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IUBMB Comments A pyridoxal 5'-phosphate enzyme. D-Perosamine is one of several dideoxy sugars found in the O-specific polysaccharide of the lipopolysaccharide component of the outer membrane of Gram-negative bacteria. The enzyme catalyses the final step in GDP-alpha-D-perosamine synthesis.
The expected taxonomic range for this enzyme is: Bacteria, Archaea
Synonyms
gdp-perosamine synthase, gdp-4-keto-6-deoxy-d-mannose-4-aminotransferase,
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GDP-4-keto-6-deoxy-D-mannose-4-aminotransferase
GDP-4-keto-6-deoxy-D-mannose-4-aminotransferase
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GDP-4-keto-6-deoxy-D-mannose-4-aminotransferase
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GDP-perosamine synthase
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GDP-perosamine synthase
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GDP-alpha-D-perosamine + 2-oxoglutarate = GDP-4-dehydro-alpha-D-rhamnose + L-glutamate
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GDP-4-amino-4,6-dideoxy-alpha-D-mannose:2-oxoglutarate aminotransferase
A pyridoxal 5'-phosphate enzyme. D-Perosamine is one of several dideoxy sugars found in the O-specific polysaccharide of the lipopolysaccharide component of the outer membrane of Gram-negative bacteria. The enzyme catalyses the final step in GDP-alpha-D-perosamine synthesis.
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GDP-4-dehydro-3,6-dideoxy-alpha-D-mannose + L-glutamate
GDP-4-amino-3,4,6-trideoxy-alpha-D-mannose + 2-oxoglutarate
GDP-4-dehydro-6-deoxy-alpha-D-mannose + L-glutamate
GDP-4-amino-4,6-dideoxy-alpha-D-mannose + 2-oxoglutarate
GDP-4-dehydro-6-deoxy-D-mannose + L-glutamate
GDP-alpha-D-perosamine + 2-oxoglutarate
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GDP-4-dehydro-6-deoxy-D-mannose + L-glutamate
GDP-D-perosamine + 2-oxoglutarate
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GDP-4-dehydro-3,6-dideoxy-alpha-D-mannose + L-glutamate
GDP-4-amino-3,4,6-trideoxy-alpha-D-mannose + 2-oxoglutarate
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GDP-4-dehydro-3,6-dideoxy-alpha-D-mannose + L-glutamate
GDP-4-amino-3,4,6-trideoxy-alpha-D-mannose + 2-oxoglutarate
the unnatural substrate is accommodated in the active site nearly as well as the natural substrate, but the absence of the 3'-OH group affects the alignment of the sugar moiety and, thus, is not properly positioned for efficient catalysis
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GDP-4-dehydro-6-deoxy-alpha-D-mannose + L-glutamate
GDP-4-amino-4,6-dideoxy-alpha-D-mannose + 2-oxoglutarate
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GDP-4-dehydro-6-deoxy-alpha-D-mannose + L-glutamate
GDP-4-amino-4,6-dideoxy-alpha-D-mannose + 2-oxoglutarate
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GDP-4-dehydro-6-deoxy-alpha-D-mannose + L-glutamate
GDP-4-amino-4,6-dideoxy-alpha-D-mannose + 2-oxoglutarate
catalyzes the final step in GDP-perosamine synthesis. L-Perosamine is a component of the O-specific polysaccharide of the lipopolysaccharide component of the outer membrane of Gram-negative bacteria
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GDP-4-dehydro-6-deoxy-alpha-D-mannose + L-glutamate
GDP-4-amino-4,6-dideoxy-alpha-D-mannose + 2-oxoglutarate
GDP-perosamine synthase can use only L-glutamate as its amino donor
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GDP-4-dehydro-6-deoxy-alpha-D-mannose + L-glutamate
GDP-4-amino-4,6-dideoxy-alpha-D-mannose + 2-oxoglutarate
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GDP-4-dehydro-6-deoxy-alpha-D-mannose + L-glutamate
GDP-4-amino-4,6-dideoxy-alpha-D-mannose + 2-oxoglutarate
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GDP-4-dehydro-6-deoxy-alpha-D-mannose + L-glutamate
GDP-4-amino-4,6-dideoxy-alpha-D-mannose + 2-oxoglutarate
GDP-4-dehydro-6-deoxy-D-mannose + L-glutamate
GDP-alpha-D-perosamine + 2-oxoglutarate
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GDP-4-dehydro-6-deoxy-D-mannose + L-glutamate
GDP-D-perosamine + 2-oxoglutarate
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GDP-4-dehydro-6-deoxy-alpha-D-mannose + L-glutamate
GDP-4-amino-4,6-dideoxy-alpha-D-mannose + 2-oxoglutarate
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GDP-4-dehydro-6-deoxy-alpha-D-mannose + L-glutamate
GDP-4-amino-4,6-dideoxy-alpha-D-mannose + 2-oxoglutarate
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GDP-4-dehydro-6-deoxy-alpha-D-mannose + L-glutamate
GDP-4-amino-4,6-dideoxy-alpha-D-mannose + 2-oxoglutarate
catalyzes the final step in GDP-perosamine synthesis. L-Perosamine is a component of the O-specific polysaccharide of the lipopolysaccharide component of the outer membrane of Gram-negative bacteria
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GDP-4-dehydro-6-deoxy-alpha-D-mannose + L-glutamate
GDP-4-amino-4,6-dideoxy-alpha-D-mannose + 2-oxoglutarate
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GDP-4-dehydro-6-deoxy-alpha-D-mannose + L-glutamate
GDP-4-amino-4,6-dideoxy-alpha-D-mannose + 2-oxoglutarate
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pyridoxal 5'-phosphate
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pyridoxal 5'-phosphate-dependent enzyme
pyridoxal 5'-phosphate
a pyridoxal-phosphate protein
pyridoxal 5'-phosphate
a pyridoxal-phosphate protein. The enzyme contains the typically conserved active site lysine residue, which forms a Schiff base with the pyridoxal 5'-phosphate cofactor
pyridoxal 5'-phosphate
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essential for catalysis of ther aminotransferase reaction
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Mg2+
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optimal concentration is 20 mM
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GDP-4-dehydro-6-deoxy-alpha-D-mannose
pH 7.5, 22°C
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pyridoxal 5'-phosphate
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pyridoxal 5'-phosphate dependent aminotransferase
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Dehydration
Accommodation of GDP-linked sugars in the active site of GDP-perosamine synthase.
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0.016
GDP-4-dehydro-3,6-dideoxy-alpha-D-mannose
pH 7.5, 22°C
0.013 - 0.06
GDP-4-dehydro-6-deoxy-alpha-D-mannose
0.07 - 0.09
GDP-4-dehydro-6-deoxy-D-mannose
0.013
GDP-4-dehydro-6-deoxy-alpha-D-mannose
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pH 7.5, 22°C
0.013
GDP-4-dehydro-6-deoxy-alpha-D-mannose
pH 7.5, 22°C
0.06
GDP-4-dehydro-6-deoxy-alpha-D-mannose
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pH 8, °C, His-tag RfbE fusion protein
0.07
GDP-4-dehydro-6-deoxy-D-mannose
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pH 7.5, 37°C
0.09
GDP-4-dehydro-6-deoxy-D-mannose
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pH and temperature not specified in the publication
0.1
L-glutamate
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pH 8, 37°C, His-tag RfbE fusion protein
0.13
L-glutamate
pH 7.5, 22°C, cosubstrate: GDP-4-dehydro-3,6-dideoxy-alpha-D-mannose
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L-glutamate
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pH and temperature not specified in the publication
2.3
L-glutamate
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pH 7.5, 37°C
4.6
L-glutamate
pH 7.5, 22°C, cosubstrate: GDP-4-dehydro-6-deoxy-D-mannose
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0.015
GDP-4-dehydro-3,6-dideoxy-alpha-D-mannose
pH 7.5, 22°C
2.7
GDP-4-dehydro-6-deoxy-alpha-D-mannose
2.7
GDP-4-dehydro-6-deoxy-alpha-D-mannose
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pH 7.5, 22°C
2.7
GDP-4-dehydro-6-deoxy-alpha-D-mannose
pH 7.5, 22°C
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208
GDP-4-dehydro-6-deoxy-alpha-D-mannose
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GDP-4-dehydro-6-deoxy-D-mannose
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pH and temperature not specified in the publication
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L-glutamate
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pH and temperature not specified in the publication
208
GDP-4-dehydro-6-deoxy-alpha-D-mannose
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pH 7.5, 22°C
208
GDP-4-dehydro-6-deoxy-alpha-D-mannose
pH 7.5, 22°C
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3 - 8
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GDP-4-dehydro-6-deoxy-alpha-D-mannose, pH 8, 37°C, His-tag RfbE fusion protein
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L-glutamate, pH 8, 37°C, His-tag RfbE fusion protein
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7.5
assay at
8
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assay at
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UniProt
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40900
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4 * 40900, SDS-PAGE
431000
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recombinant His-tagged Per fusion protein
44330
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10 * 44330, His-tag PerA, SDS-PAGE
458000
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His-tag PerA, gel filtration
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tetramer
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4 * 40900, SDS-PAGE
decamer
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10 * 44330, His-tag PerA, SDS-PAGE
decamer
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recombinant His-tagged Per fusion protein
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hanging drop method of vapor diffusion using a sparse matrix screen. Two crystal structures: a site-directed mutant protein (K186A) complexed with GDP-perosamine and the wild-type enzyme complexed with an unnatural ligand, GDP-3-deoxyperosamine. These structures, determined to 1.6 and 1.7 A resolution, respectively
the three-dimensional structure of the enzyme is determined to a nominal resolution of 1.8 A and refined to an R-factor of 17.9%. Each subunit of the dimeric enzyme contains a seven-stranded mixed beta-sheet, a two-stranded antiparallel beta-sheet, and 12 alpha-helices
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K186H
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single mutant enzyme has no detectable catalytic activity with its sugar substrate
K186H
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single mutant enzyme has no detectable catalytic activity with its sugar substrate
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50
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His-tag PerA holds 55% residual activity after 20 min incubation
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His-tag PerA, 10 min, completely inactivated
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4°C, 30 days, His-tag PerA, residual activity of 68%
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His-tagged fusion protein
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expression as a His-tagged fusion protein in Escherichia coli BL21
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expression in Escherichia coli BL21 (DE3)
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overexpression in Escherichia coli BL21 (DE3)
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Zhao, G.; Liu, J.; Liu, X.; Chen, M.; Zhang, H.; Wang, P.G.
Cloning and characterization of GDP-perosamine synthetase (Per) from Escherichia coli O157:H7 and synthesis of GDP-perosamine in vitro
Biochem. Biophys. Res. Commun.
363
525-530
2007
Escherichia coli
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Cook, P.D.; Carney, A.E.; Holden, H.M.
Accommodation of GDP-linked sugars in the active site of GDP-perosamine synthase
Biochemistry
47
10685-10693
2008
Caulobacter vibrioides (Q9A9H3), Caulobacter vibrioides
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Cook, P.D.; Holden, H.M.
GDP-perosamine synthase: structural analysis and production of a novel trideoxysugar
Biochemistry
47
2833-2840
2008
Caulobacter vibrioides (Q9A9H3), Caulobacter vibrioides
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Cook, P.D.; Kubiak, R.L.; Toomey, D.P.; Holden, H.M.
Two site-directed mutations are required for the conversion of a sugar dehydratase into an aminotransferase
Biochemistry
48
5246-5253
2009
Caulobacter vibrioides, Caulobacter vibrioides CB15
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Albermann, C.; Beuttler, H.
Identification of the GDP-N-acetyl-d-perosamine producing enzymes from Escherichia coli O157:H7
FEBS Lett.
582
479-484
2008
Escherichia coli
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Stroeher, U.H.; Karageorgos, L.E.; Brown, M.H.; Morona, R.; Manning, P.A.
A putative pathway for perosamine biosynthesis is the first function encoded within the rfb region of Vibrio cholerae O1
Gene
166
33-42
1995
Vibrio cholerae serotype O1
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Albermann, C.; Piepersberg, W.
Expression and identification of the RfbE protein from Vibrio cholerae O1 and its use for the enzymatic synthesis of GDP-D-perosamine
Glycobiology
11
655-661
2001
Vibrio cholerae serotype O1
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