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UDP-N-acetylmuramoylpentapeptide-lysine N6-alanyltransferase

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UDP-N-acetylmuramoylpentapeptide-lysine N6-alanyltransferase
Identifiers
EC no.2.3.2.10
CAS no.37257-26-4
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
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NCBIproteins

In enzymology, an UDP-N-acetylmuramoylpentapeptide-lysine N6-alanyltransferase (EC 2.3.2.10) is an enzyme that catalyzes the chemical reaction

L-alanyl-tRNA + UDP-N-acetylmuramoyl-L-alanyl-D-glutamyl-L-lysyl-D-alanyl-D-alanine tRNA + UDP-N-acetylmuramoyl-L-alanyl-D-glutamyl-N6-(L-alanyl)-L-lysyl-D- alanyl-D-alanine

Thus, the two substrates of this enzyme are L-alanyl-tRNA and UDP-N-acetylmuramoyl-L-alanyl-D-glutamyl-L-lysyl-D-alanyl-D-alanine, whereas its 3 products are tRNA, UDP-N-acetylmuramoyl-L-alanyl-D-glutamyl-N6-(L-alanyl)-L-lysyl-D-, and alanyl-D-alanine.

This enzyme belongs to the family of transferases, specifically the aminoacyltransferases. The systematic name of this enzyme class is L-alanyl-tRNA:UDP-N-acetylmuramoyl-L-alanyl-D-glutamyl-L-lysyl-D-ala nyl-D-alanine N6-alanyltransferase. Other names in common use include alanyl-transfer ribonucleate-uridine, diphosphoacetylmuramoylpentapeptide transferase, UDP-N-acetylmuramoylpentapeptide lysine N6-alanyltransferase, uridine diphosphoacetylmuramoylpentapeptide lysine, N6-alanyltransferase, L-alanyl-tRNA:UDP-N-acetylmuramoyl-L-alanyl-D-glutamyl-L-lysyl-D-, and alanyl-D-alanine 6-N-alanyltransferase. This enzyme participates in peptidoglycan biosynthesis.

Structural studies

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As of late 2007, 4 structures have been solved for this class of enzymes, with PDB accession codes 1P4N, 1XE4, 1XF8, and 1XIX.

References

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  • Plapp R, Strominger JL (1970). "Biosynthesis of the peptidoglycan of bacterial cell walls. 18 Purification and properties of L-alanyl transfer ribonucleic acid-uridine diphosphate-N-acetylmuramyl-pentapeptide transferase from Lactobacillus viridescens". J. Biol. Chem. 245 (14): 3675–82. doi:10.1016/S0021-9258(18)62979-5. PMID 4248527.