Information on EC 1.1.1.B60 - D-sorbitol dehydrogenase (NADP+)

for references in articles please use BRENDA:EC1.1.1.B60
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The expected taxonomic range for this enzyme is: Gluconobacter oxydans

EC NUMBER
COMMENTARY hide
1.1.1.B60
preliminary BRENDA-supplied EC number
RECOMMENDED NAME
GeneOntology No.
D-sorbitol dehydrogenase (NADP+)
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REACTION
REACTION DIAGRAM
COMMENTARY hide
ORGANISM
UNIPROT
LITERATURE
D-sorbitol + NADP+ = L-sorbose + NADPH + H+
show the reaction diagram
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-
-
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SYSTEMATIC NAME
IUBMB Comments
D-sorbitol:NADP+-oxidroreductase (L-sorbose-forming)
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ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
SUBSTRATE
PRODUCT                       
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
D-arabinitol+ NADP+
?
show the reaction diagram
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-
-
-
?
D-sorbitol + NADP+
L-sorbose + NADPH + H+
show the reaction diagram
mannitol + NADP+
?
show the reaction diagram
-
-
-
-
?
additional information
?
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COFACTOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
NADP+
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the enzyme exhibits high preference for NADP+ (vs. 2.5% relative activity with NAD+)
METALS and IONS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
Ba2+
-
activates
Ca2+
-
activates
Cu2+
-
activates
K+
-
activates
Zn2+
-
activates
additional information
-
Mg2+, Co2+, and Mn2+ ions show no stimulatory influence on enzyme activity
INHIBITORS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
D-sorbitol
-
inhibitory at more than 10% (w/v)
KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
38.9
D-sorbitol
-
at pH 10.0 and 25°C
TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
3820
D-sorbitol
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at pH 10.0 and 25°C
kcat/KM VALUE [1/mMs-1]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
98.1
D-sorbitol
-
at pH 10.0 and 25°C
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
TEMPERATURE RANGE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
25 - 75
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more than 40% activity between 25 and 75°C
SUBUNITS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
homodimer
GENERAL STABILITY
ORGANISM
UNIPROT
LITERATURE
stability of the enzyme significantly improves (up to 13.6fold) after cross-linking of immobilized enzyme on silica nanoparticles and retains 62.8% residual activity after 10 cycles of reuse
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Purification/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
Ni-NTA column chromatography
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Cloned/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
expressed in Escherichia coli BL21(DE3)-CodonPlus RIL cells
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