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

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The enzyme appears in viruses and cellular organisms

EC NUMBER
COMMENTARY hide
1.1.1.200
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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
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REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
oxidation
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redox reaction
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reduction
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PATHWAY
BRENDA Link
KEGG Link
MetaCyc Link
sorbitol biosynthesis I
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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
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ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
apricot, cv. Perfection
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Manually annotated by BRENDA team
pear, cv. Conference, cv. Bartlett
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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
2-deoxy-D-glucose 6-phosphate + NADPH
?
show the reaction diagram
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reduced at low rate
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?
D-galactose 6-phosphate + NADPH
?
show the reaction diagram
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reduced at a higher rate than D-glucose 6-phosphate
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r
D-glucitol-6-phosphate
D-glucose 6-phosphate + NADPH + H+
show the reaction diagram
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r
D-glucose 6-phosphate + NADPH
D-sorbitol 6-phosphate + NADP+
show the reaction diagram
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r
D-glucose 6-phosphate + NADPH + H+
D-glucitol-6-phosphate + NADP+
show the reaction diagram
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r
D-mannose 6-phosphate + NADPH
?
show the reaction diagram
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reduced at low rate
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?
D-sorbitol 6-phosphate + NADP+
D-glucose 6-phosphate + NADPH + H+
show the reaction diagram
additional information
?
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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
additional information
?
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COFACTOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
additional information
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no activity with NAD+ or NADH
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METALS and IONS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
CaCl2
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2.5 mM, in presence of 5 mM substrate, 40% increase in activity
MgCl2
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2.5 mM, in presence of 5 mM substrate, 52% increase in activity
INHIBITORS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
AgNO3
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complete inhibition at 0.1 mM
CaCl2
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2.5 mM, in presence of 50 mM substrate, 12% decrease in activity
cysteine
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47% inhibition of oxidation and 11% inhibition of reduction at 10 mM
iodoacetate
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42% inhibition of oxidation and 19% inhibition of reduction at 10 mM
MgCl2
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2.5 mM, in presence of 50 mM substrate, 12% decrease in activity
Na2EDTA
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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
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complete inhibition at 1.0 mM
phosphate
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mixed-type inhibition
ZnCl2
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2 mM, 58% inhibition, partially reversible by EDTA
ZnSO4
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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
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ACTIVATING COMPOUND
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
additional information
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enzyme activity is rapidly induced by water stress
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KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.2
D-glucose 6-phosphate
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5.1 - 9.8
D-Glucose-6-phosphate
3.9
D-sorbitol 6-phosphate
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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
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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
1.25
N-term tagged enzyme, 9.2fold purified
7.94
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pH 9.0
13530
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leaf base
18400
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leaf tip
additional information
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
9.5
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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
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about 50% of activity maximum at pH 8.5 and 10.1
TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
30 - 35
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D-sorbitol 6-phosphate oxidation
35
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D-glucose 6-phosphate reduction
TEMPERATURE RANGE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
additional information
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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
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Manually annotated by BRENDA team
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
33000
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2 * 33000, SDS-PAGE
34900
sequence analysis, A6PRase
39000
gel filtration, C-term tagged enzyme
SUBUNITS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
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
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Purification/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
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
‘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
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