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Literature summary for 2.4.1.129 extracted from

  • Zawadzka-Skomial, J.; Markiewicz, Z.; Nguyen-Disteche, M.; Devreese, B.; Frere, J.M.; Terrak, M.
    Characterization of the bifunctional glycosyltransferase/acyltransferase penicillin-binding protein 4 of Listeria monocytogenes (2006), J. Bacteriol., 188, 1875-1881.
    View publication on PubMedView publication on EuropePMC
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Cloned(Commentary)

Cloned (Comment) Organism
PBP4 was not functional in Escherichia coli Listeria monocytogenes

Inhibitors

Inhibitors Comment Organism Structure
penicillin
-
 Listeria monocytogenes

Natural Substrates/ Products (Substrates)

Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
[GlcNAc-(1-4)-Mur2Ac(oyl-L-Ala-gamma-D-Glu-L-Lys-D-Ala-D-Ala)]n-diphosphoundecaprenol + GlcNAc-(1-4)-Mur2Ac(oyl-L-Ala-gamma-D-Glu-L-Lys-D-Ala-D-Ala)-diphosphoundecaprenol Listeria monocytogenes PBP4 is dispensable and that, as in other bacteria, its absence can be compensated for by the second class A PBP, PBP1 [GlcNAc-(1-4)-Mur2Ac(oyl-L-Ala-gamma-D-Glu-L-Lys-D-Ala-D-Ala)]n+1-diphosphoundecaprenol + undecaprenyl diphosphate
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 ?

Organism

Organism UniProt Comment Textmining
Listeria monocytogenes
-
-
-

Purification (Commentary)

Purification (Comment) Organism
-
 Listeria monocytogenes

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
[GlcNAc-(1-4)-Mur2Ac(oyl-L-Ala-gamma-D-Glu-L-Lys-D-Ala-D-Ala)]n-diphosphoundecaprenol + GlcNAc-(1-4)-Mur2Ac(oyl-L-Ala-gamma-D-Glu-L-Lys-D-Ala-D-Ala)-diphosphoundecaprenol PBP4 is dispensable and that, as in other bacteria, its absence can be compensated for by the second class A PBP, PBP1 Listeria monocytogenes [GlcNAc-(1-4)-Mur2Ac(oyl-L-Ala-gamma-D-Glu-L-Lys-D-Ala-D-Ala)]n+1-diphosphoundecaprenol + undecaprenyl diphosphate
-
 ?
[GlcNAc-(1-4)-Mur2Ac(oyl-L-Ala-gamma-D-Glu-L-Lys-D-Ala-D-Ala)]n-diphosphoundecaprenol + GlcNAc-(1-4)-Mur2Ac(oyl-L-Ala-gamma-D-Glu-L-Lys-D-Ala-D-Ala)-diphosphoundecaprenol glycosyltransferase activity catalyzes glycan chain elongation from lipid II substrate undecaprenyl-pyrophosphoryl-N-acetylglucosamine-N-acetylmuramic acid-pentapeptide. PBP4 also catalyzes the aminolysis (D-Ala as acceptor) and hydrolysis of the thiolester donor substrate benzoyl-Gly-thioglycolate, indicating that PBP4 possesses both transpeptidase and carboxypeptidase activities Listeria monocytogenes [GlcNAc-(1-4)-Mur2Ac(oyl-L-Ala-gamma-D-Glu-L-Lys-D-Ala-D-Ala)]n+1-diphosphoundecaprenol + undecaprenyl diphosphate
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 ?

Synonyms

Synonyms Comment Organism
glycosyltransferase/acyltransferase penicillin-binding protein 4
-
 Listeria monocytogenes
PBP4
-
 Listeria monocytogenes