Information on EC 1.1.1.113 - L-xylose 1-dehydrogenase

for references in articles please use BRENDA:EC1.1.1.113
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The expected taxonomic range for this enzyme is: Archaea, Eukaryota

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EC NUMBER
COMMENTARY hide
1.1.1.113
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RECOMMENDED NAME
GeneOntology No.
L-xylose 1-dehydrogenase
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REACTION
REACTION DIAGRAM
COMMENTARY hide
ORGANISM
UNIPROT
LITERATURE
L-xylose + NADP+ = L-xylono-1,4-lactone + NADPH + H+
show the reaction diagram
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-
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REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
oxidation
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-
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redox reaction
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-
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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.
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CAS REGISTRY NUMBER
COMMENTARY hide
37250-44-5
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ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
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SwissProt
Manually annotated by BRENDA team
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Manually annotated by BRENDA team
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SUBSTRATE
PRODUCT                       
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
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
L-xylose + NADP+
L-xylono-1,4-lactone + NADPH
show the reaction diagram
-
-
-
?
L-xylose + NADP+
L-xylono-1,4-lactone + NADPH + H+
show the reaction diagram
-
-
-
-
?
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NATURAL SUBSTRATES
NATURAL PRODUCTS
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
L-xylose + NADP+
L-xylono-1,4-lactone + NADPH
show the reaction diagram
-
-
-
?
L-xylose + NADP+
L-xylono-1,4-lactone + NADPH + H+
show the reaction diagram
-
-
-
-
?
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COFACTOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
NADPH
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preferred cofactor
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INHIBITORS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
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pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
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MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
53000
2 * 53000, SDS-PAGE
89000
gel filtration
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SUBUNITS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
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TEMPERATURE STABILITY
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
37 - 45
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after 10 min at 37°C, 42°C, and 45°C, the retained activities of the enzyme are 97.17%, 101.10% and 87.35%, respectively
65
half-life: 56.8 h, in the presence of 3 M NaCl, stability decreases significantly with lower salt concentrations
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STORAGE STABILITY
ORGANISM
UNIPROT
LITERATURE
4°C, stable for several months
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Purification/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
ammonium sulfate, acetone, DEAE-cellulose
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Cloned/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
expressed in Kluyveromyces marxianus strain YZJ088
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ENGINEERING
ORGANISM
UNIPROT
COMMENTARY hide
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
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mutant shows a decreased NADPH and NADH xylose reductase activities, respectively, compared to wild-type
K274R/N276D
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mutant shows a decreased NADPH and NADH xylose reductase activities, respectively, compared to wild-type
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LINKS TO OTHER DATABASES (specific for EC-Number 1.1.1.113)
ExplorEnz
ExPASy
KEGG
MetaCyc
SABIO-RK
NCBI: PubMed, Protein, Nucleotide, Structure, Genome, OMIM
IUBMB Enzyme Nomenclature
PROSITE Database of protein families and domains
InterPro (database of protein families, domains and functional sites)