2.5.1.7: UDP-N-acetylglucosamine 1-carboxyvinyltransferase
This is an abbreviated version!
For detailed information about UDP-N-acetylglucosamine 1-carboxyvinyltransferase, go to the full flat file.
Word Map on EC 2.5.1.7
-
2.5.1.7
-
peptidoglycan
-
fosfomycin
-
pep
-
cloacae
-
enterobacter
-
medicine
-
epsps
-
drug development
-
5-enolpyruvylshikimate
-
sanguinis
-
5-enolpyruvylshikimate-3-phosphate
- 2.5.1.7
- peptidoglycan
- fosfomycin
- pep
- cloacae
- enterobacter
- medicine
- epsps
- drug development
-
5-enolpyruvylshikimate
- sanguinis
- 5-enolpyruvylshikimate-3-phosphate
Reaction
Synonyms
enol-pyruvyltransferase, enolpyruvyl UDP-GlcNAc synthase, enoylpyruvate transferase, enoylpyruvatetransferase, EPT, More, MurA, MurA enzyme, MurA transferase, MurAA, MurZ, phosphoenolpyruvate-UDP-acetylglucosamine-3-enolpyruvyltransferase, phosphoenolpyruvate:UDP-2-acetamido-2-deoxy-D-glucose 2-enoyl-1-carboxyethyltransferase, phosphoenolpyruvate:uridine diphosphate N-acetylglucosamine enolpyruvyltransferase, phosphoenolpyruvate:uridine-5'-diphospho-N-acetyl-2-amino-2-deoxyglucose-3-enolpyruvyltransferase, phosphopyruvate-uridine diphosphoacetylglucosamine pyruvatetransferase, pyruvate-UDP-acetylglucosamine transferase, pyruvate-uridine diphospho-N-acetyl-glucosamine transferase, pyruvate-uridine diphospho-N-acetylglucosamine transferase, pyruvatetransferase, phosphoenolpyruvate-uridine diphosphoacetylglucosamine, pyruvic-uridine diphospho-N-acetylglucosaminyltransferase, UDP-GlcNAc enolpyruvyl transferase, UDP-N-acetylglucosamine 1-carboxyvinyl transferase, UDP-N-acetylglucosamine 1-carboxyvinyl-transferase, UDP-N-acetylglucosamine 1-carboxyvinyltransferase, UDP-N-acetylglucosamine enolpyruvyl transferase, UDP-N-acetylglucosamine enolpyruvyle transferase, UDP-N-acetylglucosamine enolpyruvyltransferase, UDP-N-acetylglucosamine enoylpyruvyltransferase, UDP-N-acetylglucosamine-enolpyruvyl transferase, UDP-NAG enolpyruvyl transferase, UNAG enolpyruvyl transferase
ECTree
2.5.1.7 UDP-N-acetylglucosamine 1-carboxyvinyltransferaseAdvanced search results
results (
results (Inhibitors
Inhibitors on EC 2.5.1.7 - UDP-N-acetylglucosamine 1-carboxyvinyltransferase
Please wait a moment until all data is loaded. This message will disappear when all data is loaded.
top
INHIBITOR 
ORGANISM
UNIPROT
COMMENTARY 
LITERATURE
IMAGE
(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
-
3-Bromopyruvate
-
irreversible, inhibitory effect is increased by UDP-GlcNAc
5,5'-dithiobis(2-nitrobenzoic acid)
-
complete inhibition at 0.01 M; i.e. DTNB
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
PGE-553828
-
competitive against UDP-GlcNAc; inhibition mechanism, kinetics
-
quercetin-3-O-D-glucuronide
uncompetitive inhibition
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
-
uridine diphospho-N-acetylmuramyl-L-Ala-D-gamma-Glu-meso-alpha,epsilon-diaminopimelic-acid-D-Ala-D-Ala
(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
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
-
-
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
-
slight inhibition at 0.12 mM
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
-
slight inhibition at 0.12 mM
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
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
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
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
-
resistant to fosfomycin inhibition due to exchange of cysteine for aspartate in the active site
fosfomycin
-
selectively inhibited by fosfomycin, which forms a covalent bond to the sulfhydryl group of the catalytically relevant Cys115 residue
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
-
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
acting competitively as an analogue of phosphoenolpyruvate
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
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
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
-
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
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
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
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
insight into the catalytic mechanism and covalent inhibition by QM/MM MD simulations
-
additional information
inhibitors are identified through computational and in vitro approaches
-
