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Enzyme Nomenclature
Information on EC 1.1.1.424 - D-xylose 1-dehydrogenase (NADP+, D-xylono-1,4-lactone-forming)
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1.1.1.424 D-xylose 1-dehydrogenase (NADP+, D-xylono-1,4-lactone-forming)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).
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The expected taxonomic range for this enzyme is: Halobacteria
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SYNONYM 
ORGANISM
UNIPROT
COMMENTARY 
LITERATURE
D-xylose dehydrogenase
Gfo6
HVO_B0028
xacA
XDH
xacA
-
-
-
-
XDH
-
-
-
-
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REACTION
REACTION DIAGRAM
COMMENTARY
ORGANISM
UNIPROT
LITERATURE
D-xylose + NADP+ = D-xylono-1,4-lactone + NADPH + H+
-
-
-
-
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PATHWAY SOURCE
PATHWAYS
BRENDA
MetaCyc
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SYSTEMATIC NAME
IUBMB Comments
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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SUBSTRATE
PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate)
(Substrate)
LITERATURE
(Substrate)
(Substrate)
COMMENTARY
(Product)
(Product)
LITERATURE
(Product)
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
D-glucose + NADP+
D-gluconolactone + NADPH + H+
-
-
-
?
D-xylose + NADP+
D-xylono-1,4-lactone + NADPH + H+
-
-
-
?
D-xylose + NADP+
D-xylono-1,4-lactone + 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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NATURAL SUBSTRATE
NATURAL PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate)
(Substrate)
LITERATURE
(Substrate)
(Substrate)
COMMENTARY
(Product)
(Product)
LITERATURE
(Product)
(Product)
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
D-xylose + NADP+
D-xylono-1,4-lactone + NADPH + H+
-
-
-
?
D-xylose + NADP+
D-xylono-1,4-lactone + 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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COFACTOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
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METALS and IONS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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ACTIVATING COMPOUND
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
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KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
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TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
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kcat/KM VALUE [1/mMs-1]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
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SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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pH RANGE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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ORGANISM
COMMENTARY
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
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GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
physiological function
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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UNIPROT
ENTRY NAME
ORGANISM
NO. OF AA
NO. OF TRANSM. HELICES
MOLECULAR WEIGHT[Da]
SOURCE
SEQUENCE
LOCALIZATION PREDICTION
The reliability class of the localization prediction ranges from 1 (very reliable) to 5 (not reliable).
The reliability class of the localization prediction ranges from 1 (very reliable) to 5 (not reliable). GFO6_HALMA
Haloarcula marismortui (strain ATCC 43049 / DSM 3752 / JCM 8966 / VKM B-1809)
360
0
39937
Swiss-Prot
-
XDH1_HALVD
Haloferax volcanii (strain ATCC 29605 / DSM 3757 / JCM 8879 / NBRC 14742 / NCIMB 2012 / VKM B-1768 / DS2)
390
0
42307
Swiss-Prot
-
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MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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SUBUNIT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
tetramer
tetramer
4 * 57000, SDS-PAGE, 4 * 39900, calculated from sequence
tetramer
-
4 * 57000, SDS-PAGE, 4 * 39900, calculated from sequence
-
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PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
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CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
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REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
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, Haloferax volcanii (D4GP29), Haloferax volcanii H26, 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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