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IUBMB Comments The enzyme, characterized from the bacterium Burkholderia multivorans , participates in an L -fucose degradation pathway. The enzyme catalyses the oxidation of β-L -fucopyranose to L -fucono-1,5-lactone, which is unstable and is rapidly converted to L -fucono-1,4-lactone. The α anomer is not recognized. The enzyme can also act on β-L -galactopyranose and D -arabinose with lower activity. NADP+ is a better cosubstrate than NAD+ .
The expected taxonomic range for this enzyme is: Burkholderia multivorans
Synonyms BmulJ_04919, more
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BmulJ_04919
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beta-L-fucopyranose + NADP+ = L-fucono-1,5-lactone + NADPH + H+
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beta-L-fucopyranose:NADP+ 1-oxidoreductase
The enzyme, characterized from the bacterium Burkholderia multivorans, participates in an L-fucose degradation pathway. The enzyme catalyses the oxidation of beta-L-fucopyranose to L-fucono-1,5-lactone, which is unstable and is rapidly converted to L-fucono-1,4-lactone. The alpha anomer is not recognized. The enzyme can also act on beta-L-galactopyranose and D-arabinose with lower activity. NADP+ is a better cosubstrate than NAD+.
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4-deoxy-L-fucose + NADP+
4-deoxy-L-fucono-1,5-lactone + NADPH + H+
beta-L-fucopyranose + NADP+
L-fucono-1,5-lactone + NADPH + H+
beta-L-fucose + NAD+
L-fucono-1,5-lactone + NADH + H+
beta-L-fucose + NADP+
L-fucono-1,5-lactone + NADPH + H+
D-arabinose + NADP+
D-arabinono-1,5-lactone + NADPH + H+
Substrates: - Products: -
?
L-galactose + NADP+
L-galactono-1,5-lactone + NADPH + H+
4-deoxy-L-fucose + NADP+
4-deoxy-L-fucono-1,5-lactone + NADPH + H+
Substrates: - Products: -
?
4-deoxy-L-fucose + NADP+
4-deoxy-L-fucono-1,5-lactone + NADPH + H+
Substrates: - Products: -
?
beta-L-fucopyranose + NADP+
L-fucono-1,5-lactone + NADPH + H+
Substrates: - Products: -
?
beta-L-fucopyranose + NADP+
L-fucono-1,5-lactone + NADPH + H+
Substrates: - Products: -
?
beta-L-fucose + NAD+
L-fucono-1,5-lactone + NADH + H+
Substrates: the enzyme has preference for NADP+ over NAD+ Products: -
?
beta-L-fucose + NAD+
L-fucono-1,5-lactone + NADH + H+
Substrates: the enzyme has preference for NADP+ over NAD+ Products: -
?
beta-L-fucose + NADP+
L-fucono-1,5-lactone + NADPH + H+
Substrates: beta-L-fucose is the best substrate. The enzyme has preference for NADP+ over NAD+ Products: -
?
beta-L-fucose + NADP+
L-fucono-1,5-lactone + NADPH + H+
Substrates: beta-L-fucose is the best substrate. The enzyme has preference for NADP+ over NAD+ Products: -
?
L-galactose + NADP+
L-galactono-1,5-lactone + NADPH + H+
Substrates: - Products: -
?
L-galactose + NADP+
L-galactono-1,5-lactone + NADPH + H+
Substrates: - Products: -
?
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beta-L-fucopyranose + NADP+
L-fucono-1,5-lactone + NADPH + H+
beta-L-fucopyranose + NADP+
L-fucono-1,5-lactone + NADPH + H+
Substrates: - Products: -
?
beta-L-fucopyranose + NADP+
L-fucono-1,5-lactone + NADPH + H+
Substrates: - Products: -
?
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NADP+
the enzyme has preference for NADP+ over NAD+
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0.786
4-deoxy-L-fucose
with NADP+ as cosubstrate, at pH 8.0 and 30°C
0.0062
beta-L-fucose
with NADP+ as cosubstrate, at pH 8.0 and 30°C
0.094
D-arabinose
with NADP+ as cosubstrate, at pH 8.0 and 30°C
0.285
L-galactose
with NADP+ as cosubstrate, at pH 8.0 and 30°C
0.028
NAD+
with beta-L-fucose as cosubstrate, at pH 8.0 and 30°C
0.004
NADP+
with beta-L-fucose as cosubstrate, at pH 8.0 and 30°C
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26
4-deoxy-L-fucose
with NADP+ as cosubstrate, at pH 8.0 and 30°C
10
beta-L-fucose
with NADP+ as cosubstrate, at pH 8.0 and 30°C
21
D-arabinose
with NADP+ as cosubstrate, at pH 8.0 and 30°C
11
L-galactose
with NADP+ as cosubstrate, at pH 8.0 and 30°C
5
NAD+
with beta-L-fucose as cosubstrate, at pH 8.0 and 30°C
11
NADP+
with beta-L-fucose as cosubstrate, at pH 8.0 and 30°C
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40
4-deoxy-L-fucose
with NADP+ as cosubstrate, at pH 8.0 and 30°C
1500
beta-L-fucose
with NADP+ as cosubstrate, at pH 8.0 and 30°C
230
D-arabinose
with NADP+ as cosubstrate, at pH 8.0 and 30°C
37
L-galactose
with NADP+ as cosubstrate, at pH 8.0 and 30°C
530
NAD+
with beta-L-fucose as cosubstrate, at pH 8.0 and 30°C
3000
NADP+
with beta-L-fucose as cosubstrate, at pH 8.0 and 30°C
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UniProt
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UniProt
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Highest Expressing Human Cell Lines
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LFUCD_BURM1
Burkholderia multivorans (strain ATCC 17616 / 249)
258
0
27679
Swiss-Prot
other Location (Reliability: 4 )
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homotetramer
x-ray crystallography
homotetramer
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x-ray crystallography
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hanging drop vapor diffusion method, using 0.2 M calcium acetate, 10% (w/v) PEG 8000, 0.1 M HEPES pH 7.5 for the unliganded enzyme, or 0.2 M MgCl2, 20% (w/v) PEG8000, 0.1 M Tris pH 8.5 for enzyme in complex with NADP+ and L-fucose
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ammonium sulfate precipitation, Superdex 200 gel filtration, and ResourceQ column chromatography
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expressed in Escherichia coli BL21(DE3) cells
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Hobbs, M.E.; Vetting, M.; Williams, H.J.; Narindoshvili, T.; Kebodeaux, D.M.; Hillerich, B.; Seidel, R.D.; Almo, S.C.; Raushel, F.M.
Discovery of an L-fucono-1,5-lactonase from cog3618 of the amidohydrolase superfamily
Biochemistry
52
239-253
2013
Burkholderia multivorans (A0A0H3KNE7), Burkholderia multivorans ATCC 17616 (A0A0H3KNE7)
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