Information on EC 1.1.1.113 - L-xylose 1-dehydrogenase

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The expected taxonomic range for this enzyme is: Archaea, Eukaryota

EC NUMBER
COMMENTARY
1.1.1.113
-
RECOMMENDED NAME
GeneOntology No.
L-xylose 1-dehydrogenase
REACTION
REACTION DIAGRAM
COMMENTARY
ORGANISM
UNIPROT ACCESSION NO.
LITERATURE
L-xylose + NADP+ = L-xylono-1,4-lactone + NADPH + H+
show the reaction diagram
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-
-
-
REACTION TYPE
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
oxidation
-
-
-
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redox reaction
-
-
-
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reduction
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-
-
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SYSTEMATIC NAME
IUBMB Comments
L-xylose:NADP+ 1-oxidoreductase
Also oxidizes D-arabinose and D-lyxose.
SYNONYMS
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
L-xylose dehydrogenase
-
-
-
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NADPH-xylose reductase
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-
-
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xylose reductase
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CAS REGISTRY NUMBER
COMMENTARY
37250-44-5
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ORGANISM
COMMENTARY
LITERATURE
SEQUENCE CODE
SEQUENCE DB
SOURCE
Haloferax mediterranei DSM 1411
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SwissProt
Manually annotated by BRENDA team
SUBSTRATE
PRODUCT                      
REACTION DIAGRAM
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
(Substrate)
LITERATURE
(Substrate)
COMMENTARY
(Product)
LITERATURE
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
D-arabinose + NADP+
D-arabinono-1,4-lactone + NADPH
show the reaction diagram
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-
-
?
D-lyxose + NADP+
D-lyxono-1,4-lactone + NADPH
show the reaction diagram
-
-
-
?
D-xylose + NADP+
?
show the reaction diagram
Haloferax mediterranei, Haloferax mediterranei DSM 1411
Q977U7
88% of the activity with D-glucose and NADP+. The enzyme shows also activity with D-xylose and NAD+ as cofactor, D-glucose (NADP+ or NAD+ as cofactor), D-fucose (cofactor NADP+) and D-galactose (cofactor NADP+)
-
-
?
L-xylose + NADP+
L-xylono-1,4-lactone + NADPH
show the reaction diagram
-
-
-
?
NATURAL SUBSTRATES
NATURAL PRODUCTS
REACTION DIAGRAM
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
(Substrate)
LITERATURE
(Substrate)
COMMENTARY
(Product)
LITERATURE
(Product)
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
L-xylose + NADP+
L-xylono-1,4-lactone + NADPH
show the reaction diagram
-
-
-
?
COFACTOR
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
IMAGE
INHIBITORS
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
IMAGE
pH OPTIMUM
pH MAXIMUM
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
MOLECULAR WEIGHT
MOLECULAR WEIGHT MAXIMUM
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
89000
-
Q977U7
gel filtration
SUBUNITS
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
dimer
Q977U7
2 * 53000, SDS-PAGE
dimer
Haloferax mediterranei DSM 1411
-
2 * 53000, SDS-PAGE
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TEMPERATURE STABILITY
TEMPERATURE STABILITY MAXIMUM
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
65
-
Q977U7
half-life: 56.8 h, in the presence of 3 M NaCl, stability decreases significantly with lower salt concentrations
STORAGE STABILITY
ORGANISM
UNIPROT ACCESSION NO.
LITERATURE
4°C, stable for several months
Q977U7
Purification/COMMENTARY
ORGANISM
UNIPROT ACCESSION NO.
LITERATURE
ammonium sulfate, acetone, DEAE-cellulose
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ENGINEERING
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
K270D/N272P/S271G/R276F
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mutant shows a decreased NADPH and NADH xylose reductase activities, respectively, compared to wild-type
K270G
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mutant shows a decreased NADPH and NADH xylose reductase activities, respectively, compared to wild-type
K270M
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mutant shows a decreased NADPH and NADH xylose reductase activities, respectively, compared to wild-type
K270R
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mutant shows a 3.4fold and 2.4fold higher NADPH and NADH preferred xylose reductase activities, respectively, compared with wild-type. Mutant exhibits an improved xylose consumption rate, balanced redox system and increased ethanol yield and production rate
K270R/N272D
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mutant shows a decreased NADPH and NADH xylose reductase activities, respectively, compared to wild-type
K270R/R276H
-
mutant shows a decreased NADPH and NADH xylose reductase activities, respectively, compared to wild-type
K274R
-
mutant shows a decreased NADPH and NADH xylose reductase activities, respectively, compared to wild-type
K274R/N276D
-
mutant shows a decreased NADPH and NADH xylose reductase activities, respectively, compared to wild-type