BRENDA - Enzyme Database show
show all sequences of 1.8.1.11

Asparagusate dehydrogenase and lipoyl deydrogenase from Asparagus

Yanagawa, H.; Methods Enzymol. 62, 172-181 (1979)

Data extracted from this reference:

General Stability
General Stability
Organism
EDTA ion stabilizes the enzyme
Asparagus officinalis
PO43- stabilizes the enzyme
Asparagus officinalis
Inhibitors
Inhibitors
Commentary
Organism
Structure
arsenite
low inhibition
Asparagus officinalis
asparagusic acid
inhibits lipoyl dehydrogenase activity
Asparagus officinalis
Hg2+
inhibitory
Asparagus officinalis
iodoacetamide
low inhibition
Asparagus officinalis
additional information
inhibitors indicate an involvement of protein disulfide linkage or thiol group in the catalytic site
Asparagus officinalis
N-ethylmaleimide
-
Asparagus officinalis
NADH
above 0.1 mM
Asparagus officinalis
p-chloromercuribenzoic acid
-
Asparagus officinalis
KM Value [mM]
KM Value [mM]
KM Value Maximum [mM]
Substrate
Commentary
Organism
Structure
0.8
-
K3Fe(CN)6
enzyme II
Asparagus officinalis
0.9
-
K3Fe(CN)6
enzyme I
Asparagus officinalis
3
-
lipoic acid
-
Asparagus officinalis
20
-
asparagusic acid
-
Asparagus officinalis
Localization
Localization
Commentary
Organism
GeneOntology No.
Textmining
mitochondrion
-
Asparagus officinalis
5739
-
Molecular Weight [Da]
Molecular Weight [Da]
Molecular Weight Maximum [Da]
Commentary
Organism
110000
111000
enzyme I and II, sedimentation equilibrium
Asparagus officinalis
112000
-
calculation of amino acid content; enzyme I and II, gel filtration
Asparagus officinalis
Natural Substrates/ Products (Substrates)
Natural Substrates
Organism
Commentary (Nat. Sub.)
Natural Products
Commentary (Nat. Pro.)
Organism (Nat. Pro.)
Reversibility
asparagusate + NADH
Asparagus officinalis
essential component of pyruvate dehydrogenase complex
dihydroasparagusate + NAD+
-
Asparagus officinalis
r
Organism
Organism
Primary Accession No. (UniProt)
Commentary
Textmining
Asparagus officinalis
-
2 asparagusate dehydrogenases with lipoyl dehydrogenase activity; etiolated or green, activity levels are higher in etiolated than in green shoots
-
Purification (Commentary)
Commentary
Organism
gel filtration, ion-exchange, copurification of enzyme I and II
Asparagus officinalis
Reaction
Reaction
Commentary
Organism
3-mercapto-2-mercaptomethylpropanoate + NAD+ = asparagusate + NADH + H+
exhibits diaphorase activity; exhibits lipoyl dehydrogenase activity
Asparagus officinalis
Source Tissue
Source Tissue
Commentary
Organism
Textmining
shoot
-
Asparagus officinalis
-
shoot apex
around, higher levels than other regions
Asparagus officinalis
-
Specific Activity [micromol/min/mg]
Specific Activity Minimum [µmol/min/mg]
Specific Activity Maximum [µmol/min/mg]
Commentary
Organism
0.215
-
enzyme/fraction II towards asparagusic acid
Asparagus officinalis
0.425
-
enzyme/fraction I towards asparagusic acid
Asparagus officinalis
0.5464
-
enzyme/fraction II towards lipoic acid
Asparagus officinalis
1.082
-
enzyme/fraction I towards lipoic acid
Asparagus officinalis
Storage Stability
Storage Stability
Organism
-80°C, 67 mM sodium phosphate, pH 7.0, no loss of activity for at least 1 month
Asparagus officinalis
4°C, 67 mM sodium phosphate, pH 7.0, very unstable
Asparagus officinalis
Substrates and Products (Substrate)
Substrates
Commentary Substrates
Literature (Substrates)
Organism
Products
Commentary (Products)
Literature (Products)
Organism (Products)
Reversibility
2 ferricyanide + NADH
-
394702
Asparagus officinalis
2 ferrocyanide + NAD+ + H+
-
394702
Asparagus officinalis
?
asparagusate + NADH
essential component of pyruvate dehydrogenase complex
394702
Asparagus officinalis
dihydroasparagusate + NAD+
-
394702
Asparagus officinalis
r
asparagusic acid + NADH
reverse reaction very slow
394702
Asparagus officinalis
dihydroasparagusate + NAD+
-
394702
Asparagus officinalis
r
lipoic acid + NADH
reverse reaction very slow
394702
Asparagus officinalis
dihydrolipoic acid + NAD+
-
394702
Asparagus officinalis
r
Temperature Optimum [°C]
Temperature Optimum [°C]
Temperature Optimum Maximum [°C]
Commentary
Organism
25
-
assay at
Asparagus officinalis
40
45
-
Asparagus officinalis
Temperature Stability [°C]
Temperature Stability Minimum [°C]
Temperature Stability Maximum [°C]
Commentary
Organism
50
-
5 min, activity completely retained; above, gradual loss of lipoyl dehydrogenase activity, complete loss at 90°C
Asparagus officinalis
60
70
5 min, 1.4-fold activation of asparagusate dehydrogenase activity
Asparagus officinalis
pH Optimum
pH Optimum Minimum
pH Optimum Maximum
Commentary
Organism
5.25
-
for K3Fe(CN)6 reduction
Asparagus officinalis
5.9
-
-
Asparagus officinalis
Cofactor
Cofactor
Commentary
Organism
Structure
FAD
flavoprotein, approximately 1 mol of FAD per mol of protein
Asparagus officinalis
NAD+
up to 0.2 mM, stimulates the reduction activity if NADH concentration is 0.2 mM
Asparagus officinalis
NADH
0.1 mM optimal concentration for maximal activity; no replacement of NADH by NADPH
Asparagus officinalis
Cofactor (protein specific)
Cofactor
Commentary
Organism
Structure
FAD
flavoprotein, approximately 1 mol of FAD per mol of protein
Asparagus officinalis
NAD+
up to 0.2 mM, stimulates the reduction activity if NADH concentration is 0.2 mM
Asparagus officinalis
NADH
0.1 mM optimal concentration for maximal activity; no replacement of NADH by NADPH
Asparagus officinalis
General Stability (protein specific)
General Stability
Organism
EDTA ion stabilizes the enzyme
Asparagus officinalis
PO43- stabilizes the enzyme
Asparagus officinalis
Inhibitors (protein specific)
Inhibitors
Commentary
Organism
Structure
arsenite
low inhibition
Asparagus officinalis
asparagusic acid
inhibits lipoyl dehydrogenase activity
Asparagus officinalis
Hg2+
inhibitory
Asparagus officinalis
iodoacetamide
low inhibition
Asparagus officinalis
additional information
inhibitors indicate an involvement of protein disulfide linkage or thiol group in the catalytic site
Asparagus officinalis
N-ethylmaleimide
-
Asparagus officinalis
NADH
above 0.1 mM
Asparagus officinalis
p-chloromercuribenzoic acid
-
Asparagus officinalis
KM Value [mM] (protein specific)
KM Value [mM]
KM Value Maximum [mM]
Substrate
Commentary
Organism
Structure
0.8
-
K3Fe(CN)6
enzyme II
Asparagus officinalis
0.9
-
K3Fe(CN)6
enzyme I
Asparagus officinalis
3
-
lipoic acid
-
Asparagus officinalis
20
-
asparagusic acid
-
Asparagus officinalis
Localization (protein specific)
Localization
Commentary
Organism
GeneOntology No.
Textmining
mitochondrion
-
Asparagus officinalis
5739
-
Molecular Weight [Da] (protein specific)
Molecular Weight [Da]
Molecular Weight Maximum [Da]
Commentary
Organism
110000
111000
enzyme I and II, sedimentation equilibrium
Asparagus officinalis
112000
-
calculation of amino acid content; enzyme I and II, gel filtration
Asparagus officinalis
Natural Substrates/ Products (Substrates) (protein specific)
Natural Substrates
Organism
Commentary (Nat. Sub.)
Natural Products
Commentary (Nat. Pro.)
Organism (Nat. Pro.)
Reversibility
asparagusate + NADH
Asparagus officinalis
essential component of pyruvate dehydrogenase complex
dihydroasparagusate + NAD+
-
Asparagus officinalis
r
Purification (Commentary) (protein specific)
Commentary
Organism
gel filtration, ion-exchange, copurification of enzyme I and II
Asparagus officinalis
Source Tissue (protein specific)
Source Tissue
Commentary
Organism
Textmining
shoot
-
Asparagus officinalis
-
shoot apex
around, higher levels than other regions
Asparagus officinalis
-
Specific Activity [micromol/min/mg] (protein specific)
Specific Activity Minimum [µmol/min/mg]
Specific Activity Maximum [µmol/min/mg]
Commentary
Organism
0.215
-
enzyme/fraction II towards asparagusic acid
Asparagus officinalis
0.425
-
enzyme/fraction I towards asparagusic acid
Asparagus officinalis
0.5464
-
enzyme/fraction II towards lipoic acid
Asparagus officinalis
1.082
-
enzyme/fraction I towards lipoic acid
Asparagus officinalis
Storage Stability (protein specific)
Storage Stability
Organism
-80°C, 67 mM sodium phosphate, pH 7.0, no loss of activity for at least 1 month
Asparagus officinalis
4°C, 67 mM sodium phosphate, pH 7.0, very unstable
Asparagus officinalis
Substrates and Products (Substrate) (protein specific)
Substrates
Commentary Substrates
Literature (Substrates)
Organism
Products
Commentary (Products)
Literature (Products)
Organism (Products)
Reversibility
2 ferricyanide + NADH
-
394702
Asparagus officinalis
2 ferrocyanide + NAD+ + H+
-
394702
Asparagus officinalis
?
asparagusate + NADH
essential component of pyruvate dehydrogenase complex
394702
Asparagus officinalis
dihydroasparagusate + NAD+
-
394702
Asparagus officinalis
r
asparagusic acid + NADH
reverse reaction very slow
394702
Asparagus officinalis
dihydroasparagusate + NAD+
-
394702
Asparagus officinalis
r
lipoic acid + NADH
reverse reaction very slow
394702
Asparagus officinalis
dihydrolipoic acid + NAD+
-
394702
Asparagus officinalis
r
Temperature Optimum [°C] (protein specific)
Temperature Optimum [°C]
Temperature Optimum Maximum [°C]
Commentary
Organism
25
-
assay at
Asparagus officinalis
40
45
-
Asparagus officinalis
Temperature Stability [°C] (protein specific)
Temperature Stability Minimum [°C]
Temperature Stability Maximum [°C]
Commentary
Organism
50
-
5 min, activity completely retained; above, gradual loss of lipoyl dehydrogenase activity, complete loss at 90°C
Asparagus officinalis
60
70
5 min, 1.4-fold activation of asparagusate dehydrogenase activity
Asparagus officinalis
pH Optimum (protein specific)
pH Optimum Minimum
pH Optimum Maximum
Commentary
Organism
5.25
-
for K3Fe(CN)6 reduction
Asparagus officinalis
5.9
-
-
Asparagus officinalis
Other publictions for EC 1.8.1.11
No.
1st author
Pub Med
title
organims
journal
volume
pages
year
Activating Compound
Application
Cloned(Commentary)
Crystallization (Commentary)
Engineering
General Stability
Inhibitors
KM Value [mM]
Localization
Metals/Ions
Molecular Weight [Da]
Natural Substrates/ Products (Substrates)
Organic Solvent Stability
Organism
Oxidation Stability
Posttranslational Modification
Purification (Commentary)
Reaction
Renatured (Commentary)
Source Tissue
Specific Activity [micromol/min/mg]
Storage Stability
Substrates and Products (Substrate)
Subunits
Temperature Optimum [°C]
Temperature Range [°C]
Temperature Stability [°C]
Turnover Number [1/s]
pH Optimum
pH Range
pH Stability
Cofactor
Ki Value [mM]
pI Value
IC50 Value
Activating Compound (protein specific)
Application (protein specific)
Cloned(Commentary) (protein specific)
Cofactor (protein specific)
Crystallization (Commentary) (protein specific)
Engineering (protein specific)
General Stability (protein specific)
IC50 Value (protein specific)
Inhibitors (protein specific)
Ki Value [mM] (protein specific)
KM Value [mM] (protein specific)
Localization (protein specific)
Metals/Ions (protein specific)
Molecular Weight [Da] (protein specific)
Natural Substrates/ Products (Substrates) (protein specific)
Organic Solvent Stability (protein specific)
Oxidation Stability (protein specific)
Posttranslational Modification (protein specific)
Purification (Commentary) (protein specific)
Renatured (Commentary) (protein specific)
Source Tissue (protein specific)
Specific Activity [micromol/min/mg] (protein specific)
Storage Stability (protein specific)
Substrates and Products (Substrate) (protein specific)
Subunits (protein specific)
Temperature Optimum [°C] (protein specific)
Temperature Range [°C] (protein specific)
Temperature Stability [°C] (protein specific)
Turnover Number [1/s] (protein specific)
pH Optimum (protein specific)
pH Range (protein specific)
pH Stability (protein specific)
pI Value (protein specific)
Expression
General Information
General Information (protein specific)
Expression (protein specific)
KCat/KM [mM/s]
KCat/KM [mM/s] (protein specific)
394701
Yanagawa
-
Asparagusate reductase ...
Asparagus officinalis
Methods Enzymol.
143
516-521
1987
-
-
-
-
-
2
1
4
-
-
2
1
-
1
-
-
1
1
-
1
2
2
4
-
1
-
2
-
2
-
-
2
-
-
-
-
-
-
2
-
-
2
-
1
-
4
-
-
2
1
-
-
-
1
-
1
2
2
4
-
1
-
2
-
2
-
-
-
-
-
-
-
-
-
394702
Yanagawa
Asparagusate dehydrogenase and ...
Asparagus officinalis
Methods Enzymol.
62
172-181
1979
-
-
-
-
-
2
8
4
1
-
2
1
-
2
-
-
1
1
-
2
4
2
4
-
2
-
2
-
2
-
-
3
-
-
-
-
-
-
3
-
-
2
-
8
-
4
1
-
2
1
-
-
-
1
-
2
4
2
4
-
2
-
2
-
2
-
-
-
-
-
-
-
-
-
394703
Yanagawa
Asparagusate dehydrogenases an ...
Asparagus officinalis
J. Biol. Chem.
251
3637-3644
1976
3
-
-
-
-
-
10
6
2
-
2
1
-
2
-
-
1
1
-
1
4
-
4
-
2
-
2
-
2
-
-
3
-
-
-
3
-
-
3
-
-
-
-
10
-
6
2
-
2
1
-
-
-
1
-
1
4
-
4
-
2
-
2
-
2
-
-
-
-
-
-
-
-
-
394704
Yanagawa
Asparagusate dehydrogenases an ...
Asparagus officinalis
Biochim. Biophys. Acta
384
342-352
1975
2
-
-
-
-
2
3
-
1
-
-
1
-
2
-
-
1
-
-
1
4
2
3
-
1
-
-
-
1
-
-
-
-
-
-
2
-
-
-
-
-
2
-
3
-
-
1
-
-
1
-
-
-
1
-
1
4
2
3
-
1
-
-
-
1
-
-
-
-
-
-
-
-
-