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The expected taxonomic range for this enzyme is: Asparagus
Synonyms
asparagusate dehydrogenase,
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asparagusate dehydrogenase
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asparagusate reductase (NADH)
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asparagusate reductase (NADH2)
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asparagusic dehydrogenase
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EC 1.6.4.7
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formerly
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NADH2:asparagusate oxidoreductase
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3-mercapto-2-mercaptomethylpropanoate + NAD+ = asparagusate + NADH + H+
3-mercapto-2-mercaptomethylpropanoate + NAD+ = asparagusate + NADH + H+
exhibits lipoyl dehydrogenase activity
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3-mercapto-2-mercaptomethylpropanoate + NAD+ = asparagusate + NADH + H+
exhibits diaphorase activity
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3-mercapto-2-mercaptomethylpropanoate + NAD+ = asparagusate + NADH + H+
also acts on lipoate
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3-mercapto-2-mercaptomethylpropanoate:NAD+ oxidoreductase
Also acts on lipoate.
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2 ferricyanide + NADH
2 ferrocyanide + NAD+ + H+
asparagusate + NADH
dihydroasparagusate + NAD+
asparagusic acid + NADH
dihydroasparagusate + NAD+
lipoic acid + NADH
dihydrolipoic acid + NAD+
NADH + H+ + potassium ferricyanide
NAD+ + potassium ferrocyanide
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r
2 ferricyanide + NADH
2 ferrocyanide + NAD+ + H+
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?
2 ferricyanide + NADH
2 ferrocyanide + NAD+ + H+
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2 ferricyanide + NADH
2 ferrocyanide + NAD+ + H+
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asparagusate + NADH
dihydroasparagusate + NAD+
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r
asparagusate + NADH
dihydroasparagusate + NAD+
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participates in enzymatic pyruvate and alpha-ketoglutarate dehydrogenation
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r
asparagusate + NADH
dihydroasparagusate + NAD+
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essential component of pyruvate dehydrogenase complex
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r
asparagusate + NADH
dihydroasparagusate + NAD+
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essential component of pyruvate dehydrogenase complex
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r
asparagusic acid + NADH
dihydroasparagusate + NAD+
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r
asparagusic acid + NADH
dihydroasparagusate + NAD+
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r
asparagusic acid + NADH
dihydroasparagusate + NAD+
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reverse reaction very slow
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r
asparagusic acid + NADH
dihydroasparagusate + NAD+
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reverse reaction very slow
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r
lipoic acid + NADH
dihydrolipoic acid + NAD+
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r
lipoic acid + NADH
dihydrolipoic acid + NAD+
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r
lipoic acid + NADH
dihydrolipoic acid + NAD+
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reverse reaction very slow
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r
lipoic acid + NADH
dihydrolipoic acid + NAD+
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reverse reaction very slow
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r
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asparagusate + NADH
dihydroasparagusate + NAD+
asparagusate + NADH
dihydroasparagusate + NAD+
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r
asparagusate + NADH
dihydroasparagusate + NAD+
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participates in enzymatic pyruvate and alpha-ketoglutarate dehydrogenation
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r
asparagusate + NADH
dihydroasparagusate + NAD+
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essential component of pyruvate dehydrogenase complex
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r
asparagusate + NADH
dihydroasparagusate + NAD+
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essential component of pyruvate dehydrogenase complex
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r
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FAD
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flavoprotein, approximately 1 mol of FAD per mol of protein
NAD+
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up to 0.2 mM, stimulates the reduction activity if NADH concentration is 0.2 mM
NADH
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no replacement of NADH by NADPH
NADH
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0.1 mM optimal concentration for maximal activity
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arsenite
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low inhibition
asparagusic acid
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inhibits lipoyl dehydrogenase activity
cetyltrimethyl ammonium bromide
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affects lipoyl dehydrogenase activity
FAD
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strongly inhibits the two reductase activities
iodoacetamide
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low inhibition
NAD+
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inactivator during asparagusic acid reduction
p-chloromercuribenzoic acid
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NADH
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above 0.1 mM
NADH
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high concentrations, increase of inhibitory effect by addition of arsenite
additional information
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inhibitors indicate an involvement of protein disulfide linkage or thiol group in the catalytic site
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additional information
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inhibitors indicate an involvement of protein disulfide linkage or thiol group in the catalytic site
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lecithin
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drastic activation of lipoyl dehydrogenase activity, no activation of asparagusate dehydrogenase activity, enzyme II
NAD+
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reduction of lipoic acid is activated
sodium dodecylsulfate
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treatment of mitochondria with at 0.5% for 10-20 min, maximal solubilization of enzyme
Tween 80
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drastic activation of lipoyl dehydrogenase activity, no activation of asparagusate dehydrogenase activity, enzyme II
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20 - 21.5
Asparagusate
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enzyme I and II
3 - 3.3
lipoate
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enzyme I and II
0.8 - 0.9
potassium ferricyanide
0.8
potassium ferricyanide
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enzyme II
0.9
potassium ferricyanide
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enzyme I
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0.064
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enzyme/fraction I towards asparagusic acid
0.08323
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enzyme/fraction II towards asparagusic acid
0.1631
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enzyme/fraction I towards lipoic acid
0.213
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enzyme/fraction II towards lipoic acid
0.215
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enzyme/fraction II towards asparagusic acid
0.425
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enzyme/fraction I towards asparagusic acid
0.5464
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enzyme/fraction II towards lipoic acid
1.082
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enzyme/fraction I towards lipoic acid
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5.25
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for K3Fe(CN)6 reduction
5.9
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5.9
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asparagusic and lipoic acid reduction
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2 asparagusate dehydrogenases with lipoyl dehydrogenase activity
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brenda
etiolated
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brenda
etiolated or green, activity levels are higher in etiolated than in green shoots
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brenda
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brenda
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around, higher levels than other regions
brenda
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brenda
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brenda
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110000 - 111000
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ultracentrifugation
110000 - 111000
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enzyme I and II, sedimentation equilibrium
112000
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calculation of amino acid content
112000
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enzyme I and II, gel filtration
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60 - 70
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5 min, 1.4-fold activation of asparagusate dehydrogenase activity
50
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5 min, activity completely retained
50
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above, gradual loss of lipoyl dehydrogenase activity, complete loss at 90°C
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EDTA ion stabilizes the enzyme
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PO43- stabilizes the enzyme
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-80°C, 67 mM sodium phosphate, pH 7.0, no loss of activity for at least 1 month
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4°C, 67 mM sodium phosphate, pH 7.0, very unstable
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4°C, 67 mM sodium phosphate, pH 7.0, very unstable, complete loss of activity in two weeks
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gel filtration, ion-exchange, copurification of enzyme I and II
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gel filtration, ion-exchange, ultracentrifugation, copurification of type I and II
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SDS-extraction, gel filtration, ion-exchange
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Yanagawa, H.
Asparagusate reductase
Methods Enzymol.
143
516-521
1987
Asparagus officinalis
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brenda
Yanagawa, H.
Asparagusate dehydrogenase and lipoyl deydrogenase from Asparagus
Methods Enzymol.
62
172-181
1979
Asparagus officinalis
brenda
Yanagawa, H.; Egami, F.
Asparagusate dehydrogenases and lipoyl dehydrogenase from Asparagus mitochondria. Physical, chemical, and enzymatic properties
J. Biol. Chem.
251
3637-3644
1976
Asparagus officinalis
brenda
Yanagawa, H.; Egami, F.
Asparagusate dehydrogenases and lipoyl dehydrogenase from Asparagus mitochondria
Biochim. Biophys. Acta
384
342-352
1975
Asparagus officinalis
brenda
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1.8.1.11 asparagusate reductase
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