Information on EC 1.1.1.113 - L-xylose 1-dehydrogenase

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The expected taxonomic range for this enzyme is: Saccharomyces cerevisiae

EC NUMBER
COMMENTARY
1.1.1.113
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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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-
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reduction
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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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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
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-arabono-1,4-lactone + NADPH
show the reaction diagram
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-
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?
D-lyxose + NADP+
D-lyxono-1,4-lactone + NADPH
show the reaction diagram
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-
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?
L-xylose + NADP+
L-xylono-1,4-lactone + NADPH
show the reaction diagram
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-
-
?
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
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-
-
?
COFACTOR
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
IMAGE
pH OPTIMUM
pH MAXIMUM
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
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
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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