Information on EC 1.1.1.123 - sorbose 5-dehydrogenase (NADP+)

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 (more...)
Include results (AMENDA + additional results, but less precise; more...)


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

EC NUMBER
COMMENTARY hide
1.1.1.123
-
RECOMMENDED NAME
GeneOntology No.
sorbose 5-dehydrogenase (NADP+)
REACTION
REACTION DIAGRAM
COMMENTARY hide
ORGANISM
UNIPROT
LITERATURE
L-sorbose + NADP+ = 5-dehydro-D-fructose + NADPH + H+
show the reaction diagram
-
-
-
-
REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
oxidation
-
-
-
-
redox reaction
-
-
-
-
reduction
-
-
-
-
SYSTEMATIC NAME
IUBMB Comments
L-sorbose:NADP+ 5-oxidoreductase
-
CAS REGISTRY NUMBER
COMMENTARY hide
37250-52-5
-
ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
168-2; var. aterneum
-
-
Manually annotated by BRENDA team
adult silverleaf whitefly
-
-
Manually annotated by BRENDA team
mutant strain, SHS 752001
-
-
Manually annotated by BRENDA team
Acetobacter melanogenus
-
-
Manually annotated by BRENDA team
no activity in Bacillus cereus
-
-
-
Manually annotated by BRENDA team
no activity in Candida tropicalis
-
-
-
Manually annotated by BRENDA team
no activity in Escherichia coli K12
-
-
-
Manually annotated by BRENDA team
Boehringer, baker's and brewer's yeast
-
-
Manually annotated by BRENDA team
SUBSTRATE
PRODUCT                       
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
5-keto-D-fructose + NADPH
L-sorbose + NADP+
show the reaction diagram
5-keto-D-fructose 1-phosphate + NADPH
L-sorbose 1-phosphate + NADP+
show the reaction diagram
fructose + NADPH
sorbitol + NADP+
show the reaction diagram
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
fructose + NADPH
sorbitol + NADP+
show the reaction diagram
-
sorbitol synthesis
-
?
COFACTOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
NADP+
NADPH
additional information
-
no activity with NADH
-
METALS and IONS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
phosphate
-
in active site, likely position for the adenyl phasphate of NADP(H)
INHIBITORS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
NADP+
-
competitive inhibitor
p-hydroxymercuribenzoate
-
0.4 mM and 1 mM inhibit activity to 21% and 41% respectively
KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
1 - 5.9
5-keto-D-fructose
0.29
5-Keto-D-fructose 1-phosphate
-
-
600
fructose
-
-
0.046
NADPH
-
pH 7.5, 30°C
SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
0.77
-
+/-0.05, at 30°C
1.25
-
+/-0.08, at 42°C
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
7
-
for ketose reduction
7.4 - 8.5
-
Tris-acetate buffer
9
-
above, for sorbitol oxiation
pH RANGE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
5 - 9
-
pH 5: about 20% of activity maximum, pH 9: about 35% of activity maximum
5.5 - 10.2
-
pH 5.5 and 10.2: about 30% of activity maximum
TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
45
-
for ketose reduction
50
-
for sorbitol oxidation
TEMPERATURE RANGE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
0 - 38
-
activity decreases gradually with increasing temperature from 0°C to 27°C, falls rapidly above 27°C and is completely lost at 38°C
25 - 41
-
sorbitol content increases in a temperature dependent manner
SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
SOURCE
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
33000
-
gel filtration
38160
-
calculation from polypeptide sequence of 352 amino acids
38700
-
4 * 38700, SDS-PAGE
39000
-
4 * 39000, recombinant enzyme, SDS-PAGE
additional information
SUBUNITS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
monomer
-
1 * 33000, SDS-PAGE
tetramer
STORAGE STABILITY
ORGANISM
UNIPROT
LITERATURE
4°C, purified preparations, stable for at least 4 months
-
Purification/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
ammonium sulfate precipitation, affinity chromatography, ion exchange chromatography
-
ammonium sulfate precipitation, DEAE-Sepharose-, Gel Red A-, Phenyl Sepharose column chromatography
-
Cloned/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
expressed in Escherichia coli XL1-Blue
-
ENGINEERING
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
additional information
-
addition of Arg and loss of Asp decrease the electric potential of the adenosine ribose-binding-pocket, creating an environment favorable for NADPH-binding, the replacement of an Asp with an Ala and the adjacent Leu with an Arg change the potential