||||||||
| EC no. | 2.7.8.13 | ||||||||
| CAS no. | 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 | ||||||||
| |||||||||
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 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 translocase I,[2] 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
- ^ Ma Y, Münch D, Schneider T, Sahl HG, Bouhss A, Ghoshdastider U, Wang J, Dötsch V, Wang X, Bernhard F (November 2011). "Preparative scale cell-free production and quality optimization of MraY homologues in different expression modes". The Journal of Biological Chemistry. 286 (45): 38844–53. doi:10.1074/jbc.M111.301085. PMC 3234709. PMID 21937437.
- ^ Shiraishi, Taro; Kuzuyama, Tomohisa (2019). "Recent advances in the biosynthesis of nucleoside antibiotics". The Journal of Antibiotics. 72 (12): 913–923. doi:10.1038/s41429-019-0236-2. ISSN 1881-1469.
Further reading
- Heydanek MG, Neuhaus FC (April 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 (June 1967). "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. Bibcode:1967PNAS...57.1878H. doi:10.1073/pnas.57.6.1878. PMC 224560. PMID 5231417.
- Struve WG, Sinha RK, Neuhaus FC (January 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 (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.
