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Literature summary for 1.8.1.11 extracted from
- Asparagusate dehydrogenase and lipoyl deydrogenase from Asparagus (1979), Methods Enzymol., 62, 172-181.
General Stability
| General Stability | Organism |
|---|---|
| EDTA ion stabilizes the enzyme | Asparagus officinalis |
| PO43- stabilizes the enzyme | Asparagus officinalis |
Inhibitors
| Inhibitors | Comment | 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 | Comment | Organism | Structure |
|---|---|---|---|---|---|
| 0.8 | - |
potassium ferricyanide | enzyme II | Asparagus officinalis | |
| 0.9 | - |
potassium ferricyanide | enzyme I | Asparagus officinalis | |
| 3 | - |
lipoic acid | - |
Asparagus officinalis | |
| 20 | - |
asparagusic acid | - |
Asparagus officinalis | |
Localization
| Localization | Comment | Organism | GeneOntology No. | Textmining |
|---|---|---|---|---|
| mitochondrion | - |
Asparagus officinalis | 5739 | - |
Molecular Weight [Da]
| Molecular Weight [Da] | Molecular Weight Maximum [Da] | Comment | Organism |
|---|---|---|---|
| 110000 | 111000 | enzyme I and II, sedimentation equilibrium | Asparagus officinalis |
| 112000 | - |
calculation of amino acid content | Asparagus officinalis |
| 112000 | - |
enzyme I and II, gel filtration | Asparagus officinalis |
Natural Substrates/ Products (Substrates)
| Natural Substrates | Organism | Comment (Nat. Sub.) | Natural Products | Comment (Nat. Pro.) | Rev. | Reac. |
|---|---|---|---|---|---|---|
| asparagusate + NADH | Asparagus officinalis | essential component of pyruvate dehydrogenase complex | dihydroasparagusate + NAD+ | - |
r | |
Organism
| Organism | UniProt | Comment | Textmining |
|---|---|---|---|
| Asparagus officinalis | - |
2 asparagusate dehydrogenases with lipoyl dehydrogenase activity | - |
| Asparagus officinalis | - |
etiolated or green, activity levels are higher in etiolated than in green shoots | - |
Purification (Commentary)
| Purification (Comment) | Organism |
|---|---|
| gel filtration, ion-exchange, copurification of enzyme I and II | Asparagus officinalis |
Reaction
| Reaction | Comment | Organism | Reaction ID |
|---|---|---|---|
| 3-mercapto-2-mercaptomethylpropanoate + NAD+ = asparagusate + NADH + H+ | exhibits lipoyl dehydrogenase activity | Asparagus officinalis | |
| 3-mercapto-2-mercaptomethylpropanoate + NAD+ = asparagusate + NADH + H+ | exhibits diaphorase activity | Asparagus officinalis |
Source Tissue
| Source Tissue | Comment | 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] | Comment | 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 | Comment Substrates | Organism | Products | Comment (Products) | Rev. | Reac. |
|---|---|---|---|---|---|---|
| 2 ferricyanide + NADH | - |
Asparagus officinalis | 2 ferrocyanide + NAD+ + H+ | - |
? | |
| asparagusate + NADH | essential component of pyruvate dehydrogenase complex | Asparagus officinalis | dihydroasparagusate + NAD+ | - |
r | |
| asparagusic acid + NADH | reverse reaction very slow | Asparagus officinalis | dihydroasparagusate + NAD+ | - |
r | |
| lipoic acid + NADH | reverse reaction very slow | Asparagus officinalis | dihydrolipoic acid + NAD+ | - |
r | |
| NADH + H+ + potassium ferricyanide | - |
Asparagus officinalis | NAD+ + potassium ferrocyanide | - |
r | |
Temperature Optimum [°C]
| Temperature Optimum [°C] | Temperature Optimum Maximum [°C] | Comment | Organism |
|---|---|---|---|
| 25 | - |
assay at | Asparagus officinalis |
| 40 | 45 | - |
Asparagus officinalis |
Temperature Stability [°C]
| Temperature Stability Minimum [°C] | Temperature Stability Maximum [°C] | Comment | Organism |
|---|---|---|---|
| 50 | - |
5 min, activity completely retained | Asparagus officinalis |
| 50 | - |
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 | Comment | Organism |
|---|---|---|---|
| 5.25 | - |
for K3Fe(CN)6 reduction | Asparagus officinalis |
| 5.9 | - |
- |
Asparagus officinalis |
Cofactor
| Cofactor | Comment | 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 | no replacement of NADH by NADPH | Asparagus officinalis | |
| NADH | 0.1 mM optimal concentration for maximal activity | Asparagus officinalis | |
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Release 2023.1 (January 2023)
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