Information on EC 2.7.1.176 - UDP-N-acetylglucosamine kinase

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The enzyme appears in viruses and cellular organisms

EC NUMBER
COMMENTARY hide
2.7.1.176
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RECOMMENDED NAME
GeneOntology No.
UDP-N-acetylglucosamine kinase
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REACTION
REACTION DIAGRAM
COMMENTARY hide
ORGANISM
UNIPROT
LITERATURE
ATP + UDP-N-acetyl-alpha-D-glucosamine = ADP + UDP-N-acetyl-alpha-D-glucosamine 3'-phosphate
show the reaction diagram
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SYSTEMATIC NAME
IUBMB Comments
ATP:UDP-N-acetyl-D-glucosamine 3'-phosphotransferase
Toxic component of a toxin-antitoxin (TA) module. The phosphorylation of UDP-N-acetyl-D-glucosamine results in the inhibition of EC 2.5.1.7, UDP-N-acetylglucosamine 1-carboxyvinyltransferase, the first committed step in cell wall synthesis, which is then blocked. The activity of this enzyme is inhibited when the enzyme binds to the cognate epsilon antitoxin.
ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
and several other isogenic strains
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Manually annotated by BRENDA team
and several other isogenic strains
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Manually annotated by BRENDA team
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Manually annotated by BRENDA team
GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
evolution
malfunction
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PezT inhibition renders the host-cell capable to actively control toxin release
metabolism
physiological function
additional information
SUBSTRATE
PRODUCT                       
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
ATP + UDP-N-acetyl-D-glucosamine
ADP + UDP-N-acetyl-D-glucosamine 3'-phosphate
show the reaction diagram
additional information
?
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NATURAL SUBSTRATES
NATURAL PRODUCTS
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
ATP + UDP-N-acetyl-D-glucosamine
ADP + UDP-N-acetyl-D-glucosamine 3'-phosphate
show the reaction diagram
additional information
?
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neutralization of the bacteriotoxic protein PezT is carried out by complex formation with its cognate antitoxin PezA, proteolytic resistance of PezA once bound to PezT
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COFACTOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
METALS and IONS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
INHIBITORS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
additional information
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neutralization of the bacteriotoxic protein PezT is carried out by complex formation with its cognate antitoxin PezA, proteolytic resistance of PezA once bound to PezT
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ACTIVATING COMPOUND
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
RelA
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contributes to enforce toxin-induced dormanc. After induction of the zetaY83C toxin the expression of the relA gene is induced. Disruption of RelA is pleotropic, leading to poor growth and accumulation of phenotypic suppressors that increase expression of the other (p)ppGpp synthetase genes, ssa1 and ssa2
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additional information
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PezAT activation of toxin by antitoxin displacement
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KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
additional information
additional information
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association and dissociation kinetics of the PezAT complex, with wild-type and mutant D66T PezT, stopped-flow measurements, femtomolar affinity of PezA and PezT, detailed kinetic analysis of the PezAT interaction determined using rapid mixing methods and time-resolved size exclusion chromatography, overview
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TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
Crystallization/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
analysis of the crystal structure of the epsilon/zeta toxin-antitoxin complex bound to UDP-N-acetyl-D-glucosamine at 2.7 A resolution
purified recombinant wild-type and selenomethionine-derivated epsilon2/zeta2 protein complexes, X-ray diffraction structure determination and analysis at 1.95 A and 3.1 A resolution, respectively, multiple anomalous diffraction, modeling
GENERAL STABILITY
ORGANISM
UNIPROT
LITERATURE
overall stability of the chromosomally encoded PezAT TA system, overview. High affinity of PezAT and the resulting stabilization of PezA upon complex formation with PezT seem to impair toxin release by simple dissociation
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Purification/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
recombinant fused His-tagged PezT with His-tagged PezA from Escherichia coli BL21(DE3) by nickel affinity chromatography, PezA is cleaved off by thrombin, followed by anion exchange and gel filtration to purifiy PezT and PezA, quantitative real-time RT PCR expression analysis
recombinant His-tagged wild-type and mutant enzymes with or without PezA from Escherichia coli strain BL21(DE3) by nickel affinity chromatography
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recombinant truncated variant PezTDELTAC242 from Escherichia coli strain BL21(DE3)
Cloned/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
DNA and amino acid sequence comparisons
expression of His-tagged wild-type and mutant enzymes with or without PezA in Escherichia coli strain BL21(DE3)
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expression of zeta toxin in Escherichia coli under control of the LacI repressor-Hyper-Spank promoter using vector pDR111
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gene pezT, DNA and amino acid sequence determination and analysis, expression of truncated variant PezTDELTAC242 in Escherichia coli strain BL21(DE3)
gene pezT, DNA and amino acid sequence determination and analysis, sequence comparison, co-expression of fused His-tagged PezT with His-tagged PezA in Escherichia coli BL21(DE3). The PezA antitoxin represses transcription from PpezAT and the PezT toxin acts as a co-repressor
the gene is encoded in plasmid pSM19035. The omega-epsilon-zeta operon of this plasmid constitutes a proteic plasmid addiction system in which the epsilon and zeta genes encode an antitoxin and toxin, respectively, while omega plays an autoregulatory function
ENGINEERING
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
D66T/W232Y
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site-directed mutagenesis, a mutated tryptophan-free PezT variant
K45A
site-directed mutagenesis, the mutation abolishes PezT lethality
R157A
site-directed mutagenesis, the mutation abolishes PezT lethality
R170A
site-directed mutagenesis, the mutation abolishes PezT lethality
T117V
site-directed mutagenesis, the mutation abolishes PezT lethality
T120V
site-directed mutagenesis, the mutation abolishes PezT lethality and a delay in the growth inhibition
A111C
deletion of one A in the AAAAAAA tract, which begins at the 78-nt position, results in a frameshift and the stop codon formation after 51 codons, additional mutations are insertion of G after A32 and A111C substitution in one case and A248G substitution in the second one
A248G
deletion of one A in the AAAAAAA tract, which begins at the 78-nt position, results in a frameshift and the stop codon formation after 51 codons, additional mutations are insertion of G after A32 and A111C substitution in one case and A248G substitution in the second one
D66T
site-directed mutagenesis, a nontoxicPezT variant, no bulge formation or lysis after induction of PezT D66T
D67T
site-directed mutagenesis
K46A
site-directed mutagenesis, the change in the Walker A motif enables cloning and expression of genes K46A and D67T in Escherichia coli without coexpression of the antagonistic gene epsilon
K46A/D67T
site-directed mutagenesis, the change in the Walker A motif enables cloning and expression of genes K46A and D67T in Escherichia coli without coexpression of the antagonistic gene epsilon
R158A
site-directed mutagenesis, the mutant construct can be cloned into Escherichia coli but not overexpressed
R158A/R171S
site-directed mutagenesis, the mutant can be cloned and expressed
R171S
site-directed mutagenesis
additional information