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phosphoenolpyruvate + UDP-N-acetyl-alpha-D-glucosamine = phosphate + UDP-N-acetyl-3-O-(1-carboxyvinyl)-alpha-D-glucosamine
phosphoenolpyruvate + UDP-N-acetyl-alpha-D-glucosamine = phosphate + UDP-N-acetyl-3-O-(1-carboxyvinyl)-alpha-D-glucosamine
mechanism
-
phosphoenolpyruvate + UDP-N-acetyl-alpha-D-glucosamine = phosphate + UDP-N-acetyl-3-O-(1-carboxyvinyl)-alpha-D-glucosamine
mechanism
-
phosphoenolpyruvate + UDP-N-acetyl-alpha-D-glucosamine = phosphate + UDP-N-acetyl-3-O-(1-carboxyvinyl)-alpha-D-glucosamine
mechanism
phosphoenolpyruvate + UDP-N-acetyl-alpha-D-glucosamine = phosphate + UDP-N-acetyl-3-O-(1-carboxyvinyl)-alpha-D-glucosamine
active site SH-group
-
phosphoenolpyruvate + UDP-N-acetyl-alpha-D-glucosamine = phosphate + UDP-N-acetyl-3-O-(1-carboxyvinyl)-alpha-D-glucosamine
the addition step proceeds with protonation of C-3 of phosphoenolpyruvate from the 2-si face
-
phosphoenolpyruvate + UDP-N-acetyl-alpha-D-glucosamine = phosphate + UDP-N-acetyl-3-O-(1-carboxyvinyl)-alpha-D-glucosamine
D305 has a dual role as a general base and an essential binding partner to UDP-GlcNAc
-
phosphoenolpyruvate + UDP-N-acetyl-alpha-D-glucosamine = phosphate + UDP-N-acetyl-3-O-(1-carboxyvinyl)-alpha-D-glucosamine
Cys115 in the active site can act as proton donor, necessary for activity, or as a nucleophile
-
phosphoenolpyruvate + UDP-N-acetyl-alpha-D-glucosamine = phosphate + UDP-N-acetyl-3-O-(1-carboxyvinyl)-alpha-D-glucosamine
thermodynamical investigation of substrate binding and binding of inhibitory substrate analogue fosfomycin
phosphoenolpyruvate + UDP-N-acetyl-alpha-D-glucosamine = phosphate + UDP-N-acetyl-3-O-(1-carboxyvinyl)-alpha-D-glucosamine
Cys115 is the active site nucleophile
-
phosphoenolpyruvate + UDP-N-acetyl-alpha-D-glucosamine = phosphate + UDP-N-acetyl-3-O-(1-carboxyvinyl)-alpha-D-glucosamine
Cys115 is the active site nucleophile
-
phosphoenolpyruvate + UDP-N-acetyl-alpha-D-glucosamine = phosphate + UDP-N-acetyl-3-O-(1-carboxyvinyl)-alpha-D-glucosamine
N23 is responsible for stabilization of transition states
-
phosphoenolpyruvate + UDP-N-acetyl-alpha-D-glucosamine = phosphate + UDP-N-acetyl-3-O-(1-carboxyvinyl)-alpha-D-glucosamine
Asn23 and Asp305 are essential in the active site
-
phosphoenolpyruvate + UDP-N-acetyl-alpha-D-glucosamine = phosphate + UDP-N-acetyl-3-O-(1-carboxyvinyl)-alpha-D-glucosamine
mechanism, formation of a covalent intermediate between enzyme and enolpyruvate moiety
-
phosphoenolpyruvate + UDP-N-acetyl-alpha-D-glucosamine = phosphate + UDP-N-acetyl-3-O-(1-carboxyvinyl)-alpha-D-glucosamine
enyme exhibits an open conformation when substrate-free, and a closed, tightly-packed conformation upon substrate binding
-
phosphoenolpyruvate + UDP-N-acetyl-alpha-D-glucosamine = phosphate + UDP-N-acetyl-3-O-(1-carboxyvinyl)-alpha-D-glucosamine
enyme exhibits an open conformation when substrate-free, and a closed, tightly-packed conformation upon substrate binding
phosphoenolpyruvate + UDP-N-acetyl-alpha-D-glucosamine = phosphate + UDP-N-acetyl-3-O-(1-carboxyvinyl)-alpha-D-glucosamine
structure analysis of conformational changes upon substrate binding
-
phosphoenolpyruvate + UDP-N-acetyl-alpha-D-glucosamine = phosphate + UDP-N-acetyl-3-O-(1-carboxyvinyl)-alpha-D-glucosamine
Lys22 is located near the active site and involved in substrate binding
phosphoenolpyruvate + UDP-N-acetyl-alpha-D-glucosamine = phosphate + UDP-N-acetyl-3-O-(1-carboxyvinyl)-alpha-D-glucosamine
exchange of cysteine to aspartate in the active site
-
phosphoenolpyruvate + UDP-N-acetyl-alpha-D-glucosamine = phosphate + UDP-N-acetyl-3-O-(1-carboxyvinyl)-alpha-D-glucosamine
intramolecular general acid catalysis through protonation of the bridging oxygen of the phosphate
-
phosphoenolpyruvate + UDP-N-acetyl-alpha-D-glucosamine = phosphate + UDP-N-acetyl-3-O-(1-carboxyvinyl)-alpha-D-glucosamine
tetrahedral reaction intermediate, overall addition-elimination reaction is halted after the addition step
-
phosphoenolpyruvate + UDP-N-acetyl-alpha-D-glucosamine = phosphate + UDP-N-acetyl-3-O-(1-carboxyvinyl)-alpha-D-glucosamine
the addition step proceeds with protonation of C-3 of phosphoenolpyruvate from the 2-si face
-
-
phosphoenolpyruvate + UDP-N-acetyl-alpha-D-glucosamine = phosphate + UDP-N-acetyl-3-O-(1-carboxyvinyl)-alpha-D-glucosamine
mechanism
-
-
phosphoenolpyruvate + UDP-N-acetyl-alpha-D-glucosamine = phosphate + UDP-N-acetyl-3-O-(1-carboxyvinyl)-alpha-D-glucosamine
Cys115 is the active site nucleophile
-
-
phosphoenolpyruvate + UDP-N-acetyl-alpha-D-glucosamine = phosphate + UDP-N-acetyl-3-O-(1-carboxyvinyl)-alpha-D-glucosamine
structure analysis of conformational changes upon substrate binding
-
-
phosphoenolpyruvate + UDP-N-acetyl-alpha-D-glucosamine = phosphate + UDP-N-acetyl-3-O-(1-carboxyvinyl)-alpha-D-glucosamine
mechanism
-
-
phosphoenolpyruvate + UDP-N-acetyl-alpha-D-glucosamine = phosphate + UDP-N-acetyl-3-O-(1-carboxyvinyl)-alpha-D-glucosamine
Cys115 in the active site can act as proton donor, necessary for activity, or as a nucleophile
-
-
phosphoenolpyruvate + UDP-N-acetyl-alpha-D-glucosamine = phosphate + UDP-N-acetyl-3-O-(1-carboxyvinyl)-alpha-D-glucosamine
D305 has a dual role as a general base and an essential binding partner to UDP-GlcNAc
-
-
phosphoenolpyruvate + UDP-N-acetyl-alpha-D-glucosamine = phosphate + UDP-N-acetyl-3-O-(1-carboxyvinyl)-alpha-D-glucosamine
N23 is responsible for stabilization of transition states
-
-
phosphoenolpyruvate + UDP-N-acetyl-alpha-D-glucosamine = phosphate + UDP-N-acetyl-3-O-(1-carboxyvinyl)-alpha-D-glucosamine
Asn23 and Asp305 are essential in the active site
-
-
phosphoenolpyruvate + UDP-N-acetyl-alpha-D-glucosamine = phosphate + UDP-N-acetyl-3-O-(1-carboxyvinyl)-alpha-D-glucosamine
enyme exhibits an open conformation when substrate-free, and a closed, tightly-packed conformation upon substrate binding
-
-
phosphoenolpyruvate + UDP-N-acetyl-alpha-D-glucosamine = phosphate + UDP-N-acetyl-3-O-(1-carboxyvinyl)-alpha-D-glucosamine
Lys22 is located near the active site and involved in substrate binding
-
-
phosphoenolpyruvate + UDP-N-acetyl-alpha-D-glucosamine = phosphate + UDP-N-acetyl-3-O-(1-carboxyvinyl)-alpha-D-glucosamine
thermodynamical investigation of substrate binding and binding of inhibitory substrate analogue fosfomycin
-
-
phosphoenolpyruvate + UDP-N-acetyl-alpha-D-glucosamine = phosphate + UDP-N-acetyl-3-O-(1-carboxyvinyl)-alpha-D-glucosamine
exchange of cysteine to aspartate in the active site
-
-
phosphoenolpyruvate + UDP-N-acetyl-alpha-D-glucosamine = phosphate + UDP-N-acetyl-3-O-(1-carboxyvinyl)-alpha-D-glucosamine
-
-
-
-
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Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
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phosphoenol-2-oxobutyrate + UDP-N-acetyl-D-glucosamine
phosphate + UDP-N-acetylglucosaminyl-enol-2-oxobutyrate
-
-
-
?
phosphoenolpyruvate + UDP-N-acetyl-alpha-D-glucosamine
phosphate + UDP-N-acetyl-3-O-(1-carboxyvinyl)-alpha-D-glucosamine
phosphoenolpyruvate + UDP-N-acetyl-D-glucosamine
phosphate + UDP-N-acetyl-3-(1-carboxyvinyl)-D-glucosamine
phosphoenolpyruvate + UDP-N-acetyl-D-glucosamine
phosphate + UDP-N-acetyl-3-O-(1-carboxyvinyl)-D-glucosamine
phosphoenolpyruvate + UDP-N-acetyl-D-glucosamine
UDP-N-acetyl-3-O-(1-carboxyvinyl)-D-glucosamine + phosphate
additional information
?
-
phosphoenolpyruvate + UDP-N-acetyl-alpha-D-glucosamine
phosphate + UDP-N-acetyl-3-O-(1-carboxyvinyl)-alpha-D-glucosamine
-
-
-
-
?
phosphoenolpyruvate + UDP-N-acetyl-alpha-D-glucosamine
phosphate + UDP-N-acetyl-3-O-(1-carboxyvinyl)-alpha-D-glucosamine
-
the enzyme catalyzes the first committed step of peptidoglycan biosynthesis
-
-
?
phosphoenolpyruvate + UDP-N-acetyl-alpha-D-glucosamine
phosphate + UDP-N-acetyl-3-O-(1-carboxyvinyl)-alpha-D-glucosamine
-
-
-
-
?
phosphoenolpyruvate + UDP-N-acetyl-alpha-D-glucosamine
phosphate + UDP-N-acetyl-3-O-(1-carboxyvinyl)-alpha-D-glucosamine
-
-
-
-
?
phosphoenolpyruvate + UDP-N-acetyl-alpha-D-glucosamine
phosphate + UDP-N-acetyl-3-O-(1-carboxyvinyl)-alpha-D-glucosamine
-
-
-
?
phosphoenolpyruvate + UDP-N-acetyl-alpha-D-glucosamine
phosphate + UDP-N-acetyl-3-O-(1-carboxyvinyl)-alpha-D-glucosamine
the enzyme catalyzes the first step in the biosynthesis of the bacterial cell wall
-
-
?
phosphoenolpyruvate + UDP-N-acetyl-alpha-D-glucosamine
phosphate + UDP-N-acetyl-3-O-(1-carboxyvinyl)-alpha-D-glucosamine
-
-
-
?
phosphoenolpyruvate + UDP-N-acetyl-alpha-D-glucosamine
phosphate + UDP-N-acetyl-3-O-(1-carboxyvinyl)-alpha-D-glucosamine
-
-
-
?
phosphoenolpyruvate + UDP-N-acetyl-alpha-D-glucosamine
phosphate + UDP-N-acetyl-3-O-(1-carboxyvinyl)-alpha-D-glucosamine
-
-
-
?
phosphoenolpyruvate + UDP-N-acetyl-alpha-D-glucosamine
phosphate + UDP-N-acetyl-3-O-(1-carboxyvinyl)-alpha-D-glucosamine
-
-
-
-
?
phosphoenolpyruvate + UDP-N-acetyl-alpha-D-glucosamine
phosphate + UDP-N-acetyl-3-O-(1-carboxyvinyl)-alpha-D-glucosamine
-
-
-
-
?
phosphoenolpyruvate + UDP-N-acetyl-alpha-D-glucosamine
phosphate + UDP-N-acetyl-3-O-(1-carboxyvinyl)-alpha-D-glucosamine
-
-
-
?
phosphoenolpyruvate + UDP-N-acetyl-alpha-D-glucosamine
phosphate + UDP-N-acetyl-3-O-(1-carboxyvinyl)-alpha-D-glucosamine
-
-
-
?
phosphoenolpyruvate + UDP-N-acetyl-alpha-D-glucosamine
phosphate + UDP-N-acetyl-3-O-(1-carboxyvinyl)-alpha-D-glucosamine
-
-
-
-
?
phosphoenolpyruvate + UDP-N-acetyl-alpha-D-glucosamine
phosphate + UDP-N-acetyl-3-O-(1-carboxyvinyl)-alpha-D-glucosamine
-
-
-
-
?
phosphoenolpyruvate + UDP-N-acetyl-alpha-D-glucosamine
phosphate + UDP-N-acetyl-3-O-(1-carboxyvinyl)-alpha-D-glucosamine
-
-
-
-
?
phosphoenolpyruvate + UDP-N-acetyl-alpha-D-glucosamine
phosphate + UDP-N-acetyl-3-O-(1-carboxyvinyl)-alpha-D-glucosamine
-
-
-
-
?
phosphoenolpyruvate + UDP-N-acetyl-alpha-D-glucosamine
phosphate + UDP-N-acetyl-3-O-(1-carboxyvinyl)-alpha-D-glucosamine
-
-
-
-
?
phosphoenolpyruvate + UDP-N-acetyl-D-glucosamine
phosphate + UDP-N-acetyl-3-(1-carboxyvinyl)-D-glucosamine
-
-
i.e. UDP-N-acetyl-D-glucosamine-enolpyruvate
?
phosphoenolpyruvate + UDP-N-acetyl-D-glucosamine
phosphate + UDP-N-acetyl-3-(1-carboxyvinyl)-D-glucosamine
-
-
i.e. UDP-N-acetyl-D-glucosamine-enolpyruvate
?
phosphoenolpyruvate + UDP-N-acetyl-D-glucosamine
phosphate + UDP-N-acetyl-3-(1-carboxyvinyl)-D-glucosamine
-
-
-
?
phosphoenolpyruvate + UDP-N-acetyl-D-glucosamine
phosphate + UDP-N-acetyl-3-(1-carboxyvinyl)-D-glucosamine
-
peptidoglycan formation is essential for progression through the developmental cycle as well as for cell division
-
-
?
phosphoenolpyruvate + UDP-N-acetyl-D-glucosamine
phosphate + UDP-N-acetyl-3-(1-carboxyvinyl)-D-glucosamine
-
-
-
?
phosphoenolpyruvate + UDP-N-acetyl-D-glucosamine
phosphate + UDP-N-acetyl-3-(1-carboxyvinyl)-D-glucosamine
-
peptidoglycan formation is essential for progression through the developmental cycle as well as for cell division
-
-
?
phosphoenolpyruvate + UDP-N-acetyl-D-glucosamine
phosphate + UDP-N-acetyl-3-(1-carboxyvinyl)-D-glucosamine
-
-
-
?
phosphoenolpyruvate + UDP-N-acetyl-D-glucosamine
phosphate + UDP-N-acetyl-3-(1-carboxyvinyl)-D-glucosamine
-
-
-
?
phosphoenolpyruvate + UDP-N-acetyl-D-glucosamine
phosphate + UDP-N-acetyl-3-(1-carboxyvinyl)-D-glucosamine
-
-
-
-
?
phosphoenolpyruvate + UDP-N-acetyl-D-glucosamine
phosphate + UDP-N-acetyl-3-(1-carboxyvinyl)-D-glucosamine
-
-
-
r
phosphoenolpyruvate + UDP-N-acetyl-D-glucosamine
phosphate + UDP-N-acetyl-3-(1-carboxyvinyl)-D-glucosamine
-
-
-
r
phosphoenolpyruvate + UDP-N-acetyl-D-glucosamine
phosphate + UDP-N-acetyl-3-(1-carboxyvinyl)-D-glucosamine
-
-
r
phosphoenolpyruvate + UDP-N-acetyl-D-glucosamine
phosphate + UDP-N-acetyl-3-(1-carboxyvinyl)-D-glucosamine
-
-
r
phosphoenolpyruvate + UDP-N-acetyl-D-glucosamine
phosphate + UDP-N-acetyl-3-(1-carboxyvinyl)-D-glucosamine
-
-
-
r
phosphoenolpyruvate + UDP-N-acetyl-D-glucosamine
phosphate + UDP-N-acetyl-3-(1-carboxyvinyl)-D-glucosamine
-
-
i.e. UDP-N-acetyl-D-glucosamine-enolpyruvate
?
phosphoenolpyruvate + UDP-N-acetyl-D-glucosamine
phosphate + UDP-N-acetyl-3-(1-carboxyvinyl)-D-glucosamine
-
-
i.e. UDP-N-acetyl-D-glucosamine-enolpyruvate
?
phosphoenolpyruvate + UDP-N-acetyl-D-glucosamine
phosphate + UDP-N-acetyl-3-(1-carboxyvinyl)-D-glucosamine
-
-
i.e. UDP-N-acetyl-D-glucosamine-enolpyruvate
?
phosphoenolpyruvate + UDP-N-acetyl-D-glucosamine
phosphate + UDP-N-acetyl-3-(1-carboxyvinyl)-D-glucosamine
-
-
i.e. UDP-N-acetyl-D-glucosamine-enolpyruvate
r
phosphoenolpyruvate + UDP-N-acetyl-D-glucosamine
phosphate + UDP-N-acetyl-3-(1-carboxyvinyl)-D-glucosamine
-
specific for phosphoenolpyruvate and UDP-N-acetyl-D-glucosamine
i.e. UDP-N-acetyl-D-glucosamine-enolpyruvate
r
phosphoenolpyruvate + UDP-N-acetyl-D-glucosamine
phosphate + UDP-N-acetyl-3-(1-carboxyvinyl)-D-glucosamine
-
substrate binding structure
-
?
phosphoenolpyruvate + UDP-N-acetyl-D-glucosamine
phosphate + UDP-N-acetyl-3-(1-carboxyvinyl)-D-glucosamine
substrate binding structure
-
r
phosphoenolpyruvate + UDP-N-acetyl-D-glucosamine
phosphate + UDP-N-acetyl-3-(1-carboxyvinyl)-D-glucosamine
thermodynamic parameters of substrate binding, wild-type, C115S and K22 mutants
-
r
phosphoenolpyruvate + UDP-N-acetyl-D-glucosamine
phosphate + UDP-N-acetyl-3-(1-carboxyvinyl)-D-glucosamine
-
enzyme catalyzes the first committed step in the biosynthesis of bacterial cell wall peptidoglycan
-
-
?
phosphoenolpyruvate + UDP-N-acetyl-D-glucosamine
phosphate + UDP-N-acetyl-3-(1-carboxyvinyl)-D-glucosamine
-
pathway for biosynthesis of UDP-N-acetylmuramic acid
-
-
?
phosphoenolpyruvate + UDP-N-acetyl-D-glucosamine
phosphate + UDP-N-acetyl-3-(1-carboxyvinyl)-D-glucosamine
-
substrate binding structure
-
?
phosphoenolpyruvate + UDP-N-acetyl-D-glucosamine
phosphate + UDP-N-acetyl-3-(1-carboxyvinyl)-D-glucosamine
-
-
-
r
phosphoenolpyruvate + UDP-N-acetyl-D-glucosamine
phosphate + UDP-N-acetyl-3-(1-carboxyvinyl)-D-glucosamine
-
-
-
r
phosphoenolpyruvate + UDP-N-acetyl-D-glucosamine
phosphate + UDP-N-acetyl-3-(1-carboxyvinyl)-D-glucosamine
-
-
-
?
phosphoenolpyruvate + UDP-N-acetyl-D-glucosamine
phosphate + UDP-N-acetyl-3-(1-carboxyvinyl)-D-glucosamine
-
enzyme catalyzes the first committed step in the biosynthesis of bacterial cell wall peptidoglycan
-
-
?
phosphoenolpyruvate + UDP-N-acetyl-D-glucosamine
phosphate + UDP-N-acetyl-3-(1-carboxyvinyl)-D-glucosamine
-
-
r
phosphoenolpyruvate + UDP-N-acetyl-D-glucosamine
phosphate + UDP-N-acetyl-3-(1-carboxyvinyl)-D-glucosamine
substrate binding structure
-
r
phosphoenolpyruvate + UDP-N-acetyl-D-glucosamine
phosphate + UDP-N-acetyl-3-(1-carboxyvinyl)-D-glucosamine
thermodynamic parameters of substrate binding, wild-type, C115S and K22 mutants
-
r
phosphoenolpyruvate + UDP-N-acetyl-D-glucosamine
phosphate + UDP-N-acetyl-3-(1-carboxyvinyl)-D-glucosamine
-
-
r
phosphoenolpyruvate + UDP-N-acetyl-D-glucosamine
phosphate + UDP-N-acetyl-3-(1-carboxyvinyl)-D-glucosamine
-
specific for phosphoenolpyruvate and UDP-N-acetyl-D-glucosamine
i.e. UDP-N-acetyl-D-glucosamine-enolpyruvate
r
phosphoenolpyruvate + UDP-N-acetyl-D-glucosamine
phosphate + UDP-N-acetyl-3-(1-carboxyvinyl)-D-glucosamine
-
pathway for biosynthesis of UDP-N-acetylmuramic acid
-
-
?
phosphoenolpyruvate + UDP-N-acetyl-D-glucosamine
phosphate + UDP-N-acetyl-3-(1-carboxyvinyl)-D-glucosamine
-
-
-
?
phosphoenolpyruvate + UDP-N-acetyl-D-glucosamine
phosphate + UDP-N-acetyl-3-(1-carboxyvinyl)-D-glucosamine
-
-
-
?
phosphoenolpyruvate + UDP-N-acetyl-D-glucosamine
phosphate + UDP-N-acetyl-3-(1-carboxyvinyl)-D-glucosamine
-
-
-
?
phosphoenolpyruvate + UDP-N-acetyl-D-glucosamine
phosphate + UDP-N-acetyl-3-(1-carboxyvinyl)-D-glucosamine
-
-
-
-
?
phosphoenolpyruvate + UDP-N-acetyl-D-glucosamine
phosphate + UDP-N-acetyl-3-(1-carboxyvinyl)-D-glucosamine
-
-
?
phosphoenolpyruvate + UDP-N-acetyl-D-glucosamine
phosphate + UDP-N-acetyl-3-(1-carboxyvinyl)-D-glucosamine
-
-
?
phosphoenolpyruvate + UDP-N-acetyl-D-glucosamine
phosphate + UDP-N-acetyl-3-(1-carboxyvinyl)-D-glucosamine
-
-
i.e. UDP-N-acetyl-D-glucosamine-enolpyruvate
?
phosphoenolpyruvate + UDP-N-acetyl-D-glucosamine
phosphate + UDP-N-acetyl-3-(1-carboxyvinyl)-D-glucosamine
-
-
i.e. UDP-N-acetyl-D-glucosamine-enolpyruvate
?
phosphoenolpyruvate + UDP-N-acetyl-D-glucosamine
phosphate + UDP-N-acetyl-3-(1-carboxyvinyl)-D-glucosamine
-
substrate binding structure
-
?
phosphoenolpyruvate + UDP-N-acetyl-D-glucosamine
phosphate + UDP-N-acetyl-3-(1-carboxyvinyl)-D-glucosamine
-
enzyme catalyzes the first committed step in the biosynthesis of bacterial cell wall peptidoglycan
-
-
?
phosphoenolpyruvate + UDP-N-acetyl-D-glucosamine
phosphate + UDP-N-acetyl-3-(1-carboxyvinyl)-D-glucosamine
-
pathway for biosynthesis of UDP-N-acetylmuramic acid
-
-
?
phosphoenolpyruvate + UDP-N-acetyl-D-glucosamine
phosphate + UDP-N-acetyl-3-(1-carboxyvinyl)-D-glucosamine
-
-
i.e. UDP-N-acetyl-D-glucosamine-enolpyruvate
?
phosphoenolpyruvate + UDP-N-acetyl-D-glucosamine
phosphate + UDP-N-acetyl-3-(1-carboxyvinyl)-D-glucosamine
-
pathway for biosynthesis of UDP-N-acetylmuramic acid
-
-
?
phosphoenolpyruvate + UDP-N-acetyl-D-glucosamine
phosphate + UDP-N-acetyl-3-(1-carboxyvinyl)-D-glucosamine
-
-
i.e. UDP-N-acetyl-D-glucosamine-enolpyruvate
?
phosphoenolpyruvate + UDP-N-acetyl-D-glucosamine
phosphate + UDP-N-acetyl-3-(1-carboxyvinyl)-D-glucosamine
-
-
-
?
phosphoenolpyruvate + UDP-N-acetyl-D-glucosamine
phosphate + UDP-N-acetyl-3-(1-carboxyvinyl)-D-glucosamine
-
-
-
?
phosphoenolpyruvate + UDP-N-acetyl-D-glucosamine
phosphate + UDP-N-acetyl-3-(1-carboxyvinyl)-D-glucosamine
-
-
-
?
phosphoenolpyruvate + UDP-N-acetyl-D-glucosamine
phosphate + UDP-N-acetyl-3-(1-carboxyvinyl)-D-glucosamine
-
enzyme catalyzes the first committed step in the biosynthesis of bacterial cell wall peptidoglycan
-
-
?
phosphoenolpyruvate + UDP-N-acetyl-D-glucosamine
phosphate + UDP-N-acetyl-3-(1-carboxyvinyl)-D-glucosamine
-
-
-
-
?
phosphoenolpyruvate + UDP-N-acetyl-D-glucosamine
phosphate + UDP-N-acetyl-3-(1-carboxyvinyl)-D-glucosamine
-
-
-
?
phosphoenolpyruvate + UDP-N-acetyl-D-glucosamine
phosphate + UDP-N-acetyl-3-(1-carboxyvinyl)-D-glucosamine
-
-
i.e. UDP-N-acetyl-D-glucosamine-enolpyruvate
?
phosphoenolpyruvate + UDP-N-acetyl-D-glucosamine
phosphate + UDP-N-acetyl-3-(1-carboxyvinyl)-D-glucosamine
-
-
i.e. UDP-N-acetyl-D-glucosamine-enolpyruvate
?
phosphoenolpyruvate + UDP-N-acetyl-D-glucosamine
phosphate + UDP-N-acetyl-3-(1-carboxyvinyl)-D-glucosamine
-
-
-
?
phosphoenolpyruvate + UDP-N-acetyl-D-glucosamine
phosphate + UDP-N-acetyl-3-(1-carboxyvinyl)-D-glucosamine
-
enzyme activity is essential for the organism, the 2 isoforms can substitute for each other
-
-
?
phosphoenolpyruvate + UDP-N-acetyl-D-glucosamine
phosphate + UDP-N-acetyl-3-(1-carboxyvinyl)-D-glucosamine
-
-
-
?
phosphoenolpyruvate + UDP-N-acetyl-D-glucosamine
phosphate + UDP-N-acetyl-3-O-(1-carboxyvinyl)-D-glucosamine
-
-
-
?
phosphoenolpyruvate + UDP-N-acetyl-D-glucosamine
phosphate + UDP-N-acetyl-3-O-(1-carboxyvinyl)-D-glucosamine
-
-
-
?
phosphoenolpyruvate + UDP-N-acetyl-D-glucosamine
phosphate + UDP-N-acetyl-3-O-(1-carboxyvinyl)-D-glucosamine
-
-
-
-
?
phosphoenolpyruvate + UDP-N-acetyl-D-glucosamine
UDP-N-acetyl-3-O-(1-carboxyvinyl)-D-glucosamine + phosphate
-
-
-
?
phosphoenolpyruvate + UDP-N-acetyl-D-glucosamine
UDP-N-acetyl-3-O-(1-carboxyvinyl)-D-glucosamine + phosphate
-
-
-
?
phosphoenolpyruvate + UDP-N-acetyl-D-glucosamine
UDP-N-acetyl-3-O-(1-carboxyvinyl)-D-glucosamine + phosphate
-
-
-
r
phosphoenolpyruvate + UDP-N-acetyl-D-glucosamine
UDP-N-acetyl-3-O-(1-carboxyvinyl)-D-glucosamine + phosphate
-
-
-
-
?
phosphoenolpyruvate + UDP-N-acetyl-D-glucosamine
UDP-N-acetyl-3-O-(1-carboxyvinyl)-D-glucosamine + phosphate
-
-
-
-
r
phosphoenolpyruvate + UDP-N-acetyl-D-glucosamine
UDP-N-acetyl-3-O-(1-carboxyvinyl)-D-glucosamine + phosphate
-
-
-
r
phosphoenolpyruvate + UDP-N-acetyl-D-glucosamine
UDP-N-acetyl-3-O-(1-carboxyvinyl)-D-glucosamine + phosphate
-
-
-
-
r
phosphoenolpyruvate + UDP-N-acetyl-D-glucosamine
UDP-N-acetyl-3-O-(1-carboxyvinyl)-D-glucosamine + phosphate
-
-
-
-
?
phosphoenolpyruvate + UDP-N-acetyl-D-glucosamine
UDP-N-acetyl-3-O-(1-carboxyvinyl)-D-glucosamine + phosphate
-
-
-
?
phosphoenolpyruvate + UDP-N-acetyl-D-glucosamine
UDP-N-acetyl-3-O-(1-carboxyvinyl)-D-glucosamine + phosphate
-
-
-
r
phosphoenolpyruvate + UDP-N-acetyl-D-glucosamine
UDP-N-acetyl-3-O-(1-carboxyvinyl)-D-glucosamine + phosphate
-
-
-
r
phosphoenolpyruvate + UDP-N-acetyl-D-glucosamine
UDP-N-acetyl-3-O-(1-carboxyvinyl)-D-glucosamine + phosphate
-
-
-
?
phosphoenolpyruvate + UDP-N-acetyl-D-glucosamine
UDP-N-acetyl-3-O-(1-carboxyvinyl)-D-glucosamine + phosphate
-
-
-
-
r
phosphoenolpyruvate + UDP-N-acetyl-D-glucosamine
UDP-N-acetyl-3-O-(1-carboxyvinyl)-D-glucosamine + phosphate
-
-
-
-
r
phosphoenolpyruvate + UDP-N-acetyl-D-glucosamine
UDP-N-acetyl-3-O-(1-carboxyvinyl)-D-glucosamine + phosphate
-
-
-
-
r
phosphoenolpyruvate + UDP-N-acetyl-D-glucosamine
UDP-N-acetyl-3-O-(1-carboxyvinyl)-D-glucosamine + phosphate
-
-
-
-
r
additional information
?
-
-
no activity with (Z)-phosphoenol-2-oxobutyrate, phosphoenol-3-bromopyruvate and phosphoenol-3-phenylpyruvate
-
-
?
additional information
?
-
the enzyme does not display appreciable catalytic activity with UDP-N-acetyl-D-galactosamine as a substrate
-
-
?
additional information
?
-
-
MurA has also ATPase activity
-
-
?
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
phosphoenolpyruvate + UDP-N-acetyl-alpha-D-glucosamine
phosphate + UDP-N-acetyl-3-O-(1-carboxyvinyl)-alpha-D-glucosamine
phosphoenolpyruvate + UDP-N-acetyl-D-glucosamine
phosphate + UDP-N-acetyl-3-(1-carboxyvinyl)-D-glucosamine
phosphoenolpyruvate + UDP-N-acetyl-D-glucosamine
phosphate + UDP-N-acetyl-3-O-(1-carboxyvinyl)-D-glucosamine
phosphoenolpyruvate + UDP-N-acetyl-alpha-D-glucosamine
phosphate + UDP-N-acetyl-3-O-(1-carboxyvinyl)-alpha-D-glucosamine
-
-
-
-
?
phosphoenolpyruvate + UDP-N-acetyl-alpha-D-glucosamine
phosphate + UDP-N-acetyl-3-O-(1-carboxyvinyl)-alpha-D-glucosamine
-
the enzyme catalyzes the first committed step of peptidoglycan biosynthesis
-
-
?
phosphoenolpyruvate + UDP-N-acetyl-alpha-D-glucosamine
phosphate + UDP-N-acetyl-3-O-(1-carboxyvinyl)-alpha-D-glucosamine
-
-
-
-
?
phosphoenolpyruvate + UDP-N-acetyl-alpha-D-glucosamine
phosphate + UDP-N-acetyl-3-O-(1-carboxyvinyl)-alpha-D-glucosamine
-
-
-
-
?
phosphoenolpyruvate + UDP-N-acetyl-alpha-D-glucosamine
phosphate + UDP-N-acetyl-3-O-(1-carboxyvinyl)-alpha-D-glucosamine
-
-
-
?
phosphoenolpyruvate + UDP-N-acetyl-alpha-D-glucosamine
phosphate + UDP-N-acetyl-3-O-(1-carboxyvinyl)-alpha-D-glucosamine
the enzyme catalyzes the first step in the biosynthesis of the bacterial cell wall
-
-
?
phosphoenolpyruvate + UDP-N-acetyl-alpha-D-glucosamine
phosphate + UDP-N-acetyl-3-O-(1-carboxyvinyl)-alpha-D-glucosamine
-
-
-
?
phosphoenolpyruvate + UDP-N-acetyl-alpha-D-glucosamine
phosphate + UDP-N-acetyl-3-O-(1-carboxyvinyl)-alpha-D-glucosamine
-
-
-
?
phosphoenolpyruvate + UDP-N-acetyl-alpha-D-glucosamine
phosphate + UDP-N-acetyl-3-O-(1-carboxyvinyl)-alpha-D-glucosamine
-
-
-
?
phosphoenolpyruvate + UDP-N-acetyl-alpha-D-glucosamine
phosphate + UDP-N-acetyl-3-O-(1-carboxyvinyl)-alpha-D-glucosamine
-
-
-
-
?
phosphoenolpyruvate + UDP-N-acetyl-alpha-D-glucosamine
phosphate + UDP-N-acetyl-3-O-(1-carboxyvinyl)-alpha-D-glucosamine
-
-
-
-
?
phosphoenolpyruvate + UDP-N-acetyl-alpha-D-glucosamine
phosphate + UDP-N-acetyl-3-O-(1-carboxyvinyl)-alpha-D-glucosamine
-
-
-
?
phosphoenolpyruvate + UDP-N-acetyl-alpha-D-glucosamine
phosphate + UDP-N-acetyl-3-O-(1-carboxyvinyl)-alpha-D-glucosamine
-
-
-
?
phosphoenolpyruvate + UDP-N-acetyl-alpha-D-glucosamine
phosphate + UDP-N-acetyl-3-O-(1-carboxyvinyl)-alpha-D-glucosamine
-
-
-
-
?
phosphoenolpyruvate + UDP-N-acetyl-alpha-D-glucosamine
phosphate + UDP-N-acetyl-3-O-(1-carboxyvinyl)-alpha-D-glucosamine
-
-
-
-
?
phosphoenolpyruvate + UDP-N-acetyl-alpha-D-glucosamine
phosphate + UDP-N-acetyl-3-O-(1-carboxyvinyl)-alpha-D-glucosamine
-
-
-
-
?
phosphoenolpyruvate + UDP-N-acetyl-alpha-D-glucosamine
phosphate + UDP-N-acetyl-3-O-(1-carboxyvinyl)-alpha-D-glucosamine
-
-
-
-
?
phosphoenolpyruvate + UDP-N-acetyl-alpha-D-glucosamine
phosphate + UDP-N-acetyl-3-O-(1-carboxyvinyl)-alpha-D-glucosamine
-
-
-
-
?
phosphoenolpyruvate + UDP-N-acetyl-D-glucosamine
phosphate + UDP-N-acetyl-3-(1-carboxyvinyl)-D-glucosamine
-
peptidoglycan formation is essential for progression through the developmental cycle as well as for cell division
-
-
?
phosphoenolpyruvate + UDP-N-acetyl-D-glucosamine
phosphate + UDP-N-acetyl-3-(1-carboxyvinyl)-D-glucosamine
-
peptidoglycan formation is essential for progression through the developmental cycle as well as for cell division
-
-
?
phosphoenolpyruvate + UDP-N-acetyl-D-glucosamine
phosphate + UDP-N-acetyl-3-(1-carboxyvinyl)-D-glucosamine
-
enzyme catalyzes the first committed step in the biosynthesis of bacterial cell wall peptidoglycan
-
-
?
phosphoenolpyruvate + UDP-N-acetyl-D-glucosamine
phosphate + UDP-N-acetyl-3-(1-carboxyvinyl)-D-glucosamine
-
pathway for biosynthesis of UDP-N-acetylmuramic acid
-
-
?
phosphoenolpyruvate + UDP-N-acetyl-D-glucosamine
phosphate + UDP-N-acetyl-3-(1-carboxyvinyl)-D-glucosamine
-
enzyme catalyzes the first committed step in the biosynthesis of bacterial cell wall peptidoglycan
-
-
?
phosphoenolpyruvate + UDP-N-acetyl-D-glucosamine
phosphate + UDP-N-acetyl-3-(1-carboxyvinyl)-D-glucosamine
-
pathway for biosynthesis of UDP-N-acetylmuramic acid
-
-
?
phosphoenolpyruvate + UDP-N-acetyl-D-glucosamine
phosphate + UDP-N-acetyl-3-(1-carboxyvinyl)-D-glucosamine
-
-
-
-
?
phosphoenolpyruvate + UDP-N-acetyl-D-glucosamine
phosphate + UDP-N-acetyl-3-(1-carboxyvinyl)-D-glucosamine
-
enzyme catalyzes the first committed step in the biosynthesis of bacterial cell wall peptidoglycan
-
-
?
phosphoenolpyruvate + UDP-N-acetyl-D-glucosamine
phosphate + UDP-N-acetyl-3-(1-carboxyvinyl)-D-glucosamine
-
pathway for biosynthesis of UDP-N-acetylmuramic acid
-
-
?
phosphoenolpyruvate + UDP-N-acetyl-D-glucosamine
phosphate + UDP-N-acetyl-3-(1-carboxyvinyl)-D-glucosamine
-
pathway for biosynthesis of UDP-N-acetylmuramic acid
-
-
?
phosphoenolpyruvate + UDP-N-acetyl-D-glucosamine
phosphate + UDP-N-acetyl-3-(1-carboxyvinyl)-D-glucosamine
-
enzyme catalyzes the first committed step in the biosynthesis of bacterial cell wall peptidoglycan
-
-
?
phosphoenolpyruvate + UDP-N-acetyl-D-glucosamine
phosphate + UDP-N-acetyl-3-(1-carboxyvinyl)-D-glucosamine
-
-
-
-
?
phosphoenolpyruvate + UDP-N-acetyl-D-glucosamine
phosphate + UDP-N-acetyl-3-(1-carboxyvinyl)-D-glucosamine
-
enzyme activity is essential for the organism, the 2 isoforms can substitute for each other
-
-
?
phosphoenolpyruvate + UDP-N-acetyl-D-glucosamine
phosphate + UDP-N-acetyl-3-O-(1-carboxyvinyl)-D-glucosamine
-
-
-
?
phosphoenolpyruvate + UDP-N-acetyl-D-glucosamine
phosphate + UDP-N-acetyl-3-O-(1-carboxyvinyl)-D-glucosamine
-
-
-
?
phosphoenolpyruvate + UDP-N-acetyl-D-glucosamine
phosphate + UDP-N-acetyl-3-O-(1-carboxyvinyl)-D-glucosamine
-
-
-
-
?
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
(E)-3-fluorophosphoenolpyruvate
(hydroxymethyl)phosphonic acid
i.e. CID-21680357
(S)-2-[2-(naphthalene-1-sulfonylamino)-5-(naphthalene-1-sulfonyloxy)-benzoylamino]-pentanedioic acid
competitive with UDP-N-acetylglucosamine
(S)-2-[2-(naphthalene-1-sulfonylamino)-5-(naphthalene-1-sulfonyloxy)-benzoylamino]-succinic acid
-
(Z)-3-fluorophosphoenolpyruvate
2-(4-methylpiperazin-1-yl)-3,4-dihydronaphthalen-1(2H)-one
2-bromo-5-[(Z)-2-bromo-2-nitroethenyl]furan
-
-
2-chloro-3-(4-methoxyphenoxy)naphthalene-1,4-dione
-
-
2-oxo-1,3-benzoxathiol-5-yl (3-chlorophenyl)carbamate
2-oxo-1,3-benzoxathiol-5-yl methylcarbamate
2-oxo-1,3-benzoxathiol-5-yl pyridine-4-carboxylate
2-oxo-1,3-benzoxathiol-6-yl 4-nitrobenzenesulfonate
2-oxo-1,3-benzoxathiol-6-yl benzenesulfonate
2-oxo-1,3-benzoxathiol-6-yl methanesulfonate
2-oxo-1,3-benzoxathiol-6-yl sulfamate
2-[4-(2-hydroxyethyl)piperazin-1-yl]-3,4-dihydronaphthalen-1(2H)-one
2-[4-(2-hydroxyethyl)piperazin-1-yl]-6,7-dimethoxy-3,4-dihydronaphthalen-1(2H)-one
3-Bromopyruvate
-
irreversible, inhibitory effect is increased by UDP-GlcNAc
3-methylidenedihydrofuran-2(3H)-one
4,7-dichloro-5-hydroxy-1,3-benzoxathiol-2-one
5,5'-dithiobis(2-nitrobenzoic acid)
-
complete inhibition at 0.01 M; i.e. DTNB
5,7-dibromo-6-hydroxy-1,3-benzoxathiol-2-one
5-(prop-2-en-1-yloxy)-1,3-benzoxathiol-2-one
5-bromo-2-oxo-1,3-benzoxathiol-6-yl phenyl carbonate
5-hydroxy-1,3-benzoxathiol-2-one
5-hydroxy-7-(3-methylphenyl)-1,3-benzoxathiol-2-one
5-hydroxy-7-(4-methoxyphenyl)-1,3-benzoxathiol-2-one
5-hydroxybenzo[d][1,3]oxathiol-2-one
5-hydroxynaphtho[1,2-d][1,3]oxathiol-2-one
5-hydroxynaphtho[2,1-d][1,3]oxathiol-2-one
5-methoxy-1,3-benzoxathiole
5-methoxybenzo[d][1,3]oxathiol-2-one
6,7-dimethoxy-2-[4-(2-phenylethyl)piperazin-1-yl]-3,4-dihydronaphthalen-1(2H)-one
6-chloro-7-(4-methoxyphenoxy)quinoline-5,8-dione
-
-
7-(4-fluorophenyl)-5-hydroxy-1,3-benzoxathiol-2-one
7-chloro-6-(4-hydroxyphenoxy)quinoline-5,8-dione
HESFWYLPHQSY
-
i.e. PEP 1354. the peptide seems to prevent the closure of the Pro114-123 loop and, consequently, the open-closed transition of the MurA structure
iodoacetamide
-
inhibition by alkylation of the active site Cys155, pH-dependent, no alkylation below pH 7.0, maximum alkylation at pH 9.0
methyl 1,4-dihydroxynaphthalene-2-carboxylate
-
-
orientin
mixed type inhibition
oxalic acid
i.e. AB-00005001
oxamic acid
i.e. ZINC04658565
p-chloromercuribenzoate
-
-
PEP 1354 peptide
-
competitive inhibitor
-
PGE-553828
-
competitive against UDP-GlcNAc; inhibition mechanism, kinetics
-
phosphoenol-2-ketovalerate
-
-
phosphoenolpyruvate
-
about 65% residual activity at 2.5 mM
quercetin-3-O-D-glucuronide
uncompetitive inhibition
Tartronic acid
i.e. ZINC901335
Trypsin
wild-type and mutant C115S, no protection via individually binding of substrates or inhibitor fosfomycin, but via binding of both, the 2 substrates and inhibitor fosfomycin
-
UDP-N-acetylmuramic acid-L-Ala
-
weak
UDP-N-acetylmuramic acid-L-Ala-D-Glu
UDP-N-acetylmuramyl-L-Ala-D-Glu-meso-alpha,epsilon-diaminopimelic acid
uridine diphospho-N-acetylmuramyl-L-Ala-D-gamma-Glu-meso-alpha,epsilon-diaminopimelic-acid-D-Ala-D-Ala
(+)-6-tuliposide B
-
35% residual activity at 0.1 mM
(+)-6-tuliposide B
-
25% residual activity at 0.1 mM
(+)-tulipalin B
-
3.3% residual activity at 0.1 mM
(+)-tulipalin B
-
2.5% residual activity at 0.1 mM
(-)-tulipalin B
-
3.7% residual activity at 0.1 mM
(-)-tulipalin B
-
2.8% residual activity at 0.1 mM
(E)-3-fluorophosphoenolpyruvate
-
pseudosubstrate, formation of a tetrahedral intermediate in the reaction pathway, investigation of chirality of the intermediate stereospecifically formed at the active site in D2O
(E)-3-fluorophosphoenolpyruvate
-
formation of 2 reaction intermediates: a covalent phosphofluorolactyl-enzyme adduct and a free phosphofluorolactyl-UDP-GlcNAc tetrahedral adduct; inactivation; kinetics
(Z)-3-fluorophosphoenolpyruvate
-
pseudosubstrate, formation of a tetrahedral intermediate in the reaction pathway, investigation of chirality of the intermediate stereospecifically formed at the active site in D2O
(Z)-3-fluorophosphoenolpyruvate
-
formation of 2 reaction intermediates: a covalent phosphofluorolactyl-enzyme adduct and a free phosphofluorolactyl-UDP-GlcNAc tetrahedral adduct; inactivation; kinetics
(Z)-3-fluorophosphoenolpyruvate
-
kinetics, mutant C115D; wild-type and mutant C115D, competitive against phosphoenolpyruvate
1-tuliposide A
potent inhibitor
1-tuliposide A
potent inhibitor
1-tuliposide A
potent inhibitor
1-tuliposide A
-
potent inhibitor
1-tuliposide A
-
potent inhibitor
1-tuliposide A
-
potent inhibitor
1-tuliposide B
potent inhibitor
1-tuliposide B
potent inhibitor
1-tuliposide B
potent inhibitor
1-tuliposide B
-
potent inhibitor
1-tuliposide B
-
potent inhibitor
1-tuliposide B
-
potent inhibitor
2-(4-methylpiperazin-1-yl)-3,4-dihydronaphthalen-1(2H)-one
-
2-(4-methylpiperazin-1-yl)-3,4-dihydronaphthalen-1(2H)-one
-
-
2-(4-methylpiperazin-1-yl)-3,4-dihydronaphthalen-1(2H)-one
-
-
2-oxo-1,3-benzoxathiol-5-yl (3-chlorophenyl)carbamate
-
2-oxo-1,3-benzoxathiol-5-yl (3-chlorophenyl)carbamate
-
2-oxo-1,3-benzoxathiol-5-yl (3-chlorophenyl)carbamate
-
-
2-oxo-1,3-benzoxathiol-5-yl (3-chlorophenyl)carbamate
-
2-oxo-1,3-benzoxathiol-5-yl (3-chlorophenyl)carbamate
-
-
2-oxo-1,3-benzoxathiol-5-yl (3-chlorophenyl)carbamate
-
-
2-oxo-1,3-benzoxathiol-5-yl (3-chlorophenyl)carbamate
-
-
2-oxo-1,3-benzoxathiol-5-yl methylcarbamate
-
-
2-oxo-1,3-benzoxathiol-5-yl methylcarbamate
-
-
2-oxo-1,3-benzoxathiol-5-yl pyridine-4-carboxylate
-
-
2-oxo-1,3-benzoxathiol-5-yl pyridine-4-carboxylate
-
-
2-oxo-1,3-benzoxathiol-6-yl 4-nitrobenzenesulfonate
-
-
2-oxo-1,3-benzoxathiol-6-yl 4-nitrobenzenesulfonate
-
-
2-oxo-1,3-benzoxathiol-6-yl benzenesulfonate
-
2-oxo-1,3-benzoxathiol-6-yl benzenesulfonate
-
2-oxo-1,3-benzoxathiol-6-yl benzenesulfonate
-
-
2-oxo-1,3-benzoxathiol-6-yl benzenesulfonate
-
2-oxo-1,3-benzoxathiol-6-yl benzenesulfonate
-
-
2-oxo-1,3-benzoxathiol-6-yl benzenesulfonate
-
-
2-oxo-1,3-benzoxathiol-6-yl benzenesulfonate
-
-
2-oxo-1,3-benzoxathiol-6-yl methanesulfonate
-
2-oxo-1,3-benzoxathiol-6-yl methanesulfonate
-
2-oxo-1,3-benzoxathiol-6-yl methanesulfonate
-
-
2-oxo-1,3-benzoxathiol-6-yl methanesulfonate
-
2-oxo-1,3-benzoxathiol-6-yl methanesulfonate
-
-
2-oxo-1,3-benzoxathiol-6-yl methanesulfonate
-
-
2-oxo-1,3-benzoxathiol-6-yl methanesulfonate
-
-
2-oxo-1,3-benzoxathiol-6-yl sulfamate
-
-
2-oxo-1,3-benzoxathiol-6-yl sulfamate
-
-
2-[4-(2-hydroxyethyl)piperazin-1-yl]-3,4-dihydronaphthalen-1(2H)-one
-
2-[4-(2-hydroxyethyl)piperazin-1-yl]-3,4-dihydronaphthalen-1(2H)-one
-
-
2-[4-(2-hydroxyethyl)piperazin-1-yl]-6,7-dimethoxy-3,4-dihydronaphthalen-1(2H)-one
-
2-[4-(2-hydroxyethyl)piperazin-1-yl]-6,7-dimethoxy-3,4-dihydronaphthalen-1(2H)-one
-
-
3-methylidenedihydrofuran-2(3H)-one
-
54% residual activity at 0.1 mM
3-methylidenedihydrofuran-2(3H)-one
-
87% residual activity at 0.1 mM
4,7-dichloro-5-hydroxy-1,3-benzoxathiol-2-one
-
4,7-dichloro-5-hydroxy-1,3-benzoxathiol-2-one
-
4,7-dichloro-5-hydroxy-1,3-benzoxathiol-2-one
-
-
4,7-dichloro-5-hydroxy-1,3-benzoxathiol-2-one
-
4,7-dichloro-5-hydroxy-1,3-benzoxathiol-2-one
-
-
4,7-dichloro-5-hydroxy-1,3-benzoxathiol-2-one
-
-
4,7-dichloro-5-hydroxy-1,3-benzoxathiol-2-one
-
-
5,7-dibromo-6-hydroxy-1,3-benzoxathiol-2-one
-
-
5,7-dibromo-6-hydroxy-1,3-benzoxathiol-2-one
-
-
5-(prop-2-en-1-yloxy)-1,3-benzoxathiol-2-one
-
5-(prop-2-en-1-yloxy)-1,3-benzoxathiol-2-one
-
5-(prop-2-en-1-yloxy)-1,3-benzoxathiol-2-one
-
-
5-(prop-2-en-1-yloxy)-1,3-benzoxathiol-2-one
-
5-(prop-2-en-1-yloxy)-1,3-benzoxathiol-2-one
-
-
5-(prop-2-en-1-yloxy)-1,3-benzoxathiol-2-one
-
-
5-(prop-2-en-1-yloxy)-1,3-benzoxathiol-2-one
-
-
5-bromo-2-oxo-1,3-benzoxathiol-6-yl phenyl carbonate
-
5-bromo-2-oxo-1,3-benzoxathiol-6-yl phenyl carbonate
-
5-bromo-2-oxo-1,3-benzoxathiol-6-yl phenyl carbonate
-
5-bromo-2-oxo-1,3-benzoxathiol-6-yl phenyl carbonate
-
-
5-bromo-2-oxo-1,3-benzoxathiol-6-yl phenyl carbonate
-
-
5-bromo-2-oxo-1,3-benzoxathiol-6-yl phenyl carbonate
-
-
5-hydroxy-1,3-benzoxathiol-2-one
-
5-hydroxy-1,3-benzoxathiol-2-one
-
5-hydroxy-1,3-benzoxathiol-2-one
-
5-hydroxy-1,3-benzoxathiol-2-one
-
-
5-hydroxy-1,3-benzoxathiol-2-one
-
-
5-hydroxy-1,3-benzoxathiol-2-one
-
-
5-hydroxy-7-(3-methylphenyl)-1,3-benzoxathiol-2-one
-
-
5-hydroxy-7-(3-methylphenyl)-1,3-benzoxathiol-2-one
-
slight inhibition at 0.12 mM
5-hydroxy-7-(4-methoxyphenyl)-1,3-benzoxathiol-2-one
-
5-hydroxy-7-(4-methoxyphenyl)-1,3-benzoxathiol-2-one
-
5-hydroxy-7-(4-methoxyphenyl)-1,3-benzoxathiol-2-one
-
-
5-hydroxy-7-(4-methoxyphenyl)-1,3-benzoxathiol-2-one
-
5-hydroxy-7-(4-methoxyphenyl)-1,3-benzoxathiol-2-one
-
-
5-hydroxy-7-(4-methoxyphenyl)-1,3-benzoxathiol-2-one
-
-
5-hydroxy-7-(4-methoxyphenyl)-1,3-benzoxathiol-2-one
-
slight inhibition at 0.12 mM
5-hydroxy-7-(4-methoxyphenyl)-1,3-benzoxathiol-2-one
-
-
5-hydroxybenzo[d][1,3]oxathiol-2-one
-
-
5-hydroxybenzo[d][1,3]oxathiol-2-one
-
-
5-hydroxynaphtho[1,2-d][1,3]oxathiol-2-one
-
5-hydroxynaphtho[1,2-d][1,3]oxathiol-2-one
-
5-hydroxynaphtho[1,2-d][1,3]oxathiol-2-one
-
-
5-hydroxynaphtho[1,2-d][1,3]oxathiol-2-one
-
5-hydroxynaphtho[1,2-d][1,3]oxathiol-2-one
-
-
5-hydroxynaphtho[1,2-d][1,3]oxathiol-2-one
-
-
5-hydroxynaphtho[1,2-d][1,3]oxathiol-2-one
-
-
5-hydroxynaphtho[2,1-d][1,3]oxathiol-2-one
-
-
5-hydroxynaphtho[2,1-d][1,3]oxathiol-2-one
-
-
5-methoxy-1,3-benzoxathiole
-
-
5-methoxy-1,3-benzoxathiole
-
slight inhibition at 0.12 mM
5-methoxybenzo[d][1,3]oxathiol-2-one
-
-
5-methoxybenzo[d][1,3]oxathiol-2-one
-
-
6,7-dimethoxy-2-[4-(2-phenylethyl)piperazin-1-yl]-3,4-dihydronaphthalen-1(2H)-one
-
6,7-dimethoxy-2-[4-(2-phenylethyl)piperazin-1-yl]-3,4-dihydronaphthalen-1(2H)-one
-
-
7-(4-fluorophenyl)-5-hydroxy-1,3-benzoxathiol-2-one
-
-
7-(4-fluorophenyl)-5-hydroxy-1,3-benzoxathiol-2-one
-
slight inhibition at 0.12 mM
7-chloro-6-(4-hydroxyphenoxy)quinoline-5,8-dione
-
-
7-chloro-6-(4-hydroxyphenoxy)quinoline-5,8-dione
-
-
cnicin
sesquiterpene lactone. The enzyme catalyzes the formation of a covalent adduct between cnicin and substrate UDP-N-acetylglucosamine via an anti-Michael 1,3-addition of UDP-N-acetylglucosamine to an alpha,beta-unsaturated carbonyl function in cnicin thus forming a noncovalent suicide inhibitor
cnicine
-
Co2+
-
metal ions do not enhance the activity of enzymes, activity is inhibited by 10 mM
Cu2+
-
metal ions do not enhance the activity of enzymes, activity is inhibited by 10 mM
Cu2+
-
metal ions do not enhance the activity of enzymes, activity is inhibited by 10 mM
cynaropicrin
-
diarylmethane
-
ebselen
-
ebselen
inhibitor covalently modifies the cysteine residue near the active site-loop of MurA, modification changes the open conformation of MurA to a more closed configuration, when compound is incubated for 30 min with dithiothreitol, its inhibitory activity against Haemophilus influenzae MurA is completely eliminated
epi-(+)-6-tuliposide B
-
19% residual activity at 0.1 mM
epi-(+)-6-tuliposide B
-
17% residual activity at 0.1 mM
Fe2+
-
metal ions do not enhance the activity of enzymes, activity is inhibited by 10 mM
Fe2+
-
metal ions do not enhance the activity of enzymes, activity is inhibited by 10 mM
fosfomycin
-
50 mM, 3fold inhibition
fosfomycin
-
resistant to fosfomycin inhibition due to exchange of cysteine for aspartate in the active site
fosfomycin
-
irreversible, active site SH-group is involved
fosfomycin
-
alkylates Cys115
fosfomycin
-
binds covalently to Cys115
fosfomycin
irreversible, alkylation of C115
fosfomycin
-
selectively inhibited by fosfomycin, which forms a covalent bond to the sulfhydryl group of the catalytically relevant Cys115 residue
fosfomycin
irreversible inhibitor
fosfomycin
-
alkylates Cys115; competitive against phosphoenolpyruvate; inhibits the wild-type, mutant C155D is completely resistant; t1/2 for inactivation of the wild-type enzyme: 6 s
fosfomycin
-
binds covalently to Cys115
fosfomycin
-
binding study by isothermal titration calorimetry; binds covalently to Cys115
fosfomycin
-
selectively inhibited by fosfomycin, which forms a covalent bond to the sulfhydryl group of the catalytically relevant Cys115 residue
fosfomycin
enolpyruvyl UDP-GlcNAc synthase is an antimicrobial target that is inhibited by the antibiotic fosfomycin
fosfomycin
irreversible inhibitor
fosfomycin
-
irreversible inhibition
fosfomycin
acting competitively as an analogue of phosphoenolpyruvate
fosfomycin
-
more than 90% inhibition at 0.2 mM
fosfomycin
irreversible inhibitor
fosfomycin
-
irreversible inhibitor
fosfomycin
-
despite low level expression during normal growth, murZ expression is strongly induced up to 6fold following exposure to inhibitors of peptidoglycan biosynthesis, minimum inhibitory concentration is 4 mg/ml; the naturally occurring antibiotic, which is an analogue of phosphoenolpyruvate, irreversibly inhibits the majority of MurA enzymes, fosfomycin minimum inhibitory concentration is 8 mg/ml, peptidoglycan content is reduced by approximately 25% following inactivation of murA
fosfomycin
-
irreversible inhibitor
fosfomycin
-
irreversible inhibitor
fosfomycin
-
about 50% residual activity at 50 mM
HESFWYLPHHQSY
competitive inhibition
HESFWYLPHHQSY
competitive inhibition
HESFWYLPHHQSY
-
competitive inhibition
HESFWYLPHHQSY
competitive inhibition
HESFWYLPHHQSY
-
competitive inhibition
HESFWYLPHHQSY
-
competitive inhibition
HESFWYLPHHQSY
-
competitive inhibition
imidazole
-
MnCl2
-
metal ions do not enhance the activity of enzymes, activity is inhibited by 10 mM
MnCl2
-
metal ions do not enhance the activity of enzymes, activity is inhibited by 10 mM
N-ethylmaleimide
-
-
N-ethylmaleimide
-
complete inhibition at 0.2 M
phosphonomycin
-
i.e. L-cis-2-epoxypropylphosphonic acid; inhibitor binding site is distinct from active site; irreversible inactivation, requires the presence of UDP-GlcNAc
-
phosphonomycin
irreversible inactivation, requires the presence of UDP-GlcNAc
-
pyrazolopyrimidine
reversible inhibitor
pyrazolopyrimidine
reversible inhibitor
pyrazolopyrimidine
reversible inhibitor
pyrazolopyrimidine
-
reversible inhibitor
pyrazolopyrimidine
-
reversible inhibitor
pyrazolopyrimidine
-
reversible inhibitor
RWJ-110192
reversible inhibitor
RWJ-110192
reversible inhibitor
RWJ-110192
reversible inhibitor
RWJ-110192
-
reversible inhibitor
RWJ-110192
-
reversible inhibitor
RWJ-110192
-
reversible inhibitor
RWJ-140998
irreversible inhibitor
RWJ-140998
irreversible inhibitor
RWJ-140998
irreversible inhibitor
RWJ-140998
-
irreversible inhibitor
RWJ-140998
-
irreversible inhibitor
RWJ-140998
-
irreversible inhibitor
RWJ-3981
irreversible inhibitor
RWJ-3981
irreversible inhibitor
RWJ-3981
irreversible inhibitor
RWJ-3981
-
irreversible inhibitor
RWJ-3981
-
irreversible inhibitor
RWJ-3981
-
irreversible inhibitor
T6361
-
-
T6361
competitive inhibition
T6361
competitive inhibition
T6361
competitive inhibition
T6361
-
competitive inhibition
T6361
-
competitive inhibition
T6361
-
competitive inhibition
T6362
-
T6362
competitive inhibition
T6362
competitive inhibition
T6362
competitive inhibition
T6362
-
competitive inhibition
T6362
-
competitive inhibition
T6362
-
competitive inhibition
terreic acid
irreversible inhibitor
terreic acid
irreversible inhibitor
terreic acid
irreversible inhibitor
terreic acid
-
irreversible inhibitor
terreic acid
-
irreversible inhibitor
terreic acid
-
irreversible inhibitor
thimerosal
-
thimerosal
inhibitor covalently modifies the cysteine residue near the active site-loop of MurA, modification changes the open conformation of MurA to a more closed configuration, when compound is incubated for 30 min with dithiothreitol, its inhibitory activity against Haemophilus influenzae MurA is completely eliminated
thiram
-
thiram
inhibitor covalently modifies the cysteine residue near the active site-loop of MurA, modification changes the open conformation of MurA to a more closed configuration, when compound is incubated for 30 min with dithiothreitol, its inhibitory activity against Haemophilus influenzae MurA is completely eliminated
tulipaline A
-
tulipaline B
-
UDP-N-acetylmuramic acid
-
weak
UDP-N-acetylmuramic acid
-
competitive with phosphate
UDP-N-acetylmuramic acid
-
UDP-N-acetylmuramic acid
-
-
UDP-N-acetylmuramic acid-L-Ala-D-Glu
-
weak
UDP-N-acetylmuramic acid-L-Ala-D-Glu
-
no inhibition
UDP-N-acetylmuramyl-L-Ala-D-Glu-meso-alpha,epsilon-diaminopimelic acid
-
-
UDP-N-acetylmuramyl-L-Ala-D-Glu-meso-alpha,epsilon-diaminopimelic acid
-
inhibitor binding site is distinct from active site
UDP-N-acetylmuramyl-L-Ala-D-Glu-meso-alpha,epsilon-diaminopimelic acid
-
above 1 mM
uridine diphospho-N-acetylmuramyl-L-Ala-D-gamma-Glu-meso-alpha,epsilon-diaminopimelic-acid-D-Ala-D-Ala
-
-
uridine diphospho-N-acetylmuramyl-L-Ala-D-gamma-Glu-meso-alpha,epsilon-diaminopimelic-acid-D-Ala-D-Ala
-
inhibitor binding site is distinct from active site
uridine diphospho-N-acetylmuramyl-L-Ala-D-gamma-Glu-meso-alpha,epsilon-diaminopimelic-acid-D-Ala-D-Ala
-
above 1 mM
Zn2+
-
metal ions do not enhance the activity of enzymes, activity is inhibited by 10 mM
Zn2+
-
metal ions do not enhance the activity of enzymes, activity is inhibited by 10 mM
additional information
-
no inhibition by pyruvate and fluoropyruvate
-
additional information
inhibitors derived from 5-sulfonoxy-anthranilic acid obstruct the transition from the open and unliganded to the closed UDP-N-acetylglucosamine liganded form
-
additional information
-
no inhibition by UDP-galactose
-
additional information
insight into the catalytic mechanism and covalent inhibition by QM/MM MD simulations
-
additional information
inhibitors are identified through computational and in vitro approaches
-
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0.002
(+/-)-tulipaline B
Escherichia coli
-
pH and temperature not specified in the publication
0.00853 - 0.01204
2-(4-methylpiperazin-1-yl)-3,4-dihydronaphthalen-1(2H)-one
0.0028
2-bromo-5-[(Z)-2-bromo-2-nitroethenyl]furan
Escherichia coli
-
pH and temperature not specified in the publication
0.00071
2-chloro-3-(4-methoxyphenoxy)naphthalene-1,4-dione
Haemophilus influenzae
-
pH and temperature not specified in the publication
0.00286
2-oxo-1,3-benzoxathiol-5-yl (3-chlorophenyl)carbamate
0.00046
2-oxo-1,3-benzoxathiol-5-yl methylcarbamate
0.00058
2-oxo-1,3-benzoxathiol-5-yl pyridine-4-carboxylate
0.00515 - 0.01079
2-oxo-1,3-benzoxathiol-6-yl 4-nitrobenzenesulfonate
0.00196 - 0.00668
2-oxo-1,3-benzoxathiol-6-yl benzenesulfonate
0.00076 - 0.00113
2-oxo-1,3-benzoxathiol-6-yl methanesulfonate
0.00025 - 0.01794
2-oxo-1,3-benzoxathiol-6-yl sulfamate
0.01252 - 0.02249
2-[4-(2-hydroxyethyl)piperazin-1-yl]-3,4-dihydronaphthalen-1(2H)-one
0.00313 - 0.01735
2-[4-(2-hydroxyethyl)piperazin-1-yl]-6,7-dimethoxy-3,4-dihydronaphthalen-1(2H)-one
0.00028 - 0.00109
4,7-dichloro-5-hydroxy-1,3-benzoxathiol-2-one
0.00095 - 0.00349
5,7-dibromo-6-hydroxy-1,3-benzoxathiol-2-one
0.00801
5-(prop-2-en-1-yloxy)-1,3-benzoxathiol-2-one
0.00727
5-hydroxy-7-(3-methylphenyl)-1,3-benzoxathiol-2-one
Escherichia coli
-
in 50 mM Tris-HCl, pH 7.9, at 37°C
0.00951
5-hydroxy-7-(4-methoxyphenyl)-1,3-benzoxathiol-2-one
Escherichia coli
-
in 50 mM Tris-HCl, pH 7.9, at 37°C
0.00053 - 0.02707
5-hydroxybenzo[d][1,3]oxathiol-2-one
0.0031 - 0.02431
5-hydroxynaphtho[1,2-d][1,3]oxathiol-2-one
0.00155 - 0.02609
5-hydroxynaphtho[2,1-d][1,3]oxathiol-2-one
0.01428
5-methoxy-1,3-benzoxathiole
Escherichia coli
-
in 50 mM Tris-HCl, pH 7.9, at 37°C
0.00645 - 0.02479
5-methoxybenzo[d][1,3]oxathiol-2-one
0.02256 - 0.029
6,7-dimethoxy-2-[4-(2-phenylethyl)piperazin-1-yl]-3,4-dihydronaphthalen-1(2H)-one
0.000053
6-chloro-7-(4-methoxyphenoxy)quinoline-5,8-dione
Haemophilus influenzae
-
pH and temperature not specified in the publication
0.01854
7-(4-fluorophenyl)-5-hydroxy-1,3-benzoxathiol-2-one
Escherichia coli
-
in 50 mM Tris-HCl, pH 7.9, at 37°C
0.000064
7-chloro-6-(4-hydroxyphenoxy)quinoline-5,8-dione
Haemophilus influenzae
-
pH and temperature not specified in the publication
0.0103
cnicin
Escherichia coli
-
pH and temperature not specified in the publication
0.006
Cpd1
Escherichia coli
-
pH and temperature not specified in the publication
-
0.0001
ebselen
Haemophilus influenzae
50 mM Tris-HCl, pH 7.8, compound displays an anti-MurA activity that is above 90% at a concentration below 0.002 mM
0.00046 - 11.7
fosfomycin
0.2
HESFWYLPHQSY
Pseudomonas aeruginosa
-
pH and temperature not specified in the publication
0.0087
methyl 1,4-dihydroxynaphthalene-2-carboxylate
Haemophilus influenzae
-
pH and temperature not specified in the publication
0.0002
RWJ-3981
Escherichia coli
-
pH and temperature not specified in the publication
0.0004
thimerosal
Haemophilus influenzae
50 mM Tris-HCl, pH 7.8, compound displays an anti-MurA activity that is above 90% at a concentration below 0.002 mM
0.0007
thiram
Haemophilus influenzae
50 mM Tris-HCl, pH 7.8, compound displays an anti-MurA activity that is above 90% at a concentration below 0.002 mM
additional information
additional information
Bacillus anthracis
-
in wild-type background, IC50 of fosfomycin is 2,048 microg/ml. In a strain with antisense-based expression attenuation of the MurA1 gene encoding UDP-N-acetylglucosamine enolpyruvyl transferase, IC50 value is 126 microg/ml. Prsence of xylose further decreases the IC50 value to 18 microg/ml
-
0.00853
2-(4-methylpiperazin-1-yl)-3,4-dihydronaphthalen-1(2H)-one
Escherichia coli
-
0.00853
2-(4-methylpiperazin-1-yl)-3,4-dihydronaphthalen-1(2H)-one
Escherichia coli
-
pH and temperature not specified in the publication
0.01204
2-(4-methylpiperazin-1-yl)-3,4-dihydronaphthalen-1(2H)-one
Staphylococcus aureus
-
-
0.00286
2-oxo-1,3-benzoxathiol-5-yl (3-chlorophenyl)carbamate
Staphylococcus aureus
-
in 50 mM Tris-HCl, pH 7.9, at 37°C
0.00286
2-oxo-1,3-benzoxathiol-5-yl (3-chlorophenyl)carbamate
Escherichia coli
-
in 50 mM Tris-HCl, pH 7.9, at 37°C
0.00046
2-oxo-1,3-benzoxathiol-5-yl methylcarbamate
Staphylococcus aureus
-
in 50 mM Tris-HCl, pH 7.9, at 37°C
0.00046
2-oxo-1,3-benzoxathiol-5-yl methylcarbamate
Escherichia coli
-
in 50 mM Tris-HCl, pH 7.9, at 37°C
0.00058
2-oxo-1,3-benzoxathiol-5-yl pyridine-4-carboxylate
Staphylococcus aureus
-
in 50 mM Tris-HCl, pH 7.9, at 37°C
0.00058
2-oxo-1,3-benzoxathiol-5-yl pyridine-4-carboxylate
Escherichia coli
-
in 50 mM Tris-HCl, pH 7.9, at 37°C
0.00515
2-oxo-1,3-benzoxathiol-6-yl 4-nitrobenzenesulfonate
Escherichia coli
-
in 50 mM Tris-HCl, pH 7.9, at 37°C
0.01079
2-oxo-1,3-benzoxathiol-6-yl 4-nitrobenzenesulfonate
Staphylococcus aureus
-
in 50 mM Tris-HCl, pH 7.9, at 37°C
0.00196
2-oxo-1,3-benzoxathiol-6-yl benzenesulfonate
Escherichia coli
-
in 50 mM Tris-HCl, pH 7.9, at 37°C
0.00668
2-oxo-1,3-benzoxathiol-6-yl benzenesulfonate
Staphylococcus aureus
-
in 50 mM Tris-HCl, pH 7.9, at 37°C
0.00076
2-oxo-1,3-benzoxathiol-6-yl methanesulfonate
Escherichia coli
-
in 50 mM Tris-HCl, pH 7.9, at 37°C
0.00113
2-oxo-1,3-benzoxathiol-6-yl methanesulfonate
Staphylococcus aureus
-
in 50 mM Tris-HCl, pH 7.9, at 37°C
0.00025
2-oxo-1,3-benzoxathiol-6-yl sulfamate
Escherichia coli
-
in 50 mM Tris-HCl, pH 7.9, at 37°C
0.00239
2-oxo-1,3-benzoxathiol-6-yl sulfamate
Staphylococcus aureus
-
in 50 mM Tris-HCl, pH 7.9, at 37°C
0.00243
2-oxo-1,3-benzoxathiol-6-yl sulfamate
Escherichia coli
-
in 50 mM Tris-HCl, pH 7.9, at 37°C
0.01794
2-oxo-1,3-benzoxathiol-6-yl sulfamate
Staphylococcus aureus
-
in 50 mM Tris-HCl, pH 7.9, at 37°C
0.01252
2-[4-(2-hydroxyethyl)piperazin-1-yl]-3,4-dihydronaphthalen-1(2H)-one
Staphylococcus aureus
-
-
0.02249
2-[4-(2-hydroxyethyl)piperazin-1-yl]-3,4-dihydronaphthalen-1(2H)-one
Escherichia coli
-
0.00313
2-[4-(2-hydroxyethyl)piperazin-1-yl]-6,7-dimethoxy-3,4-dihydronaphthalen-1(2H)-one
Escherichia coli
-
0.01735
2-[4-(2-hydroxyethyl)piperazin-1-yl]-6,7-dimethoxy-3,4-dihydronaphthalen-1(2H)-one
Staphylococcus aureus
-
-
0.00028
4,7-dichloro-5-hydroxy-1,3-benzoxathiol-2-one
Escherichia coli
-
pH and temperature not specified in the publication
0.00028
4,7-dichloro-5-hydroxy-1,3-benzoxathiol-2-one
Escherichia coli
-
in 50 mM Tris-HCl, pH 7.9, at 37°C
0.00109
4,7-dichloro-5-hydroxy-1,3-benzoxathiol-2-one
Staphylococcus aureus
-
in 50 mM Tris-HCl, pH 7.9, at 37°C
0.00095
5,7-dibromo-6-hydroxy-1,3-benzoxathiol-2-one
Escherichia coli
-
in 50 mM Tris-HCl, pH 7.9, at 37°C
0.00349
5,7-dibromo-6-hydroxy-1,3-benzoxathiol-2-one
Staphylococcus aureus
-
in 50 mM Tris-HCl, pH 7.9, at 37°C
0.00801
5-(prop-2-en-1-yloxy)-1,3-benzoxathiol-2-one
Staphylococcus aureus
-
in 50 mM Tris-HCl, pH 7.9, at 37°C
0.00801
5-(prop-2-en-1-yloxy)-1,3-benzoxathiol-2-one
Escherichia coli
-
in 50 mM Tris-HCl, pH 7.9, at 37°C
0.00053
5-hydroxybenzo[d][1,3]oxathiol-2-one
Escherichia coli
-
in 50 mM Tris-HCl, pH 7.9, at 37°C
0.02707
5-hydroxybenzo[d][1,3]oxathiol-2-one
Staphylococcus aureus
-
in 50 mM Tris-HCl, pH 7.9, at 37°C
0.0031
5-hydroxynaphtho[1,2-d][1,3]oxathiol-2-one
Escherichia coli
-
in 50 mM Tris-HCl, pH 7.9, at 37°C
0.02431
5-hydroxynaphtho[1,2-d][1,3]oxathiol-2-one
Staphylococcus aureus
-
in 50 mM Tris-HCl, pH 7.9, at 37°C
0.00155
5-hydroxynaphtho[2,1-d][1,3]oxathiol-2-one
Escherichia coli
-
in 50 mM Tris-HCl, pH 7.9, at 37°C
0.02609
5-hydroxynaphtho[2,1-d][1,3]oxathiol-2-one
Staphylococcus aureus
-
in 50 mM Tris-HCl, pH 7.9, at 37°C
0.00645
5-methoxybenzo[d][1,3]oxathiol-2-one
Escherichia coli
-
in 50 mM Tris-HCl, pH 7.9, at 37°C
0.02479
5-methoxybenzo[d][1,3]oxathiol-2-one
Staphylococcus aureus
-
in 50 mM Tris-HCl, pH 7.9, at 37°C
0.02256
6,7-dimethoxy-2-[4-(2-phenylethyl)piperazin-1-yl]-3,4-dihydronaphthalen-1(2H)-one
Escherichia coli
-
0.029
6,7-dimethoxy-2-[4-(2-phenylethyl)piperazin-1-yl]-3,4-dihydronaphthalen-1(2H)-one
Staphylococcus aureus
-
-
0.00046
fosfomycin
Escherichia coli
-
0.00053
fosfomycin
Pseudomonas aeruginosa
-
enzyme is pre-incubated with the inhibitor in the presence of 1 mM UDP-N-acetyl-D-glucosamine, reaction is started by addition of phosphoenolpyruvate
0.0006
fosfomycin
Escherichia coli
-
in 50 mM Tris-HCl, pH 7.9, at 37°C
0.00077
fosfomycin
Escherichia coli
-
enzyme is pre-incubated with the inhibitor in the presence of 1 mM UDP-N-acetyl-D-glucosamine, reaction is started by addition of phosphoenolpyruvate
0.00125
fosfomycin
Staphylococcus aureus
-
in 50 mM Tris-HCl, pH 7.9, at 37°C
0.00136
fosfomycin
Staphylococcus aureus
-
-
0.00136
fosfomycin
Staphylococcus aureus
-
50 mM HEPES, 250 mM methylthioguanosine, 0.1 U/ml purine-nucleoside phosphorylase, 100 mM dithiothreitol, pH 7.6
0.00137
fosfomycin
Staphylococcus aureus
-
50 mM HEPES, 250 mM methylthioguanosine, 0.1 U/ml purine-nucleoside phosphorylase, 100 mM dithiothreitol, pH 7.6
0.0045
fosfomycin
Pseudomonas aeruginosa
-
enzyme shows 5-7fold shift in IC50 for the inhibitor upon pre-incubation with the substrate UDP-N-acetyl-D-glucosamine
0.0051
fosfomycin
Escherichia coli
-
enzyme shows 5-7fold shift in IC50 for the inhibitor upon pre-incubation with the substrate UDP-N-acetyl-D-glucosamine
0.0088
fosfomycin
Escherichia coli
-
pH and temperature not specified in the publication
0.04
fosfomycin
Haemophilus influenzae
50 mM Tris-HCl, pH 7.8, compound displays an anti-MurA activity that is above 90% at a concentration below 0.002 mM
11.7
fosfomycin
Acinetobacter baumannii
-
pH 7.5, 37°C
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C115D
the mutant enzyme lacks the ability to react with phosphoenolpyruvate covalently
C251S
-
site-directed mutagenesis, Cys251 is not involved in the catalysis, unaltered biochemical properties
C354S
-
site-directed mutagenesis, Cys354 is not involved in the catalysis, unaltered biochemical properties
C381S
-
site-directed mutagenesis, Cys381 is not involved in the catalysis, unaltered biochemical properties
D305C
-
site-directed mutagenesis, weaker binding of UDP-GlcNAc, no activity
D305E
-
site-directed mutagenesis, weaker binding of UDP-GlcNAc, 0.1% activity compared to the wild-type
D305H
-
site-directed mutagenesis, weaker binding of UDP-GlcNAc, no activity, fosfomycin is not covalently attached to Cys115
K22V/R120K
no residual activity, heat capacity changes are markedly redcued
K22V/R120V
no residual activity
N23A
-
site-directed mutagenesis, reduced activity, 20fold higher apparent dissociation constant for fosfomycin compared to wild-type
N23S
-
site-directed mutagenesis, reduced activity, 200fold higher apparent dissociation constant for fosfomycin compared to wild-type
R120K
less than 0.05% of wild-type activity, heat capacity changes are markedly redcued
C251S
-
site-directed mutagenesis, Cys251 is not involved in the catalysis, unaltered biochemical properties
-
C354S
-
site-directed mutagenesis, Cys354 is not involved in the catalysis, unaltered biochemical properties
-
C381S
-
site-directed mutagenesis, Cys381 is not involved in the catalysis, unaltered biochemical properties
-
D305A
-
site-directed mutagenesis, weaker binding of UDP-GlcNAc, no activity, fosfomycin is not covalently attached to Cys115
-
D305C
-
site-directed mutagenesis, weaker binding of UDP-GlcNAc, no activity
-
D305E
-
site-directed mutagenesis, weaker binding of UDP-GlcNAc, 0.1% activity compared to the wild-type
-
K22E
-
site-directed mutagenesis, exchange of conserved Lys residue located near the active site and involved in substrate binding leading to conformational changes, shows less than 0.5% activity compared to the wild-type, altered UDP-GlcNAc binding, highly reduced formation of covalent adduct between active site Cys115 and phosphoenolpyruvate or inhibitor fosfomycin
-
K22R
-
site-directed mutagenesis, exchange of conserved Lys residue located near the active site and involved in substrate binding leading to conformational changes, shows less than 0.5% activity compared to the wild-type, slightly reduced formation of covalent adduct between active site Cys115 and phosphoenolpyruvate or inhibitor fosfomycin
-
K22V
-
site-directed mutagenesis, exchange of conserved Lys residue located near the active site and involved in substrate binding leading to conformational changes, shows less than 0.5% activity compared to the wild-type, reduced formation of covalent adduct between active site Cys115 and phosphoenolpyruvate or inhibitor fosfomycin
-
N23A
-
site-directed mutagenesis, reduced activity, 20fold higher apparent dissociation constant for fosfomycin compared to wild-type
-
N23S
-
site-directed mutagenesis, reduced activity, 200fold higher apparent dissociation constant for fosfomycin compared to wild-type
-
C120S
-
catalytically inactive
C115A
-
site-directed mutagenesis, overexpression in Escherichia coli, no activity
C115E
-
site-directed mutagenesis, overexpression in Escherichia coli, gains fosfomycin resistance, enhanced pH-dependency of the reaction, low activity
C115N
-
site-directed mutagenesis, overexpression in Escherichia coli, deamination of Asn115 to Asp115
C115S
-
site-directed mutagenesis, overexpression in Escherichia coli, no activity
C115A
-
site-directed mutagenesis, overexpression in Escherichia coli, no activity
-
C115D
-
site-directed mutagenesis, overexpression in Escherichia coli, gains fosfomycin resistance, forms only the phospholactyl-enzyme intermediate adduct, but no UDP-GlcNAc-phosphoenolpyruvate, higher kcat than the wild-type at pH 7.0, enhanced pH-dependency of the reaction
-
C115E
-
site-directed mutagenesis, overexpression in Escherichia coli, gains fosfomycin resistance, enhanced pH-dependency of the reaction, low activity
-
C115N
-
site-directed mutagenesis, overexpression in Escherichia coli, deamination of Asn115 to Asp115
-
C115S
-
site-directed mutagenesis, overexpression in Escherichia coli, no activity
-
C115D
-
mutant protein is functional and resistant to fosfomycin and inhibitors 2-[4-(2-hydroxyethyl)piperazin-1-yl]-6,7-dimethoxy-3,4-dihydronaphthalen-1(2H)-one and2-(4-methylpiperazin-1-yl)-3,4-dihydronaphthalen-1(2H)-one
D120C
the mutant shows resistance against fosfomycin
C115S
-
-
C115S
mutant enzyme is capable of catalyzing the wild type enzyme reaction but is unable to release the products (single turnover), activity is not affected by fosfomycin
D305A
-
site-directed mutagenesis, weaker binding of UDP-GlcNAc, no activity, fosfomycin is not covalently attached to Cys115
D305A
-
crystallization data
K22E
site-directed mutagenesis, exchange of conserved Lys residue located near the active site and involved in substrate binding leading to conformational changes, shows less than 0.5% activity compared to the wild-type, altered UDP-GlcNAc binding, highly reduced formation of covalent adduct between active site Cys115 and phosphoenolpyruvate or inhibitor fosfomycin
K22E
0.05% of wild-type activity, no formation of covalent adduct with fosfomycin
K22R
0.3% of wild-type activity
K22R
site-directed mutagenesis, exchange of conserved Lys residue located near the active site and involved in substrate binding leading to conformational changes, shows less than 0.5% activity compared to the wild-type, slightly reduced formation of covalent adduct between active site Cys115 and phosphoenolpyruvate or inhibitor fosfomycin
K22V
site-directed mutagenesis, exchange of conserved Lys residue located near the active site and involved in substrate binding leading to conformational changes, shows less than 0.5% activity compared to the wild-type, reduced formation of covalent adduct between active site Cys115 and phosphoenolpyruvate or inhibitor fosfomycin
K22V
0.03% of wild-type activity, similar to wild-type in binding of fosfomycin, presence of UDP-N-acetylglucosamine required
C115D
-
site-directed mutagenesis, overexpression in Escherichia coli, gains fosfomycin resistance, forms only the phospholactyl-enzyme intermediate adduct, but no UDP-GlcNAc-phosphoenolpyruvate, higher kcat than the wild-type at pH 7.0, enhanced pH-dependency of the reaction
C115D
mutant protein is functional and resistant to fosfomycin and inhibitors 2-[4-(2-hydroxyethyl)piperazin-1-yl]-6,7-dimethoxy-3,4-dihydronaphthalen-1(2H)-one and2-(4-methylpiperazin-1-yl)-3,4-dihydronaphthalen-1(2H)-one
C117D
-
the mutation shifts ithe optimum pH from 7.8 to 6.0. The mutant is not inhibited by 1 mM fosfomycin
C117D
-
the mutant is not inhibited by fosfomycin
additional information
-
antisense-based modulation of murA1 gene expression, which encodes UDP-N-acetylglucosamine enolpyruvyl transferase, hypersensitizes cells to the MurA-specific antibiotic fosfomycin despite the normally high resistance of Bacillus anthracis to this drug
additional information
construction of a murA(Z) deletion mutant strain without catalytic activity, cells grow only when complemented by the enzyme expressed from a plasmid
additional information
-
construction of a murA(Z) deletion mutant strain without catalytic activity, cells grow only when complemented by the enzyme expressed from a plasmid
additional information
-
individually inactivation of the 2 isoforms by allelic replacement shows, that the 2 forms can substitute for each other, a double deletion mutant is not viable
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Gunetileke, K.G.; Anwar, R.A.
Biosynthesis of uridine diphospho-N-acetylmuramic acid. II. Purification and properties of pyruvate-uridine diphospho-N-acetylglucosamine transferase and characterization of uridine diphospho-N-acetylenopyruvylglucosamine
J. Biol. Chem.
243
5770-5778
1968
Enterobacter cloacae, Enterobacter cloacae NRC 492
brenda
Zemell, R.I.; Anwar, R.A.
Pyruvate-uridine diphospho-N-acetylglucosamine transferase. Purification to homogeneity and feedback inhibition
J. Biol. Chem.
250
3185-3192
1975
Enterobacter cloacae
brenda
Zemell, R.I.; Anwar, R.A.
Mechanism of pyruvate-uridine diphospho-N-acetylglucosamine transferase. Evidence for an enzyme-enolpyruvate intermediate
J. Biol. Chem.
250
4959-4964
1975
Enterobacter cloacae
brenda
Venkateswaran, P.S.; Lugtenberg, E.J.J.; Wu, H.C.
Inhibition of phosphoenolpyruvate:uridine diphosphate N-acetylglucosamine enolpyruvyltransferase by uridine diphosphate N-acetylmuramyl peptides
Biochim. Biophys. Acta
293
570-574
1973
Bacillus cereus, Escherichia coli, Escherichia coli K-235, Bacillus cereus T
brenda
Wickus, G.G.; Strominger, J.L.
Partial purification and properties of the pyruvate-uridine diphospho-N-acetylglucosamine transferase from Staphylococcus epidermidis
J. Bacteriol.
113
287-290
1973
Staphylococcus epidermidis, Staphylococcus epidermidis Texas 26
brenda
Wanke, C.; Falchetto, R.; Amrhein, N.
The UDP-N-acetylglucosamine 1-carboxyvinyl-transferase of Enterobacter cloacae. Molecular cloning, sequencing of the gene and overexpression of the enzyme
FEBS Lett.
301
271-276
1992
Enterobacter cloacae, Enterobacter cloacae DSM 30054
brenda
Marquardt, J.L.; Siegele, D.A.; Kolter, R.; Walsh, C.T.
Cloning and sequencing of Escherichia coli murZ and purification of its product, a UDP-N-acetylglucosamine enolpyruvyl transferase
J. Bacteriol.
174
5748-5752
1992
Escherichia coli (P0A749), Escherichia coli
brenda
Anwar, R.A.; Vlaovic, M.
Effect of phosphoenolpyruvate analogs on the activity of enoylpyruvate transferase and the effect of UDP-N-acetylglucosamine on the reactivity of the active site SH group
Biochim. Biophys. Acta
616
389-394
1980
Enterobacter cloacae
brenda
Brown, E.D.; Vivas, E.I.; Walsh, C.T.; Kolter, R.
MurA (MurZ), the enzyme that catalyzes the first committed step in peptidoglycan biosynthesis, is essential in Escherichia coli
J. Bacteriol.
177
4194-4197
1995
Escherichia coli (P0A749), Escherichia coli
brenda
Kim, D.H.; Lees, W.J.; Walsh, C.T.
Stereochemical analysis of the tetrahedral adduct formed at the active site of UDP-GlcNAc enolpyruvyl transferase from the pseudosubstrates, (E)- and (Z)-3-fluorophosphoenolpyruvate, in D2O
J. Am. Chem. Soc.
117
6380-6381
1995
Escherichia coli, Escherichia coli MurZ
-
brenda
Kim, D.H.; Lees, W.J.; Haley, T.M.; Walsh, C.T.
Kinetic characterization of the inactivation of UDP-GlcNAc enolpyruvyl transferase by (Z)-3-fluorophosphoenolpyruvate: evidence for two oxocarbenium ion intermediates in enolpyruvyl transfer catalysis
J. Am. Chem. Soc.
117
1494-1502
1995
Escherichia coli, Escherichia coli MurZ
-
brenda
Kim, D.H.; Lees, W.J.; Kempsell, K.E.; Lane, W.S.; Duncan, K.; Walsh, C.T.
Characterization of a Cys115 to Asp substitution in the Escherichia coli cell wall biosynthetic enzyme UDP-GlcNAc enolpyruvyl transferase (MurA) that confers resistance to inactivation by the antibiotic fosfomycin
Biochemistry
35
4923-4928
1996
Enterobacter cloacae, Escherichia coli, Escherichia coli MurA
brenda
Skarzynski, T.; Mistry, A.; Wonacott, A.; Hutchinson, S.E.; Kelly, V.A.; Duncan, K.
Structure of UDP-N-acetylglucosamine enolpyruvyl transferase, and enzyme essential for the synthesis of bacterial peptidoglycan, complexed with substrate UDP-N-acetylglucosamine and the drug fosfomycin
Structure
4
1465-1474
1996
Escherichia coli
brenda
Schoenbrunn, E.; Sack, S.; Eschenburg, S.; Perrakis, A.; Krekel, F.; Amrhein, N.; Mandelkow, E.
Crystal structure of UDP-N-acetylglucosamine enolpyruvyltransferase, the target of the antibiotic fosfomycin
Structure
4
1065-1075
1996
Enterobacter cloacae
brenda
Schonbrunn, E.; Svergun, D.I.; Amrhein, N.; Koch, M.H.J.
Studies on the conformational changes in the bacterial cell wall biosynthetic enzyme UDP-N-acetylglucosamine enolpyruvyltransferase (MurA)
Eur. J. Biochem.
253
406-412
1998
Enterobacter cloacae, Enterobacter cloacae DSM 30054
brenda
Krekel, F.; Oecking, C.; Amrhein, N.; Macheroux, P.
Substrate and inhibitor-induced conformational changes in the structurally related enzymes UDP-N-acetylglucosamine enolpyruvyl transferase (MurA) and 5-enolpyruvylshikimate 3-phosphate synthase (EPSPS)
Biochemistry
38
8864-8878
1999
Enterobacter cloacae (P33038), Enterobacter cloacae DSM 30054 (P33038)
brenda
Samland, A.K.; Amrhein, N.; Macheroux, P.
Lysine 22 in UDP-N-acetylglucosamine enolpyruvyl transferase from Enterobacter cloacae is crucial for enzymatic activity and the formation of covalent adducts with the substrate phosphoenolpyruvate and the antibiotic fosfomycin
Biochemistry
38
13162-13169
1999
Enterobacter cloacae (P33038), Enterobacter cloacae, Enterobacter cloacae DSM 30054 (P33038)
brenda
Du, W.; Brown, J.R.; Sylvester, D.R.; Huang, J.; Chalker, A.F.; So, C.Y.; Holmes, D.J.; Payne, D.J.; Wallis, N.G.
Two active forms of UDP-N-acetylglucosamine enolpyruvyl transferase in gram-positive bacteria
J. Bacteriol.
182
4146-4152
2000
Streptococcus pneumoniae
brenda
Krekel, F.; Samland, A.K.; Macheroux, P.; Amrhein, N.; Evans, J.N.S.
Determination of the pKa value of C115 in MurA (UDP-N-acetylglucosamine enolpyruvyltransferase) from Enterobacter cloacae
Biochemistry
39
12671-12677
2000
Enterobacter cloacae, Enterobacter cloacae DSM 30054
brenda
Dai, H.J.; Parker, C.N.; Bao, J.J.
Characterization and inhibition study of MurA enzyme by capillary electrophoresis
J. Chromatogr. B
766
123-132
2002
Escherichia coli, Escherichia coli MurA
brenda
Samland, A.K.; Jelesarov, I.; Kuhn, R.; Amrhein, N.; Macheroux, P.
Thermodynamic characterization of ligand-induced conformational changes in UDP-N-acetylglucosamine enolpyruvyl transferase
Biochemistry
40
9950-9956
2001
Enterobacter cloacae (P33038), Enterobacter cloacae DSM 30054 (P33038)
brenda
Samland, A.K.; Etezady-Esfarjani, T.; Amrhein, N.; Macheroux, P.
Asparagine 23 and aspartate 305 are essential residues in the active site of UDP-N-acetylglucosamine enolpyruvyl transferase from Enterobacter cloacae
Biochemistry
40
1550-1559
2001
Enterobacter cloacae, Enterobacter cloacae DSM 30054
brenda
McCoy, A.J.; Sandlin, R.C.; Maurelli, A.T.
In vitro and in vivo functional activity of Chlamydia MurA, a UDP-N-acetylglucosamine enolpyruvyl transferase involved in peptidoglycan synthesis and fosfomycin resistance
J. Bacteriol.
185
1218-1228
2003
Chlamydia trachomatis, Chlamydia trachomatis MurA
brenda
Mizyed, S.; Oddone, A.; Byczynski, B.; Hughes, D.W.; Berti, P.J.
UDP-N-acetylmuramic acid (UDP-MurNAc) is a potent inhibitor of MurA (enolpyruvyl-UDP-GlcNAc synthase)
Biochemistry
44
4011-4017
2005
Escherichia coli
brenda
Thomas, A.M.; Ginj, C.; Jelesarov, I.; Amrhein, N.; Macheroux, P.
Role of K22 and R120 in the covalent binding of the antibiotic fosfomycin and the substrate-induced conformational change in UDP-N-acetylglucosamine enolpyruvyl transferase
Eur. J. Biochem.
271
2682-2690
2004
Enterobacter cloacae (P33038)
brenda
Byczynski, B.; Mizyed, S.; Berti, P.J.
Nonenzymatic breakdown of the tetrahedral (alpha-carboxyketal phosphate) intermediates of MurA and AroA, two carboxyvinyl transferases. Protonation of different functional groups controls the rate and fate of breakdown
J. Am. Chem. Soc.
125
12541-12550
2003
Escherichia coli
brenda
Eschenburg, S.; Kabsch, W.; Healy, M.L.; Schonbrunn, E.
A new view of the mechanisms of UDP-N-acetylglucosamine enolpyruvyl transferase (MurA) and 5-enolpyruvylshikimate-3-phosphate synthase (AroA) derived from X-ray structures of their tetrahedral reaction intermediate states
J. Biol. Chem.
278
49215-49222
2003
Enterobacter cloacae
brenda
Eschenburg, S.; Priestman, M.A.; Abdul-Latif, F.A.; Delachaume, C.; Fassy, F.; Schonbrunn, E.
A novel inhibitor that suspends the induced fit mechanism of UDP-N-acetylglucosamine enolpyruvyl transferase (MurA)
J. Biol. Chem.
280
14070-14075
2005
Enterobacter cloacae (P33038)
brenda
Zhang, F.; Berti, P.J.
Phosphate analogues as probes of the catalytic mechanisms of MurA and AroA, two carboxyvinyl transferases
Biochemistry
45
6027-6037
2006
Escherichia coli
brenda
Eschenburg, S.; Priestman, M.; Schoenbrunn, E.
Evidence that the fosfomycin target Cys115 in UDP-N-acetylglucosamine enolpyruvyl transferase (MurA) is essential for product release
J. Biol. Chem.
280
3757-3763
2005
Enterobacter cloacae (P33038), Enterobacter cloacae
brenda
Klein, C.D.; Bachelier, A.
Molecular modeling and bioinformatical analysis of the antibacterial target enzyme MurA from a drug design perspective
J. Comput. Aided Mol. Des.
20
621-628
2006
Enterobacter cloacae, Escherichia coli
brenda
Griffiths, E.; Gupta, R.S.
Lateral transfers of serine hydroxymethyltransferase (glyA) and UDP-N-acetylglucosamine enolpyruvyl transferase (murA) genes from free-living Actinobacteria to the parasitic chlamydiae
J. Mol. Evol.
63
283-296
2006
Simkania negevensis (Q49K92), Simkania negevensis, Waddlia chondrophila (Q8GNY2), Waddlia chondrophila
brenda
Yoon, H.J.; Ku, M.J.; Ahn, H.J.; Lee, B.I.; Mikami, B.; Suh, S.W.
Crystallization and preliminary X-ray crystallographic analysis of UDP-N-acetylglucosamine enolpyruvyl transferase from Haemophilus influenzae in complex with UDP-N-acetylglucosamine and fosfomycin
Mol. Cell
19
398-401
2005
Haemophilus influenzae
brenda
Molina-Lopez, J.; Sanschagrin, F.; Levesque, R.C.
A peptide inhibitor of MurA UDP-N-acetylglucosamine enolpyruvyl transferase: the first committed step in peptidoglycan biosynthesis
Peptides
27
3115-3121
2006
Pseudomonas aeruginosa
brenda
Kedar, G.C.; Brown-Driver, V.; Reyes, D.R.; Hilgers, M.T.; Stidham, M.A.; Shaw, K.J.; Finn, J.; Haselbeck, R.J.
Comparison of the essential cellular functions of the two murA genes of Bacillus anthracis
Antimicrob. Agents Chemother.
52
2009-2013
2008
Bacillus anthracis
brenda
Dunsmore, C.J.; Miller, K.; Blake, K.L.; Patching, S.G.; Henderson, P.J.; Garnett, J.A.; Stubbings, W.J.; Phillips, S.E.; Palestrant, D.J.; Angeles, J.D.; Leeds, J.A.; Chopra, I.; Fishwick, C.W.
2-Aminotetralones: novel inhibitors of MurA and MurZ
Bioorg. Med. Chem. Lett.
18
1730-1734
2008
Staphylococcus aureus, Escherichia coli (P0A749)
brenda
Steinbach, A.; Scheidig, A.J.; Klein, C.D.
The unusual binding mode of cnicin to the antibacterial target enzyme MurA revealed by X-ray crystallography
J. Med. Chem.
51
5143-5147
2008
Escherichia coli (P0A749)
brenda
Yoon, H.; Lee, S.J.; Mikami, B.; Park, H.; Yoo, J.; Suh, S.W.
Crystal structure of UDP-N-acetylglucosamine enolpyruvyl transferase from Haemophilus influenzae in complex with UDP-N-acetylglucosamine and fosfomycin
Proteins Struct. Funct. Bioinform.
71
1032-1037
2008
Haemophilus influenzae (P45025), Haemophilus influenzae
brenda
Kumar, S.; Parvathi, A.; Hernandez, R.L.; Cadle, K.M.; Varela, M.F.
Identification of a novel UDP-N-acetylglucosamine enolpyruvyl transferase (MurA) from Vibrio fischeri that confers high fosfomycin resistance in Escherichia coli
Arch. Microbiol.
191
425-429
2009
Aliivibrio fischeri (B6DVJ7), Aliivibrio fischeri
brenda
Jackson, S.G.; Zhang, F.; Chindemi, P.; Junop, M.S.; Berti, P.J.
Evidence of kinetic control of ligand binding and staged product release in MurA (enolpyruvyl UDP-GlcNAc synthase)-catalyzed reactions
Biochemistry
48
11715-11723
2009
Escherichia coli (P0A749)
brenda
Jin, B.S.; Han, S.G.; Lee, W.K.; Ryoo, S.W.; Lee, S.J.; Suh, S.W.; Yu, Y.G.
Inhibitory mechanism of novel inhibitors of UDP-N-acetylglucosamine enolpyruvyl transferase from Haemophilus influenzae
J. Microbiol. Biotechnol.
19
1582-1589
2009
Haemophilus influenzae (P45025), Haemophilus influenzae
brenda
Blake, K.L.; ONeill, A.J.; Mengin-Lecreulx, D.; Henderson, P.J.; Bostock, J.M.; Dunsmore, C.J.; Simmons, K.J.; Fishwick, C.W.; Leeds, J.A.; Chopra, I.
The nature of Staphylococcus aureus MurA and MurZ and approaches for detection of peptidoglycan biosynthesis inhibitors
Mol. Microbiol.
72
335-343
2009
Staphylococcus aureus
brenda
Dube, S.; Nanda, K.; Rani, R.; Kaur, N.; Nagpal, J.; Upadhyay, D.; Cliffe, I.; Saini, K.; Purnapatre, K.
UDP-N-acetylglucosamine enolpyruvyl transferase from Pseudomonas aeruginosa
World J. Microbiol. Biotechnol.
26
1623-1629
2010
Escherichia coli, Pseudomonas aeruginosa
brenda
Bensen, D.C.; Rodriguez, S.; Nix, J.; Cunningham, M.L.; Tari, L.W.
Structure of MurA (UDP-N-acetylglucosamine enolpyruvyl transferase) from Vibrio fischeri in complex with substrate UDP-N-acetylglucosamine and the drug fosfomycin
Acta Crystallogr. Sect. F
68
382-385
2012
Aliivibrio fischeri (B5F9P4), Aliivibrio fischeri, Aliivibrio fischeri MJ11 (B5F9P4)
brenda
Vesic, D.; Kristich, C.J.
MurAA is required for intrinsic cephalosporin resistance of Enterococcus faecalis
Antimicrob. Agents Chemother.
56
2443-2451
2012
Enterococcus faecalis
brenda
Gautam, A.; Rishi, P.; Tewari, R.
UDP-N-acetylglucosamine enolpyruvyl transferase as a potential target for antibacterial chemotherapy: recent developments
Appl. Microbiol. Biotechnol.
92
211-225
2011
Streptococcus pneumoniae, Staphylococcus aureus, Pseudomonas aeruginosa, Escherichia coli (P0A749), Enterobacter cloacae (P33038), Mycobacterium tuberculosis (P9WJM1), Mycobacterium tuberculosis H37Rv (P9WJM1)
brenda
Cheng, G.; Hu, Y.; Lu, N.; Li, J.; Wang, Z.; Chen, Q.; Zhu, B.
Identification of a novel fosfomycin-resistant UDP-N-acetylglucosamine enolpyruvyl transferase (MurA) from a soil metagenome
Biotechnol. Lett.
35
273-278
2013
uncultured bacterium (H2DMJ3)
brenda
Han, S.; Jin, B.; Lee, W.; Yu, Y.
Kinetic properties of wild-type and C117D mutant UDP-N-acetylglucosamine enolpyruvyl transferase (MurA) from Haemophilus influenzae
Bull. Korean Chem. Soc.
32
2549-2552
2011
Haemophilus influenzae
-
brenda
Babajan, B.; Chaitanya, M.; Rajsekhar, C.; Gowsia, D.; Madhusudhana, P.; Naveen, M.; Chitta, S.K.; Anuradha, C.M.
Comprehensive structural and functional characterization of Mycobacterium tuberculosis UDP-NAG enolpyruvyl transferase (Mtb-MurA) and prediction of its accurate binding affinities with inhibitors
Interdiscip. Sci.
3
204-216
2011
Mycobacterium tuberculosis (P9WJM1), Mycobacterium tuberculosis, Mycobacterium tuberculosis H37Rv (P9WJM1)
brenda
Miller, K.; Dunsmore, C.J.; Leeds, J.A.; Patching, S.G.; Sachdeva, M.; Blake, K.L.; Stubbings, W.J.; Simmons, K.J.; Henderson, P.J.; De Los Angeles, J.; Fishwick, C.W.; Chopra, I.
Benzothioxalone derivatives as novel inhibitors of UDP-N-acetylglucosamine enolpyruvyl transferases (MurA and MurZ)
J. Antimicrob. Chemother.
65
2566-2573
2010
Escherichia coli, Staphylococcus aureus, Escherichia coli JM109, Staphylococcus aureus SH1000
brenda
Zhu, J.Y.; Yang, Y.; Han, H.; Betzi, S.; Olesen, S.H.; Marsilio, F.; Schoenbrunn, E.
Functional consequence of covalent reaction of phosphoenolpyruvate with UDP-N-acetylglucosamine 1-carboxyvinyltransferase (MurA)
J. Biol. Chem.
287
12657-12667
2012
Enterobacter cloacae (P33038)
brenda
Kaur, N.; Khokhar, M.; Jain, V.; Bharatam, P.V.; Sandhir, R.; Tewari, R.
Identification of druggable targets for Acinetobacter baumannii via subtractive genomics and plausible inhibitors for MurA and MurB
Appl. Biochem. Biotechnol.
171
417-436
2013
Acinetobacter baumannii
brenda
Hrast, M.; Sosic, I.; Sink, R.; Gobec, S.
Inhibitors of the peptidoglycan biosynthesis enzymes MurA-F
Bioorg. Chem.
55
2-15
2014
Escherichia coli
brenda
Shigetomi, K.; Olesen, S.H.; Yang, Y.; Mitsuhashi, S.; Schoenbrunn, E.; Ubukata, M.
MurA as a primary target of tulipalin B and 6-tuliposide B
Biosci. Biotechnol. Biochem.
77
2517-2519
2013
Enterobacter cloacae, Escherichia coli
brenda
Han, S.G.; Lee, W.K.; Jin, B.S.; Lee, K.I.; Lee, H.H.; Yu, Y.G.
Identification of novel irreversible inhibitors of UDP-N-acetylglucosamine enolpyruvyl transferase (MurA) from Haemophilus influenzae
J. Microbiol. Biotechnol.
23
329-334
2013
Haemophilus influenzae
brenda
Shahab, M.; Verma, M.; Pathak, M.; Mitra, K.; Misra-Bhattacharya, S.
Cloning, expression and characterization of UDP-N-acetylglucosamine enolpyruvyl transferase (MurA) from Wolbachia endosymbiont of human lymphatic filarial parasite Brugia malayi
PLoS ONE
9
e99884
2014
Wolbachia sp.
brenda
Xu, L.; Wu, D.; Liu, L.; Zheng, Q.; Song, Y.; Ye, L.; Sha, S.; Kang, J.; Xin, Y.; Ma, Y.
Characterization of mycobacterial UDP-N-acetylglucosamine enolpyruvyle transferase (MurA)
Res. Microbiol.
165
91-101
2014
Mycobacterium tuberculosis, Mycobacterium tuberculosis H37Rv, Mycolicibacterium smegmatis, Mycolicibacterium smegmatis mc(2)155 / ATCC 700084
brenda
Lima, A.H.; Dos Santos, A.M.; Alves, C.N.; Lameira, J.
Computed insight into a peptide inhibitor preventing the induced fit mechanism of MurA enzyme from Pseudomonas aeruginosa
Chem. Biol. Drug Des.
89
599-607
2017
Pseudomonas aeruginosa
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Boulhissa, I.; Chikhi, A.; Bensegueni, A.; Ghattas, M.A.; Mokrani, E.H.; Alrawashdeh, S.; Eddin Obaid, D.E.
Investigation for new inhibitors of UDP-N-acetylglucosamine enolpyruvyl transferase (MurA) by virtual screening with antibacterial sssessment
Curr. Comput. Aided Drug Des.
17
214-224
2020
Escherichia coli (P0A749), Escherichia coli, Escherichia coli K12 (P0A749)
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Alhaji Isa, M.; Majumdar, R.; Haider, S.; Kandasamy, S.
Molecular modelling and dynamic simulation of UDP-N-acetylglucosamine 1-carboxyvinyltransferase (MurA) from Mycobacterium tuberculosis using in silico approach
Inform. Med. Unlocked
12
56-66
2018
Mycobacterium tuberculosis (P9WJM1), Mycobacterium tuberculosis ATCC 25618 (P9WJM1)
-
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Sonkar, A.; Shukla, H.; Shukla, R.; Kalita, J.; Tripathi, T.
Unfolding of Acinetobacter baumannii MurA proceeds through a metastable intermediate A combined spectroscopic and computational investigation
Int. J. Biol. Macromol.
126
941-951
2019
Acinetobacter baumannii
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Sonkar, A.; Shukla, H.; Shukla, R.; Kalita, J.; Pandey, T.; Tripathi, T.
UDP-N-Acetylglucosamine enolpyruvyl transferase (MurA) of Acinetobacter baumannii (AbMurA) Structural and functional properties
Int. J. Biol. Macromol.
97
106-114
2017
Acinetobacter baumannii
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Mihalovits, L.M.; Ferenczy, G.G.; Keseru, G.M.
Catalytic mechanism and covalent inhibition of UDP-N-acetylglucosamine enolpyruvyl transferase (MurA) Implications to the design of novel antibacterials
J. Chem. Inf. Model.
59
5161-5173
2019
Escherichia coli (P0A749)
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Kumar, A.; Saranathan, R.; Prashanth, K.; Tiwary, B.K.; Krishna, R.
Inhibition of the MurA enzyme in Fusobacterium nucleatum by potential inhibitors identified through computational and in vitro approaches
Mol. Biosyst.
13
939-954
2017
Fusobacterium nucleatum subsp. nucleatum (Q8RIQ1), Fusobacterium nucleatum subsp. nucleatum ATCC 25586 (Q8RIQ1)
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