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EC Tree
IUBMB Comments The enzyme, which participates in the degradation of D-xylose, has been characterized from several halophilic archaeal species. cf. EC 1.1.1.179, D-xylose 1-dehydrogenase (NADP+, D-xylono-1,5-lactone-forming).
The expected taxonomic range for this enzyme is: Halobacteria
Synonyms
Gfo6,
HVO_B0028 ,
xacA ,
XDH ,
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Gfo6
-
HVO_B0028
-
xacA
-
-
-
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D-xylose + NADP+ = D-xylono-1,4-lactone + NADPH + H+
-
-
-
-
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D-xylose:NADP+ 1-oxidoreductase (D-xylono-1,4-lactone-forming)
The enzyme, which participates in the degradation of D-xylose, has been characterized from several halophilic archaeal species. cf. EC 1.1.1.179, D-xylose 1-dehydrogenase (NADP+, D-xylono-1,5-lactone-forming).
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D-glucose + NADP+
D-gluconolactone + H+ + NADPH
D-glucose + NADP+
D-glucoselactone + NADPH + H+
D-ribose + NADP+
D-ribonolactone + H+ + NADPH
D-xylose + NAD+
D-xylonolactone + H+ + NADH
D-xylose + NAD+
D-xylonolactone + NADH + H+
D-xylose + NADP+
D-xylono-1,4-lactone + H+ + NADPH
D-xylose + NADP+
D-xylonolactone + H+ + NADPH
D-xylose + NADP+
D-xylonolactone + NADPH + H+
additional information
?
-
D-glucose + NADP+
D-gluconolactone + H+ + NADPH
-
-
?
D-glucose + NADP+
D-gluconolactone + H+ + NADPH
-
-
?
D-glucose + NADP+
D-glucoselactone + NADPH + H+
-
-
?
D-glucose + NADP+
D-glucoselactone + NADPH + H+
-
-
?
D-ribose + NADP+
D-ribonolactone + H+ + NADPH
-
-
?
D-ribose + NADP+
D-ribonolactone + H+ + NADPH
-
-
?
D-xylose + NAD+
D-xylonolactone + H+ + NADH
-
-
?
D-xylose + NAD+
D-xylonolactone + H+ + NADH
-
-
?
D-xylose + NAD+
D-xylonolactone + NADH + H+
-
-
?
D-xylose + NAD+
D-xylonolactone + NADH + H+
-
-
?
D-xylose + NADP+
D-xylono-1,4-lactone + H+ + NADPH
-
-
?
D-xylose + NADP+
D-xylono-1,4-lactone + H+ + NADPH
-
-
?
D-xylose + NADP+
D-xylonolactone + H+ + NADPH
-
-
?
D-xylose + NADP+
D-xylonolactone + H+ + NADPH
-
-
?
D-xylose + NADP+
D-xylonolactone + NADPH + H+
-
-
?
D-xylose + NADP+
D-xylonolactone + NADPH + H+
-
-
?
additional information
?
-
no substrates: L-arabinose, D-arabinose, D-ribose, D-mannose, and L-mannose
-
-
additional information
?
-
no substrates: L-arabinose, D-arabinose, D-ribose, D-mannose, and L-mannose
-
-
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D-xylose + NAD+
D-xylonolactone + H+ + NADH
D-xylose + NAD+
D-xylonolactone + NADH + H+
D-xylose + NADP+
D-xylonolactone + H+ + NADPH
D-xylose + NADP+
D-xylonolactone + NADPH + H+
additional information
?
-
D-xylose + NAD+
D-xylonolactone + H+ + NADH
-
-
-
?
D-xylose + NAD+
D-xylonolactone + H+ + NADH
-
-
-
?
D-xylose + NAD+
D-xylonolactone + NADH + H+
-
-
-
?
D-xylose + NAD+
D-xylonolactone + NADH + H+
-
-
-
?
D-xylose + NADP+
D-xylonolactone + H+ + NADPH
-
-
-
?
D-xylose + NADP+
D-xylonolactone + H+ + NADPH
-
-
-
?
D-xylose + NADP+
D-xylonolactone + NADPH + H+
-
-
-
?
D-xylose + NADP+
D-xylonolactone + NADPH + H+
-
-
-
?
additional information
?
-
no substrates: L-arabinose, D-arabinose, D-ribose, D-mannose, and L-mannose
-
-
-
additional information
?
-
no substrates: L-arabinose, D-arabinose, D-ribose, D-mannose, and L-mannose
-
-
-
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NAD+
-
NAD+
NADP+ is preferred over NAD+
NADP+
-
NADP+
NADP+ is preferred over NAD+
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KCl
maximum activity at 1.5 M, strong stimulation
MgCl2
maximum activity at 0.1 M, strong stimulation
NaCl
maximum activity at 1.5 M, strong stimulation
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2.3
D-ribose
pH 8.3, 37°C
64
D-glucose
pH 8.3, 37°C
198
D-glucose
pH 7.5, 42°C
1.2
D-xylose
pH 8.3, 37°C
4.7
D-xylose
pH 7.5, 42°C
0.36
NAD+
pH 7.5, 42°C
0.031
NADP+
pH 7.5, 42°C
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273
D-glucose
pH 8.3, 37°C
360
D-ribose
pH 8.3, 37°C
356
D-xylose
pH 8.3, 37°C
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4.3
D-glucose
pH 8.3, 37°C
157
D-ribose
pH 8.3, 37°C
297
D-xylose
pH 8.3, 37°C
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24.1
substrate D-xylose, pH 7.5, 42°C
7.8
substrate D-glucose, pH 7.5, 42°C
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8.3
presence of 1.5 M KCl
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7
50% of maximum activity
9
50% of maximum activity
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-
UniProt
brenda
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UniProt
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SwissProt
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SwissProt
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physiological function
D-xylose is oxidized exclusively to the tricarboxylic acid cycle intermediate alpha-ketoglutarate, involving D-xylose dehydrogenase (HVO_B0028), a xylonate dehydratase (HVO_B0038A), 2-keto-3-deoxyxylonate dehydratase (HVO_B0027), and alpha-ketoglutarate semialdehyde dehydrogenase (HVO_B0039). An HVO_B0028 gene deletion mutant cannot grow on xylose but grows unaffected on glucose as the wild-type
physiological function
Haloferax volcanii degrades the pentoses D-xylose and L-arabinose via an oxidative pathway to 2-oxoglutarate as an intermediate. The initial dehydrogenases of the pathway, D-xylose dehydrogenase (XDH) and L-arabinose dehydrogenase (L-AraDH) catalyze the NADP+ dependent D-xylose and L-arabinose oxidation
physiological function
-
Haloferax volcanii degrades the pentoses D-xylose and L-arabinose via an oxidative pathway to 2-oxoglutarate as an intermediate. The initial dehydrogenases of the pathway, D-xylose dehydrogenase (XDH) and L-arabinose dehydrogenase (L-AraDH) catalyze the NADP+ dependent D-xylose and L-arabinose oxidation
physiological function
-
D-xylose is oxidized exclusively to the tricarboxylic acid cycle intermediate alpha-ketoglutarate, involving D-xylose dehydrogenase (HVO_B0028), a xylonate dehydratase (HVO_B0038A), 2-keto-3-deoxyxylonate dehydratase (HVO_B0027), and alpha-ketoglutarate semialdehyde dehydrogenase (HVO_B0039). An HVO_B0028 gene deletion mutant cannot grow on xylose but grows unaffected on glucose as the wild-type
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XDH1_HALVD
Haloferax volcanii (strain ATCC 29605 / DSM 3757 / JCM 8879 / NBRC 14742 / NCIMB 2012 / VKM B-1768 / DS2)
390
0
42307
Swiss-Prot
-
GFO6_HALMA
Haloarcula marismortui (strain ATCC 43049 / DSM 3752 / JCM 8966 / VKM B-1809)
360
0
39937
Swiss-Prot
-
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tetramer
4 * 57000, SDS-PAGE, 4 * 39900, calculated from sequence
tetramer
-
4 * 57000, SDS-PAGE, 4 * 39900, calculated from sequence
tetramer
4 * 55000, SDS-PAGE
tetramer
-
4 * 55000, SDS-PAGE
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both native and recombinant protein
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expression in Escherichia coli
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Sutter, J.; Johnsen, U.; Schönheit, P.
Characterization of a pentonolactonase involved in D-xylose and L-arabinose catabolism in the haloarchaeon Haloferax volcanii
FEMS Microbiol. Lett.
364
fnx140
2017
Haloferax volcanii (D4GP29), Haloferax volcanii DSM 3757 (D4GP29)
brenda
Johnsen, U.; Schonheit, P.
Novel xylose dehydrogenase in the halophilic archaeon Haloarcula marismortui
J. Bacteriol.
186
6198-6207
2004
Haloarcula marismortui (Q5UY95), Haloarcula marismortui DSM 3752 (Q5UY95)
brenda
Johnsen, U.; Dambeck, M.; Zaiss, H.; Fuhrer, T.; Soppa, J.; Sauer, U.; Schonheit, P.
D-Xylose degradation pathway in the halophilic archaeon Haloferax volcanii
J. Biol. Chem.
284
27290-27303
2009
Haloferax volcanii (D4GP29), Haloferax volcanii DSM 3757 (D4GP29)
brenda
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Enzyme Nomenclature
1.1.1.424 D-xylose 1-dehydrogenase (NADP+, D-xylono-1,4-lactone-forming)
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