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Literature summary for 2.4.1.129 extracted from

  • Perlstein, D.; Wang, T.; Doud, E.; Kahne, D.; Walker, S.
    The role of the substrate lipid in processive glycan polymerization by the peptidoglycan glycosyltransferases (2010), J. Am. Chem. Soc., 132, 48-49.
    View publication on PubMedView publication on EuropePMC

Organism

Organism UniProt Comment Textmining
Aquifex aeolicus
-
-
-

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
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Aquifex aeolicus [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
PBP1a
-
Aquifex aeolicus
PGT
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Aquifex aeolicus

General Information

General Information Comment Organism
physiological function PGT catalyzes the polymerization of lipid II to form the bacterial cell wall Aquifex aeolicus