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

for references in articles please use BRENDA:EC1.1.1.B60
Please wait a moment until all data is loaded. This message will disappear when all data is loaded.
Specify your search results
Select one or more organisms in this record:
Show additional data
Do not include text mining results
Include (text mining) results
Include results (AMENDA + additional results, but less precise)


The expected taxonomic range for this enzyme is: Gluconobacter oxydans

top print hide
EC NUMBER
COMMENTARY hide
1.1.1.B60
preliminary BRENDA-supplied EC number
top print hide
RECOMMENDED NAME
GeneOntology No.
D-sorbitol dehydrogenase (NADP+)
-
top print hide
REACTION
REACTION DIAGRAM
COMMENTARY hide
ORGANISM
UNIPROT
LITERATURE
D-sorbitol + NADP+ = L-sorbose + NADPH + H+
show the reaction diagram
-
-
-
-
top print hide
SYSTEMATIC NAME
IUBMB Comments
D-sorbitol:NADP+-oxidroreductase (L-sorbose-forming)
-
top
top print hide
ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
-
-
-
Manually annotated by BRENDA team
top print hide
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
-
-
-
-
?
D-sorbitol + NADP+
L-sorbose + NADPH + H+
show the reaction diagram
mannitol + NADP+
?
show the reaction diagram
-
-
-
-
?
additional information
?
-
top print hide
COFACTOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
NADP+
-
the enzyme exhibits high preference for NADP+ (vs. 2.5% relative activity with NAD+)
top print hide
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
top print hide
INHIBITORS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
D-sorbitol
-
inhibitory at more than 10% (w/v)
top print hide
KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
38.9
D-sorbitol
-
at pH 10.0 and 25°C
top print hide
TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
3820
D-sorbitol
-
at pH 10.0 and 25°C
top print hide
kcat/KM VALUE [1/mMs-1]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
98.1
D-sorbitol
-
at pH 10.0 and 25°C
top print hide
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
top print hide
TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
top print hide
TEMPERATURE RANGE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
25 - 75
-
more than 40% activity between 25 and 75°C
top print hide
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
54000
-
2 * 54000, SDS-PAGE
top print hide
SUBUNITS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
homodimer
top print hide
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
-
top print hide
Purification/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
Ni-NTA column chromatography
-
top print hide
Cloned/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
expressed in Escherichia coli BL21(DE3)-CodonPlus RIL cells
-
top
top
LINKS TO OTHER DATABASES (specific for EC-Number 1.1.1.B60)
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)