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IUBMB Comments A pyridoxal-phosphate protein. The enzyme is involved in biosynthesis of UDP-N,N'-diacetylbacillosamine, an intermediate in protein glycosylation pathways in several bacterial species, including N-linked glycosylation of certain L-asparagine residues in Campylobacter species [2-4] and O-linked glycosylation of certain L-serine residues in Neisseria species .
The enzyme appears in viruses and cellular organisms
Synonyms
cj1121c,
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aminotransferase, uridine diphospho-4-amino-2-acetamido-2,4,6-trideoxyglucose
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UDP-4-keto-6-deoxy-GlcNAc C4 aminotransferase
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uridine diphospho-4-amino-2-acetamido-2,4,6-trideoxyglucose aminotransferase
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PglE
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UDP-N-acetylbacillosamine + 2-oxoglutarate = UDP-2-acetamido-2,6-dideoxy-alpha-D-xylo-hex-4-ulose + L-glutamate
UDP-N-acetylbacillosamine + 2-oxoglutarate = UDP-2-acetamido-2,6-dideoxy-alpha-D-xylo-hex-4-ulose + L-glutamate
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UDP-N-acetylbacillosamine + 2-oxoglutarate = UDP-2-acetamido-2,6-dideoxy-alpha-D-xylo-hex-4-ulose + L-glutamate
A pyridoxal-phosphate protein
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UDP-N-acetylbacillosamine + 2-oxoglutarate = UDP-2-acetamido-2,6-dideoxy-alpha-D-xylo-hex-4-ulose + L-glutamate
A pyridoxal-phosphate protein.
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amino group transfer
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UDP-4-amino-4,6-dideoxy-N-acetyl-alpha-D-glucosamine:2-oxoglutarate aminotransferase
A pyridoxal-phosphate protein. The enzyme is involved in biosynthesis of UDP-N,N'-diacetylbacillosamine, an intermediate in protein glycosylation pathways in several bacterial species, including N-linked glycosylation of certain L-asparagine residues in Campylobacter species [2-4] and O-linked glycosylation of certain L-serine residues in Neisseria species [5].
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UDP-2-acetamido-2,6-dideoxy-alpha-D-xylo-4-hexulose + L-glutamate
UDP-4-amino-4,6-dideoxy-alpha-D-N-acetyl-D-glucosamine + 2-oxoglutarate
UDP-2-acetamido-4-keto-2,6-dideoxyhexose + L-glutamate
UDP-2-acetamido-4-amino-2,4,6-trideoxyhexose + 2-oxoglutarate
UDP-2-acetamido-2,6-dideoxy-alpha-D-xylo-4-hexulose + L-glutamate
UDP-4-amino-4,6-dideoxy-alpha-D-N-acetyl-D-glucosamine + 2-oxoglutarate
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UDP-2-acetamido-2,6-dideoxy-alpha-D-xylo-4-hexulose + L-glutamate
UDP-4-amino-4,6-dideoxy-alpha-D-N-acetyl-D-glucosamine + 2-oxoglutarate
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the enzyme is involved in the biosynthesis of an undecaprenyl diphosphate-linked disaccharide
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UDP-2-acetamido-2,6-dideoxy-alpha-D-xylo-4-hexulose + L-glutamate
UDP-4-amino-4,6-dideoxy-alpha-D-N-acetyl-D-glucosamine + 2-oxoglutarate
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UDP-2-acetamido-2,6-dideoxy-alpha-D-xylo-4-hexulose + L-glutamate
UDP-4-amino-4,6-dideoxy-alpha-D-N-acetyl-D-glucosamine + 2-oxoglutarate
the enzyme (Cj1121c) is involved in biosynthesis of bacillosamine
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UDP-2-acetamido-2,6-dideoxy-alpha-D-xylo-4-hexulose + L-glutamate
UDP-4-amino-4,6-dideoxy-alpha-D-N-acetyl-D-glucosamine + 2-oxoglutarate
the enzyme (Cj1121c) does not utilize UDP-2-acetamido-2,6-dideoxy-beta-L-arabino-hex-4-ulose as substrate
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UDP-2-acetamido-4-keto-2,6-dideoxyhexose + L-glutamate
UDP-2-acetamido-4-amino-2,4,6-trideoxyhexose + 2-oxoglutarate
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UDP-2-acetamido-4-keto-2,6-dideoxyhexose + L-glutamate
UDP-2-acetamido-4-amino-2,4,6-trideoxyhexose + 2-oxoglutarate
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glutamate can only partially be replaced by glutamine and cannot be replaced by asparagine and aspartate
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UDP-2-acetamido-2,6-dideoxy-alpha-D-xylo-4-hexulose + L-glutamate
UDP-4-amino-4,6-dideoxy-alpha-D-N-acetyl-D-glucosamine + 2-oxoglutarate
UDP-2-acetamido-4-keto-2,6-dideoxyhexose + L-glutamate
UDP-2-acetamido-4-amino-2,4,6-trideoxyhexose + 2-oxoglutarate
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UDP-2-acetamido-2,6-dideoxy-alpha-D-xylo-4-hexulose + L-glutamate
UDP-4-amino-4,6-dideoxy-alpha-D-N-acetyl-D-glucosamine + 2-oxoglutarate
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UDP-2-acetamido-2,6-dideoxy-alpha-D-xylo-4-hexulose + L-glutamate
UDP-4-amino-4,6-dideoxy-alpha-D-N-acetyl-D-glucosamine + 2-oxoglutarate
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the enzyme is involved in the biosynthesis of an undecaprenyl diphosphate-linked disaccharide
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UDP-2-acetamido-2,6-dideoxy-alpha-D-xylo-4-hexulose + L-glutamate
UDP-4-amino-4,6-dideoxy-alpha-D-N-acetyl-D-glucosamine + 2-oxoglutarate
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UDP-2-acetamido-2,6-dideoxy-alpha-D-xylo-4-hexulose + L-glutamate
UDP-4-amino-4,6-dideoxy-alpha-D-N-acetyl-D-glucosamine + 2-oxoglutarate
the enzyme (Cj1121c) is involved in biosynthesis of bacillosamine
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pyridoxal 5'-phosphate
a pyridoxal 5'-phosphate protein
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additional information
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not affected by MgCl2 at 0.01 M
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pyridoxal 5'-phosphate
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absolute requirement
additional information
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not affected by EDTA
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0.048
UDP-2-acetamido-2,6-dideoxy-alpha-D-xylo-4-hexulose
pH 7.7, 37°C
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2.4
UDP-2-acetamido-2,6-dideoxy-alpha-D-xylo-4-hexulose
pH 7.7, 37°C
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37
assay at
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UniProt
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UniProt
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type XIV, ATCC 6314
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structure of PglE in complex with an external aldimine, to 2.0 A resolution. In presence of the external aldimine, a dramatic movement of the loops defined by Ser24 to Gly31 and Tyr180 to Gly190 takes place. Comparison of PglE to sugar aminotransferases PseC, DesI, and ArnB
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-15°C, stable for at least 3 weeks
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type XIV, ATCC 6314, partial
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expression in Escherichia coli
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Distler, J.; Kaufman, B.; Roseman, S.
Enzymic synthesis of a diamino sugar nucleotide by extracts of type XIV Diplococcus pneumoniae
Arch. Biochem. Biophys.
116
466-478
1966
Streptococcus pneumoniae
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Schoenhofen, I.C.; McNally, D.J.; Vinogradov, E.; Whitfield, D.; Young, N.M.; Dick, S.; Wakarchuk, W.W.; Brisson, J.R.; Logan, S.M.
Functional characterization of dehydratase/aminotransferase pairs from Helicobacter and Campylobacter: enzymes distinguishing the pseudaminic acid and bacillosamine biosynthetic pathways
J. Biol. Chem.
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723-732
2006
Campylobacter jejuni subsp. jejuni (Q0P9D3)
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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
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Morrison, J.P.; Troutman, J.M.; Imperiali, B.
Development of a multicomponent kinetic assay of the early enzymes in the Campylobacter jejuni N-linked glycosylation pathway
Bioorg. Med. Chem.
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8167-8171
2010
Campylobacter jejuni
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Riegert, A.S.; Young, N.M.; Watson, D.C.; Thoden, J.B.; Holden, H.M.
Structure of the external aldimine form of PglE, an aminotransferase required for N,N-diacetylbacillosamine biosynthesis
Protein Sci.
24
1609-1616
2015
Campylobacter jejuni subsp. jejuni (Q0P9D3), Campylobacter jejuni subsp. jejuni ATCC 700819 (Q0P9D3)
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