Information on EC 2.3.1.209 - dTDP-4-amino-4,6-dideoxy-D-glucose acyltransferase

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The enzyme appears in viruses and cellular organisms

EC NUMBER
COMMENTARY hide
2.3.1.209
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RECOMMENDED NAME
GeneOntology No.
dTDP-4-amino-4,6-dideoxy-D-glucose acyltransferase
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REACTION
REACTION DIAGRAM
COMMENTARY hide
ORGANISM
UNIPROT
LITERATURE
acetyl-CoA + dTDP-4-amino-4,6-dideoxy-alpha-D-glucose = CoA + dTDP-4-acetamido-4,6-dideoxy-alpha-D-glucose
show the reaction diagram
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PATHWAY
BRENDA Link
KEGG Link
MetaCyc Link
dTDP-N-acetylviosamine biosynthesis
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SYSTEMATIC NAME
IUBMB Comments
acetyl-CoA:dTDP-4-amino-4,6-dideoxy-alpha-D-glucose N-acetyltransferase
The non-activated product, 4-acetamido-4,6-dideoxy-alpha-D-glucose, is part of the O antigens of Shigella dysenteriae type 7 and Escherichia coli O7.
ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
O7 type strain
UniProt
Manually annotated by BRENDA team
O7 type strain
UniProt
Manually annotated by BRENDA team
pv. tabaci, gene vioB
UniProt
Manually annotated by BRENDA team
pv. tabaci, gene vioB
UniProt
Manually annotated by BRENDA team
serotype 7 type strain, gene vioB
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Manually annotated by BRENDA team
GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
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
acetyl-CoA + dTDP-4-amino-4,6-dideoxy-alpha-D-glucose
CoA + dTDP-4-acetamido-4,6-dideoxy-alpha-D-glucose
show the reaction diagram
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
acetyl-CoA + dTDP-4-amino-4,6-dideoxy-alpha-D-glucose
CoA + dTDP-4-acetamido-4,6-dideoxy-alpha-D-glucose
show the reaction diagram
COFACTOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
acetyl-CoA
METALS and IONS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
additional information
no effect by presence of Mg2+, Ca2+, Mn2+, and Co2+or EDTA on enzyne activity, the enzyme is divalent cation-independent
INHIBITORS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
Fe2+
96% inhibition at 5 mM
KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.554
acetyl-CoA
pH 7.4, 37C, recombinant His-tagged enzyme
0.142
dTDP-4-amino-4,6-dideoxy-alpha-D-glucose
pH 7.4, 37C, recombinant His-tagged enzyme
TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
21.6
acetyl-CoA
Escherichia coli
Q9XCW3
pH 7.4, 37C, recombinant His-tagged enzyme
155.3
dTDP-4-amino-4,6-dideoxy-alpha-D-glucose
Escherichia coli
Q9XCW3
pH 7.4, 37C, recombinant His-tagged enzyme
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
TEMPERATURE RANGE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
4 - 65
activity range, complete substrate conversion at 25-50C
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
27100
x * 27100, recombinant His-tagged enzyme, SDS-PAGE
SUBUNITS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
Purification/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
recombinant His-tagged enzyme from Escherichia coli strain BL21(DE3) by nickel affinity chromatography
Cloned/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
DNA and amino acid sequence determination and analysis
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from strain G1112, DNA and amino acid sequence determination and analysis, overexpression of the His-tagged enzyme in Escherichia coli strain BL21(DE3)
gene vioB, DNA and amino acid sequence determination and analysis
ENGINEERING
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
additional information
APPLICATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
drug development