Information on EC 2.3.1.203 - UDP-N-acetylbacillosamine N-acetyltransferase

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The enzyme appears in viruses and cellular organisms

EC NUMBER
COMMENTARY hide
2.3.1.203
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RECOMMENDED NAME
GeneOntology No.
UDP-N-acetylbacillosamine N-acetyltransferase
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REACTION
REACTION DIAGRAM
COMMENTARY hide
ORGANISM
UNIPROT
LITERATURE
acetyl-CoA + UDP-N-acetylbacillosamine = CoA + UDP-N,N'-diacetylbacillosamine
show the reaction diagram
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PATHWAY
BRENDA Link
KEGG Link
MetaCyc Link
UDP-N,N'-diacetylbacillosamine biosynthesis
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Amino sugar and nucleotide sugar metabolism
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SYSTEMATIC NAME
IUBMB Comments
acetyl-CoA:UDP-4-amino-4,6-dideoxy-N-acetyl-alpha-D-glucosamine N-acetyltransferase
The product, UDP-N,N'-diacetylbacillosamine, is an intermediate in protein glycosylation pathways in several bacterial species, including N-linked glycosylation of certain L-asparagine residues in Campylobacter species [1,2] and O-linked glycosylation of certain L-serine residues in Neisseria species [3].
GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
metabolism
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-4-amino-2,4,6-trideoxy-alpha-D-glucopyranose
CoA + UDP-2,4-diacetamido-2,4,6-trideoxy-alpha-D-glucopyranose
show the reaction diagram
acetyl-CoA + UDP-2-acetamido-4-amino-2,4,6-trideoxy-alpha-D-glucose
CoA + UDP-N,N'-diacetylbacillosamine
show the reaction diagram
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?
acetyl-CoA + UDP-4-amino-4,6-dideoxy-N-acetyl-alpha-D-glucosamine
CoA + UDP-N,N'-diacetylbacillosamine
show the reaction diagram
COFACTOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
NADH
-
dependent on
KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.09 - 4.6
UDP-2-acetamido-4-amino-2,4,6-trideoxy-alpha-D-glucopyranose
0.41
UDP-4-amino-4,6-dideoxy-N-acetyl-alpha-D-glucosamine
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at 37C, pH 7.7
TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
1200 - 510000
UDP-2-acetamido-4-amino-2,4,6-trideoxy-alpha-D-glucopyranose
8050
UDP-4-amino-4,6-dideoxy-N-acetyl-alpha-D-glucosamine
Campylobacter jejuni
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at 37C, pH 7.7
kcat/KM VALUE [1/mMs-1]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
800 - 730000
UDP-2-acetamido-4-amino-2,4,6-trideoxy-alpha-D-glucopyranose
171534
20000
UDP-4-amino-4,6-dideoxy-N-acetyl-alpha-D-glucosamine
Campylobacter jejuni
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at 37C, pH 7.7
28627
LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY hide
GeneOntology No.
LITERATURE
SOURCE
PDB
SCOP
CATH
ORGANISM
UNIPROT
Campylobacter jejuni subsp. jejuni serotype O:2 (strain ATCC 700819 / NCTC 11168)
Campylobacter jejuni subsp. jejuni serotype O:2 (strain ATCC 700819 / NCTC 11168)
Campylobacter jejuni subsp. jejuni serotype O:2 (strain ATCC 700819 / NCTC 11168)
Campylobacter jejuni subsp. jejuni serotype O:2 (strain ATCC 700819 / NCTC 11168)
Campylobacter jejuni subsp. jejuni serotype O:2 (strain ATCC 700819 / NCTC 11168)
Campylobacter jejuni subsp. jejuni serotype O:2 (strain ATCC 700819 / NCTC 11168)
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
62700
gel filtration
SUBUNITS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
homotrimer
2 * 22025, electrospray ionization mass spectrometry
Crystallization/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
compared to isoforms PglD and PglB, WeeI contains an additional loop (Gln174-Pro180) that forms the substrate binding pocket near the pyranose moiety. Residue Gln174 seems to be critical for catalysis. When aligned to the PglD UDP-4-amino structure, this position is analogous to Asn162 that interacts with the carbonyl oxygen of the pyranose C2-acetyl group. In the WeeI apo-structure, Gln174 is within 5 A of the catalytic base His138 and 3.6 A of the AcCoA thioester
apoenzyme or in complex with CoA, hanging drop vapor diffusion method, using 0.1 M sodium acetate (pH 4.5) and 1.9 M ammonium sulfate, at 30C
apo-crystal structures of the acetyltransferase domain ATD and in complex with AcCoA. The N-terminal section (Asn199-Leu285) comprises a binding pocket for the UDP-4-amino sugar substrate through a beta-alpha-beta-alpha-beta Rossman fold motif. The C-terminus (Pro286-Leu403) is composed of a left-handed beta-helix motif that, in conjunction with an adjacent PglB-ATD protomer in the trimeric state, forms an extended cleft that is utilized for AcCoA binding
Purification/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
HisTrap column chromatography and Superdex 200 gel filtration
Ni-NTA resin column chromatography
Cloned/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
expressed in Escherichia coli AD202 cells
expressed in Escherichia coli BL21 (DE3) pLysS cells
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expressed in Escherichia coli BL21 cells
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ENGINEERING
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
F13A
active site mutant, strong loss of activity
Q174A
active site mutant, strong loss of activity
T176A
active site mutant, strong loss of activity
F13A
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active site mutant, strong loss of activity
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Q174A
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active site mutant, strong loss of activity
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T176A
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active site mutant, strong loss of activity
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D332A
active site mutant, strong loss of activity
H210F
active site mutant, strong loss of activity
Q369A
active site mutant, strong loss of activity
Q370A
active site mutant, 50% loss of activity
D332A
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active site mutant, strong loss of activity
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H210F
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active site mutant, strong loss of activity
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Q369A
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active site mutant, strong loss of activity
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Q370A
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active site mutant, 50% loss of activity
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