Information on EC 1.1.1.200 - aldose-6-phosphate reductase (NADPH)

for references in articles please use BRENDA:EC1.1.1.200
Word Map on EC 1.1.1.200
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:

The enzyme appears in viruses and cellular organisms

EC NUMBER
COMMENTARY hide
1.1.1.200
-
RECOMMENDED NAME
GeneOntology No.
aldose-6-phosphate reductase (NADPH)
REACTION
REACTION DIAGRAM
COMMENTARY hide
ORGANISM
UNIPROT
LITERATURE
D-sorbitol 6-phosphate + NADP+ = D-glucose 6-phosphate + NADPH + H+
show the reaction diagram
-
-
-
-
REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
oxidation
-
-
-
-
redox reaction
-
-
-
-
reduction
-
-
-
-
PATHWAY
BRENDA Link
KEGG Link
MetaCyc Link
sorbitol biosynthesis I
-
-
SYSTEMATIC NAME
IUBMB Comments
D-aldose-6-phosphate:NADP+ 1-oxidoreductase
In the reverse reaction, acts also on D-galactose 6-phosphate and, more slowly, on D-mannose 6-phosphate and 2-deoxy-D-glucose 6-phosphate.
CAS REGISTRY NUMBER
COMMENTARY hide
76901-04-7
-
ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
cultivar Mogi
-
-
Manually annotated by BRENDA team
-
-
-
Manually annotated by BRENDA team
apricot, cv. Perfection
-
-
Manually annotated by BRENDA team
pear, cv. Conference, cv. Bartlett
-
-
Manually annotated by BRENDA team
GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
physiological function
-
sorbitol-6-phosphate dehydrogenase is a key enzyme for sorbitol synthesis and plays an important role in the alleviation of salinity stress in plants
SUBSTRATE
PRODUCT                       
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
2-deoxy-D-glucose 6-phosphate + NADPH
?
show the reaction diagram
-
reduced at low rate
-
-
?
D-galactose 6-phosphate + NADPH
?
show the reaction diagram
-
reduced at a higher rate than D-glucose 6-phosphate
-
-
r
D-glucitol-6-phosphate
D-glucose 6-phosphate + NADPH + H+
show the reaction diagram
-
-
-
r
D-glucose 6-phosphate + NADPH
D-sorbitol 6-phosphate + NADP+
show the reaction diagram
-
-
-
-
r
D-glucose 6-phosphate + NADPH + H+
D-glucitol-6-phosphate + NADP+
show the reaction diagram
-
-
-
r
D-glucose 6-phosphate + NADPH + H+
D-sorbitol 6-phosphate + NADP+
show the reaction diagram
-
-
-
-
r
D-mannose 6-phosphate + NADPH
?
show the reaction diagram
-
reduced at low rate
-
-
?
D-sorbitol 6-phosphate + NADP+
D-glucose 6-phosphate + NADPH + H+
show the reaction diagram
additional information
?
-
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
D-sorbitol 6-phosphate + NADP+
D-glucose 6-phosphate + NADPH + H+
show the reaction diagram
-
-
-
-
?
additional information
?
-
COFACTOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
NADP+
NADPH
additional information
-
no activity with NAD+ or NADH
-
METALS and IONS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
CaCl2
-
2.5 mM, in presence of 5 mM substrate, 40% increase in activity
MgCl2
-
2.5 mM, in presence of 5 mM substrate, 52% increase in activity
INHIBITORS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
AgNO3
-
complete inhibition at 0.1 mM
CaCl2
-
2.5 mM, in presence of 50 mM substrate, 12% decrease in activity
cysteine
-
47% inhibition of oxidation and 11% inhibition of reduction at 10 mM
iodoacetate
-
42% inhibition of oxidation and 19% inhibition of reduction at 10 mM
MgCl2
-
2.5 mM, in presence of 50 mM substrate, 12% decrease in activity
Na2EDTA
-
35% inhibition of oxidation and 11% inhibition of reduction at 10 mM
NaCl
200 mM cause about 65% inhibition of the enzyme activity
p-chloromercuribenzoate
-
complete inhibition at 1.0 mM
phosphate
-
mixed-type inhibition
ZnCl2
-
2 mM, 58% inhibition, partially reversible by EDTA
ZnSO4
-
complete inhibition of oxidation and 80% inhibition of reduction at 1.25 mM
additional information
no significant differences in activity when ATP, ADP, AMP, ADP-glucose, UTP, UDP-glucose, inorganic phosphate or diphosphate (5 mM each), 10% (v/v) glycerol, 500 mM glucitol or 20% (w/v) sucrose are added to the enzyme assay mixture
-
ACTIVATING COMPOUND
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
additional information
-
enzyme activity is rapidly induced by water stress
-
KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.2 - 15.9
D-glucose 6-phosphate
5.1 - 9.8
D-Glucose-6-phosphate
3.9 - 7.21
D-sorbitol 6-phosphate
1.7 - 3
D-sorbitol-6-phosphate
TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.0011 - 0.222
D-glucitol-6-phosphate
0.009 - 0.7
D-glucose 6-phosphate
Ki VALUE [mM]
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.42
phosphate
-
pH 9.0
SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
0.017
C-term tagged enzyme, purified enzyme
0.136
N-term tagged enzyme, crude extract
0.477
-
with D-sorbitol 6-phosphate as substrate, at pH 8.0 and 25°C
0.603
-
with D-glucose 6-phosphate as substrate, at pH 8.0 and 25°C
1.25
N-term tagged enzyme, 9.2fold purified
7.94
-
pH 9.0
13530
-
leaf base
18400
-
leaf tip
additional information
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
9.5
-
both directions
pH RANGE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
6 - 10
N- and the C-term tagged enzymes. Both recombinant enzymes similarly show optimal activity in a broad pH range in the direction of D-glucose 6-phosphate reduction, and a narrow range (pH 9.0-10.0) in the opposite oxidative direction
8.5 - 10.1
-
about 50% of activity maximum at pH 8.5 and 10.1
TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
30 - 35
-
D-sorbitol 6-phosphate oxidation
35
-
D-glucose 6-phosphate reduction
TEMPERATURE RANGE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
additional information
-
no activity at 50°C
SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
SOURCE
LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY hide
GeneOntology No.
LITERATURE
SOURCE
level of soluble recombinant enzyme is much higher in the N-term tagged protein than in the C-term tagged one. In the C-term tagged one the majority of the protein is in the insoluble form
-
Manually annotated by BRENDA team
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
33000
-
2 * 33000, SDS-PAGE
34900
sequence analysis, A6PRase
SUBUNITS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
?
-
x * 39000, SDS-PAGE
monomer
gel filtration, C-term tagged enzyme
STORAGE STABILITY
ORGANISM
UNIPROT
LITERATURE
-80°C, 25 mM Tris-HCl buffer, pH 8.0, 300 mM NaCl, 1 mM beta-mercaptoethanol, 10% (v/v) glycerol, 1 mM EDTA, 0.5 mM DTT, 6 months
1°C, 1 week, partially purified enzyme
-
Purification/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
Ni-NTA column chromatography
-
one-step protein purification by immobilized metal affinity chromatography, N-term tagged protein 95% pure, C-term tagged one 75% pure
Cloned/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
amplified gene cloned into the pGEM-T Easy vector, heterologous expression with a His-tag alternatively placed in the N- or C-terminus in Escherichia coli BL21 Star (DE3) cells
expressed in Escherichia coli BL21 cells
-
‘Greensleeves’ apple is transformed with a cDNA encoding aldose 6-phosphate reductase in the antisense orientation. Antisense expression of A6PR decreases A6PR activity in mature leaves to approximately 15-30% of the untransformed control. The antisense plants have lower concentrations of sorbitol but higher concentrations of sucrose and starch in mature leaves at both dusk and predawn
-
EXPRESSION
ORGANISM
UNIPROT
LITERATURE
At 400 mM sucrose and 400 mM fructose, transcription increases by approximately 4fold. Palatinose increases the enzyme transcription much more drastically than sucrose. Mannose and 3-O-methylglucose also increase enzyme transcription
-
enzyme transcription is decreased to 40% by 800 mM sorbitol
-