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Information on EC 2.3.1.203 - UDP-N-acetylbacillosamine N-acetyltransferase and Organism(s) Campylobacter jejuni and UniProt Accession Q0P9D1

for references in articles please use BRENDA:EC2.3.1.203
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IUBMB Comments
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 .
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This record set is specific for:
Campylobacter jejuni
UNIPROT: Q0P9D1
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The taxonomic range for the selected organisms is: Campylobacter jejuni
The enzyme appears in selected viruses and cellular organisms
Synonyms
cj1123c, more
SYNONYM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
PATHWAY SOURCE
PATHWAYS
-
-
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].
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-glucose
CoA + UDP-N,N'-diacetylbacillosamine
show the reaction diagram
-
-
-
?
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-4-amino-4,6-dideoxy-N-acetyl-alpha-D-glucosamine
CoA + UDP-N,N'-diacetylbacillosamine
show the reaction diagram
-
-
i.e. UDP-2,4-diacetamido-2,4,6-trideoxy-alpha-D-glucopyranose
-
?
KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.41
UDP-4-amino-4,6-dideoxy-N-acetyl-alpha-D-glucosamine
-
at 37°C, pH 7.7
TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
8050
UDP-4-amino-4,6-dideoxy-N-acetyl-alpha-D-glucosamine
-
at 37°C, pH 7.7
kcat/KM VALUE [1/mMs-1]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
20000
UDP-4-amino-4,6-dideoxy-N-acetyl-alpha-D-glucosamine
-
at 37°C, pH 7.7
ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY hide
GeneOntology No.
LITERATURE
SOURCE
GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
metabolism
-
the enzyme catalyzes the final step in N,N'-diacetylbacillosamine synthesis by N-acetylation of UDP-4-amino-4,6-dideoxy-N-acetyl-alpha-D-glucosamine at the C4 position
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
22025
2 * 22025, electrospray ionization mass spectrometry
62700
gel filtration
23500
-
x * 23500, His-tagged enzyme, SDS-PAGE
SUBUNIT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
homotrimer
2 * 22025, electrospray ionization mass spectrometry
?
-
x * 23500, His-tagged enzyme, SDS-PAGE
CRYSTALLIZATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
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 30°C
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
-
REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Olivier, N.B.; Chen, M.M.; Behr, J.R.; Imperiali, B.
In vitro biosynthesis of UDP-N,N'-diacetylbacillosamine by enzymes of the Campylobacter jejuni general protein glycosylation system
Biochemistry
45
13659-13669
2006
Campylobacter jejuni, Campylobacter jejuni NCTC 11168
Manually annotated by BRENDA team
Rangarajan, E.S.; Ruane, K.M.; Sulea, T.; Watson, D.C.; Proteau, A.; Leclerc, S.; Cygler, M.; Matte, A.; Young, N.M.
Structure and active site residues of PglD, an N-acetyltransferase from the bacillosamine synthetic pathway required for N-glycan synthesis in Campylobacter jejuni
Biochemistry
47
1827-1836
2008
Campylobacter jejuni (Q0P9D1)
Manually annotated by BRENDA team
Ding, W.; Nothaft, H.; Szymanski, C.M.; Kelly, J.
Identification and quantification of glycoproteins using ion-pairing normal-phase liquid chromatography and mass spectrometry
Mol. Cell. Proteomics
8
2170-2185
2009
Campylobacter jejuni, Campylobacter jejuni NCTC 11168
Manually annotated by BRENDA team