Information on EC 2.3.1.201 - UDP-2-acetamido-3-amino-2,3-dideoxy-glucuronate N-acetyltransferase

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The enzyme appears in viruses and cellular organisms

EC NUMBER
COMMENTARY hide
2.3.1.201
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RECOMMENDED NAME
GeneOntology No.
UDP-2-acetamido-3-amino-2,3-dideoxy-glucuronate N-acetyltransferase
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REACTION
REACTION DIAGRAM
COMMENTARY hide
ORGANISM
UNIPROT
LITERATURE
acetyl-CoA + UDP-2-acetamido-3-amino-2,3-dideoxy-alpha-D-glucuronate = CoA + UDP-2,3-diacetamido-2,3-dideoxy-alpha-D-glucuronate
show the reaction diagram
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REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
acetylation
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PATHWAY
BRENDA Link
KEGG Link
MetaCyc Link
UDP-2,3-diacetamido-2,3-dideoxy-alpha-D-mannuronate biosynthesis
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Amino sugar and nucleotide sugar metabolism
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SYSTEMATIC NAME
IUBMB Comments
acetyl-CoA:UDP-2-acetamido-3-amino-2,3-dideoxy-alpha-D-glucuronate N-acetyltransferase
This enzyme participates in the biosynthetic pathway for UDP-alpha-D-ManNAc3NAcA (UDP-2,3-diacetamido-2,3-dideoxy-alpha-D-mannuronic acid), an important precursor of B-band lipopolysaccharide.
ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
physiological function
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the enzyme is required for B-band O-antigen biosynthesis in Pseudomonas aeruginosa
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 + UDP-2-acetamido-3-amino-2,3-dideoxy-alpha-D-glucuronate
CoA + UDP-2,3-diacetamido-2,3-dideoxy-alpha-D-glucuronate
show the reaction diagram
additional information
?
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no activity with UDP-GlcNAcA, UDP-GlcNAc, and UDP-2-acetamido-4-amino-2,4,6-trideoxy-D-glucosamine
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COFACTOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
pyridoxal 5'-phosphate
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KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.107
UDP-2-acetamido-3-amino-2,3-dideoxy-alpha-D-glucuronate
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in 50 mM HEPES (pH 8.0), 2.5 mM dithiothreitol, and 2 mM MgCl2, at 30°C
TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
48.3
UDP-2-acetamido-3-amino-2,3-dideoxy-alpha-D-glucuronate
Pseudomonas aeruginosa
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in 50 mM HEPES (pH 8.0), 2.5 mM dithiothreitol, and 2 mM MgCl2, at 30°C
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
pH RANGE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
TEMPERATURE RANGE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
pI VALUE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
8
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pI-value of above 8.0, isoelectric focusing
8.2
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calculated from amino acid sequence
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
61000
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His-tagged enzyme, gel filtration
68180
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MALDI-TOF mass spectrometry
SUBUNITS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
?
x * 22700, predicted from amino acid sequence
homotrimer
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3 * 22726, His-tagged enzyme, calculated from amino acid sequence; 3 * 22726, MALDI-TOF mass spectrometry; 3 * 23000, His-tagged enzyme, SDS-PAGE
trimer
Crystallization/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
hanging drop vapor diffusion method. The enzyme complexed with acetyl-CoA and UDP is crystallized at pH 8.0 in the presence of 100 mM HEPPS, 16-20% (w/v) poly(ethylene glycol) 3400 and 210 mM tetramethylammonium chloride. The enzyme bound to CoA and UDP-2-acetamido-3-amino-2,3-dideoxy-alpha-D-glucuronate is crystallized using 17% (w/v) poly(ethylene glycol) 3400, 300 mM NaCl, 100 mM HEPPS (pH 8.0), 210 mM tetramethylammonium chloride
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QM/MM calculations reveal two sequential steps in the catalyzation process. The nucleophilic attack of the C3-amino group of the substrate on the carbonyl carbon of acetyl-CoA occurs in concert with the departure of CoA from acetyl-CoA, generating a negatively charged CoA and a positively charged intermediate. Subsequently, the sulfur anion of CoA accepts the proton of the positively charged intermediate to yield the final product. Asn84 is important for promoting the catalysis by forming a hydrogen bond with the C3-amino group to position the lone pair of the electrons of the C3-amino group in an ideal orientation for nucleophilic attack and stabilize the transition states and intermediate
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GENERAL STABILITY
ORGANISM
UNIPROT
LITERATURE
incubation of the enzyme with acetyl-CoA significantly enhances the stability of the protein and prevents precipitation over a course of 14 days
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Purification/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
Ni-NTA agarose column chromatography
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Ni-NTA agarose resin column chromatography, gel filtration
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Ni-NTA column chromatography
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nickel-nitrilotriacetic acid-agarose column chromatography
Cloned/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
expressed as an N-terminally histidine-tagged fusion protein in Escherichia coli BL21(DE3) pLysS cells
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expressed in Escherichia coli BL21-CodonPlus(DE3) RIL cells
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expressed in Escherichia coli Rosetta(DE3) cells
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expressed in Escherichia coli Tuner(DE3) cells
ENGINEERING
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
K136A
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the mutation reduces the stabilizing effects of acetyl-CoA
K136R
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the mutation showed no discernible effect the stabilizing effects of acetyl-CoA on the purified mutant protein