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Information on EC 2.5.1.7 - UDP-N-acetylglucosamine 1-carboxyvinyltransferase and Organism(s) Escherichia coli and UniProt Accession P0A749
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EC Tree
2.5.1.7 UDP-N-acetylglucosamine 1-carboxyvinyltransferaseSpecify your search results
Word Map
- 2.5.1.7
- peptidoglycan
- fosfomycin
- pep
- cloacae
- enterobacter
- medicine
- epsps
- drug development
-
5-enolpyruvylshikimate
- sanguinis
- 5-enolpyruvylshikimate-3-phosphate
The taxonomic range for the selected organisms is: Escherichia coli
The expected taxonomic range for this enzyme is: Bacteria, Archaea, Eukaryota
The expected taxonomic range for this enzyme is: Bacteria, Archaea, Eukaryota
Reaction Schemes
Synonyms
udp-n-acetylglucosamine enolpyruvyl transferase, mura enzyme, muraa, udp-n-acetylglucosamine 1-carboxyvinyltransferase, udp-n-acetylglucosamine enolpyruvyltransferase, udp-nag enolpyruvyl transferase, udp-n-acetylglucosamine 1-carboxyvinyl-transferase, udp-glcnac enolpyruvyl transferase, udp-n-acetylglucosamine 1-carboxyvinyl transferase, udp-n-acetylglucosamine enolpyruvyle transferase, 
more
topSYNONYM 
ORGANISM
UNIPROT
COMMENTARY 
LITERATURE
enoylpyruvate transferase
-
-
-
-
enoylpyruvatetransferase
-
-
-
-
MurA
MurA transferase
-
-
-
-
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-N-acetylglucosamine 1-carboxyvinyl-transferase
UDP-N-acetylglucosamine enoylpyruvyltransferase
-
-
-
-
UDP-N-acetylglucosamine 1-carboxyvinyl-transferase
-
-
-
-
REACTION
REACTION DIAGRAM
COMMENTARY
ORGANISM
UNIPROT
LITERATURE
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
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
Cys115 is the active site nucleophile
-
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
-
REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
carboxyvinyl group transfer
-
-
-
-
PATHWAY SOURCE
PATHWAYS
BRENDA
-
-, -, -, -
SYSTEMATIC NAME
IUBMB Comments
phosphoenolpyruvate:UDP-N-acetyl-D-glucosamine 1-carboxyvinyltransferase
-
CAS REGISTRY NUMBER
COMMENTARY
9023-27-2
-
SUBSTRATE
PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate)
(Substrate)
LITERATURE
(Substrate)
(Substrate)
COMMENTARY
(Product)
(Product)
LITERATURE
(Product)
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
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
-
-
-
r
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
UDP-N-acetyl-3-O-(1-carboxyvinyl)-D-glucosamine + phosphate
-
-
-
-
r
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-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
-
-
?
NATURAL SUBSTRATE
NATURAL PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate)
(Substrate)
LITERATURE
(Substrate)
(Substrate)
COMMENTARY
(Product)
(Product)
LITERATURE
(Product)
(Product)
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
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-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-D-glucosamine
phosphate + UDP-N-acetyl-3-(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 step in the biosynthesis of the bacterial cell wall
-
-
?
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
-
-
?
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
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
-
6,7-dimethoxy-2-[4-(2-phenylethyl)piperazin-1-yl]-3,4-dihydronaphthalen-1(2H)-one
-
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
phosphonomycin
irreversible inactivation, requires the presence of UDP-GlcNAc
-
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
Fe2+
-
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
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
-
above 1 mM
Zn2+
-
metal ions do not enhance the activity of enzymes, activity is inhibited by 10 mM
fosfomycin
enolpyruvyl UDP-GlcNAc synthase is an antimicrobial target that is inhibited by the antibiotic fosfomycin
fosfomycin
acting competitively as an analogue of phosphoenolpyruvate
(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
(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
(Z)-3-fluorophosphoenolpyruvate
-
wild-type and mutant C115D, competitive against phosphoenolpyruvate
fosfomycin
-
selectively inhibited by fosfomycin, which forms a covalent bond to the sulfhydryl group of the catalytically relevant Cys115 residue
phosphonomycin
-
irreversible inactivation, requires the presence of UDP-GlcNAc
-
additional information
insight into the catalytic mechanism and covalent inhibition by QM/MM MD simulations
-
ACTIVATING COMPOUND
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
0.015
UDP-N-acetyl-D-glucosamine
pH and temperature not specified in the publication
0.004
phosphoenolpyruvate
pH and temperature not specified in the publication
TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
1.8
UDP-N-acetyl-D-glucosamine
-
the calculated value for UDP is 40 times higher than that of ADP
3.8
phosphoenolpyruvate
pH and temperature not specified in the publication
3.8
UDP-N-acetyl-D-glucosamine
pH and temperature not specified in the publication
kcat/KM VALUE [1/mMs-1]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
0.01
phosphoenolpyruvate
pH and temperature not specified in the publication
0.00025
UDP-N-acetyl-D-glucosamine
pH and temperature not specified in the publication
520000
additional information
MurA-catalyzed breakdown of its tetrahedral intermediate at pH 7.5, second-order rate constant
-
570000
additional information
MurA-catalyzed breakdown of its tetrahedral intermediate at pH 10.0
-
6000000
additional information
MurA-catalyzed breakdown of its tetrahedral intermediate at pH 5.0
-
Ki VALUE [mM]
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
IC50 VALUE [mM]
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
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
-
0.02256
6,7-dimethoxy-2-[4-(2-phenylethyl)piperazin-1-yl]-3,4-dihydronaphthalen-1(2H)-one
Escherichia coli
-
0.002
(+/-)-tulipaline B
Escherichia coli
-
pH and temperature not specified in the publication
0.00853
2-(4-methylpiperazin-1-yl)-3,4-dihydronaphthalen-1(2H)-one
Escherichia coli
-
pH and temperature not specified in the publication
0.0028
2-bromo-5-[(Z)-2-bromo-2-nitroethenyl]furan
Escherichia coli
-
pH and temperature not specified in the publication
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
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
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
0.00196
2-oxo-1,3-benzoxathiol-6-yl benzenesulfonate
Escherichia coli
-
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
0.00095
5,7-dibromo-6-hydroxy-1,3-benzoxathiol-2-one
Escherichia coli
-
in 50 mM Tris-HCl, pH 7.9, at 37°C
0.00801
5-(prop-2-en-1-yloxy)-1,3-benzoxathiol-2-one
Escherichia coli
-
in 50 mM Tris-HCl, pH 7.9, at 37°C
0.00727
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
5-hydroxybenzo[d][1,3]oxathiol-2-one
Escherichia coli
-
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
0.00155
5-hydroxynaphtho[2,1-d][1,3]oxathiol-2-one
Escherichia coli
-
in 50 mM Tris-HCl, pH 7.9, at 37°C
0.00645
5-methoxybenzo[d][1,3]oxathiol-2-one
Escherichia coli
-
in 50 mM Tris-HCl, pH 7.9, at 37°C
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
0.00025
2-oxo-1,3-benzoxathiol-6-yl sulfamate
Escherichia coli
-
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
0.00028
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
0.00077
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
0.0051
fosfomycin
Escherichia coli
-
enzyme shows 5-7fold shift in IC50 for the inhibitor upon pre-incubation with the substrate UDP-N-acetyl-D-glucosamine
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
pH RANGE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
37
ORGANISM
COMMENTARY
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
murA instead of murZ is recommended to be used to designate the gene at 69.3 min of the chromosome
SwissProt
LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY
GeneOntology No.
LITERATURE
SOURCE
GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
drug target
catalyzes the first step in the biosynthesis of the bacterial cell wall. This pathway is essential for the growth of bacteria but missing in mammals, that nominates MurA as an attractive antibacterial target
metabolism
physiological function
malfunction
-
gram-negative bacteria have only one copy of the murA gene, its deletion is lethal
physiological function
-
enzyme catalyzes the first committed step of bacterial cell wall biosynthesis
metabolism
the enzyme catalyzes the first step in the biosynthesis of the bacterial cell wall
metabolism
the enzyme catalyzes the first step of peptidoglycan biosynthesis pathway which is essential in the bacterial cell wall composition
physiological function
catalyzes the first committed step in peptidoglycan biosynthesis
physiological function
the enzyme catalyzes the first committed step in the biosynthesis of peptidoglycan, an integral and essential component of the bacterial cell wall
physiological function
the enzyme catalyzes the first step of peptidoglycan biosynthesis pathway which is essential in the bacterial cell wall composition
PDB
SCOP
CATH
UNIPROT
ORGANISM
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
89000
-
as fusion protein with maltose binding protein, determined by SDS-PAGE
SUBUNIT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
monomer
it appears to be a monomer in solution, even at high concentrations
additional information
-
two-domain structure with the active site located between them, substrate binding structure
CRYSTALLIZATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
in complex with inhibitor cnicin and substrate UDP-N-acetylglucosamine, at 2.0 A resolution. The enzyme catalyzes the formation of a covalent adduct between cnicin and 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
MurA is crystallized in the presence of sodium phosphite and UDP-N-acetylmuramic acid using the hanging drop vapor diffusion method, the MurA cocrystal structure with UDP-N-acetylmuramic acid and phosphite reveals a new staged MurA conformation in which the Arg397 side chain tracked phosphite out of the catalytic site
crystallization of the enzyme complexed with UDP-N-acetylglucosamine and fosfomycin, two-domain structure with the active site located between them, structure and substrate binding analysis
-
PROTEIN VARIANTS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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
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
additional information
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
GENERAL STABILITY
ORGANISM
UNIPROT
LITERATURE
PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
purified protein has significant amounts of UDP-N-acteylmuramic acid bound
-
CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
DNA and amino acid sequence determination and analysis, chromosome mapping at 69.3 min, overexpression in Escherichia coli strain JLM 16
expression from plasmid in Escherichia coli deletion mutant, functional complementation
cloning and expression of MurA using pMAL expression system in frame with the fusion maltose binding protein in Escherichia coli BL21
-
APPLICATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
drug development
-
enzyme is an ideal target for the discovery of novel antibiotics against gram-negative pathogens as they have only one copy of murA gene in its genome
medicine
REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
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, Bacillus cereus T, Escherichia coli, Escherichia coli K-235
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
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
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
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Escherichia coli, Escherichia coli MurZ
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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
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Escherichia coli, Escherichia coli MurZ
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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
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
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
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
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
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
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
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)
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)
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)
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
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
Enterobacter cloacae (P33038), Escherichia coli (P0A749), Mycobacterium tuberculosis (P9WJM1), Mycobacterium tuberculosis H37Rv (P9WJM1), Pseudomonas aeruginosa, Staphylococcus aureus, Streptococcus pneumoniae
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, Escherichia coli JM109, Staphylococcus aureus, Staphylococcus aureus SH1000
Hrast, M.; Sosic, I.; Sink, R.; Gobec, S.
Inhibitors of the peptidoglycan biosynthesis enzymes MurA-F
Bioorg. Chem.
55
2-15
2014
Escherichia coli
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
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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