Misplaced Pages

Phospho-N-acetylmuramoyl-pentapeptide-transferase

Article snapshot taken from Wikipedia with creative commons attribution-sharealike license. Give it a read and then ask your questions in the chat. We can research this topic together.
(Redirected from MraY)
phospho-N-acetylmuramoyl-pentapeptide-transferase
Identifiers
EC no.2.7.8.13
CAS no.9068-50-2
Databases
IntEnzIntEnz view
BRENDABRENDA entry
ExPASyNiceZyme view
KEGGKEGG entry
MetaCycmetabolic pathway
PRIAMprofile
PDB structuresRCSB PDB PDBe PDBsum
Gene OntologyAmiGO / QuickGO
Search
PMCarticles
PubMedarticles
NCBIproteins

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 {\displaystyle \rightleftharpoons } 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.

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, 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

  1. 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.
  2. 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

Transferases: phosphorus-containing groups (EC 2.7)
2.7.1-2.7.4:
phosphotransferase/kinase
(PO4)
2.7.1: OH acceptor
2.7.2: COOH acceptor
2.7.3: N acceptor
2.7.4: PO4 acceptor
2.7.6: diphosphotransferase
(P2O7)
2.7.7: nucleotidyltransferase
(PO4-nucleoside)
Polymerase
DNA polymerase
DNA-directed DNA polymerase
I/A
γ
θ
ν
T7
Taq
II/B
α
δ
ε
ζ
Pfu
III/C
IV/X
β
λ
μ
TDT
V/Y
η
ι
κ
RNA-directed DNA polymerase
Reverse transcriptase
Telomerase
RNA polymerase
Template-directed
RNA polymerase I
II
III
IV
V
ssRNAP
POLRMT
Primase
1
2
PrimPol
RNA-dependent RNA polymerase
Polyadenylation
PAP
PNPase
Phosphorolytic
3' to 5' exoribonuclease
Nucleotidyltransferase
Guanylyltransferase
Other
2.7.8: miscellaneous
Phosphatidyltransferases
Glycosyl-1-phosphotransferase
2.7.10-2.7.13: protein kinase
(PO4; protein acceptor)
2.7.10: protein-tyrosine
2.7.11: protein-serine/threonine
2.7.12: protein-dual-specificity
2.7.13: protein-histidine
Enzymes
Activity
Regulation
Classification
Kinetics
Types
Portal:


This EC 2.7 enzyme-related article is a stub. You can help Misplaced Pages by expanding it.

Categories: