UDP-N-acetylmuramoyl-tripeptide—D-alanyl-D-alanine ligase

In enzymology, a UDP-N-acetylmuramoyl-tripeptide—D-alanyl-D-alanine ligase (EC 6.3.2.10) is an enzyme that catalyzes the chemical reaction

ATP + UDP-N-acetylmuramoyl-L-alanyl-gamma-D-glutamyl-L-lysine + D-alanyl-D-alanine ADP + phosphate + UDP-N-acetylmuramoyl-L-alanyl-gamma-D-glutamyl-L-lysyl-D-alanyl-D- alanine
UDP-N-acetylmuramoyl-tripeptide—D-alanyl-D-alanine ligase
Identifiers
EC no.6.3.2.10
CAS no.9023-60-3
Databases
IntEnzIntEnz view
BRENDABRENDA entry
ExPASyNiceZyme view
KEGGKEGG entry
MetaCycmetabolic pathway
PRIAMprofile
PDB structuresRCSB PDB PDBe PDBsum
Gene OntologyAmiGO / QuickGO
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PMCarticles
PubMedarticles
NCBIproteins

The 3 substrates of this enzyme are ATP, UDP-N-acetylmuramoyl-L-alanyl-gamma-D-glutamyl-L-lysine, and D-alanyl-D-alanine, whereas its 4 products are ADP, phosphate, UDP-N-acetylmuramoyl-L-alanyl-gamma-D-glutamyl-L-lysyl-D-alanyl-D-, and alanine.

This enzyme belongs to the family of ligases, specifically those forming carbon-nitrogen bonds as acid-D-amino-acid ligases (peptide synthases).

Nomenclature

The systematic name of this enzyme class is UDP-N-acetylmuramoyl-L-alanyl-D-glutamyl-L-lysine:D-alanyl-D-alanine ligase (ADP-forming). Other names in common use include MurF synthetase, UDP-N-acetylmuramoyl-L-alanyl-D-glutamyl-L-lysyl-D-alanyl-D-alanine, synthetase, UDP-N-acetylmuramoylalanyl-D-glutamyl-lysine-D-alanyl-D-alanine, ligase, uridine diphosphoacetylmuramoylpentapeptide synthetase, UDPacetylmuramoylpentapeptide synthetase, and UDP-MurNAc-L-Ala-D-Glu-L-Lys:D-Ala-D-Ala ligase. This enzyme participates in lysine biosynthesis and peptidoglycan biosynthesis.

References

    • Ito E, Strominger JL (1962). "Enzymatic synthesis of the peptide in bacterial uridine nucleotides II. Enzymatic synthesis and addition of D-alanyl-D-alanine". J. Biol. Chem. 237: 2696–2703.
    • 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.


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