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Literature summary for 5.3.2.2 extracted from
- Regulation of succinate dehydrogenase and tautomerization of oxaloacetate (1989), Adv. Enzyme Regul., 28, 271-280.
Activating Compound
| Activating Compound | Comment | Organism | Structure |
|---|---|---|---|
| Acid-labile sulfur | enzyme form OAT-2 contains 2 atoms of acid-labile sulfur | Bos taurus |
Inhibitors
| Inhibitors | Comment | Organism | Structure |
|---|---|---|---|
| diphosphate | enzyme form OAT-2 is inhibited, enzyme form OAT-1 not | Bos taurus |  |
| Fluorocitrate | inhibition of OAT-2, tautomerase reaction and aconitase reaction | Bos taurus | |
| Maleate | enzyme form OAT-2 is inhibited, enzyme form OAT-1 not | Bos taurus | |
| NEM | enzyme form OAT-2 is inhibited, enzyme form OAT-1 not | Bos taurus | |
| oxalate | enzyme form OAT-1 is inhibited, enzyme form OAT-2 not | Bos taurus | |
KM Value [mM]
| KM Value [mM] | KM Value Maximum [mM] | Substrate | Comment | Organism | Structure |
|---|---|---|---|---|---|
| 0.045 | - |
enol-oxaloacetate | enzyme form OAT-1 | Bos taurus | |
| 0.068 | - |
keto-oxaloacetate | enzyme form OAT-1 | Bos taurus | |
| 220 | - |
enol-oxaloacetate | enzyme form OAT-2 | Bos taurus | |
Localization
| Localization | Comment | Organism | GeneOntology No. | Textmining |
|---|---|---|---|---|
| mitochondrial matrix | - |
Bos taurus | 5759 | - |
Metals/Ions
| Metals/Ions | Comment | Organism | Structure |
|---|---|---|---|
| Fe | enzyme form OAT-2 contains 2 atoms of non-heme Fe per mol | Bos taurus | |
Molecular Weight [Da]
| Molecular Weight [Da] | Molecular Weight Maximum [Da] | Comment | Organism |
|---|---|---|---|
| 37000 | - |
enzyme form OAT-1 | Bos taurus |
| 80000 | - |
enzyme form OAT-2 | Bos taurus |
Natural Substrates/ Products (Substrates)
| Natural Substrates | Organism | Comment (Nat. Sub.) | Natural Products | Comment (Nat. Pro.) | Rev. | Reac. |
|---|---|---|---|---|---|---|
| additional information | Bos taurus | significant role of enzymatic oxaloacetate tautomerization in the control of the succinate dehydrogenase activity in the mitochondrial matrix | ? | - |
? | |
Organism
| Organism | UniProt | Comment | Textmining |
|---|---|---|---|
| Bos taurus | - |
enzyme forms OAT-1 and OAT-2 | - |
Source Tissue
| Source Tissue | Comment | Organism | Textmining |
|---|---|---|---|
| heart | - |
Bos taurus | - |
Substrates and Products (Substrate)
| Substrates | Comment Substrates | Organism | Products | Comment (Products) | Rev. | Reac. |
|---|---|---|---|---|---|---|
| keto-Oxaloacetate | r | Bos taurus | Enol-oxaloacetate | - |
? | |
| additional information | OAT-2 catalyzes aconitase reaction after treatment with Fe2+ | Bos taurus | ? | - |
? | |
| additional information | significant role of enzymatic oxaloacetate tautomerization in the control of the succinate dehydrogenase activity in the mitochondrial matrix | Bos taurus | ? | - |
? | |
Subunits
| Subunits | Comment | Organism |
|---|---|---|
| monomer | 1 * 37000, enzyme form OAT-1 | Bos taurus |
| monomer | 1 * 80000, enzyme form OAT-2 | Bos taurus |
Temperature Stability [°C]
| Temperature Stability Minimum [°C] | Temperature Stability Maximum [°C] | Comment | Organism |
|---|---|---|---|
| 40 | - |
enzyme form OAT-1: no inactivation | Bos taurus |
| 40 | - |
enzyme form OAT-2: t1/2: about 15 min | Bos taurus |
Turnover Number [1/s]
| Turnover Number Minimum [1/s] | Turnover Number Maximum [1/s] | Substrate | Comment | Organism | Structure |
|---|---|---|---|---|---|
| 3.58 | - |
keto-oxaloacetate | enzyme form OAT-1, 25°C, pH 9.0 | Bos taurus | |
| 26.7 | - |
enol-oxaloacetate | enzyme form OAT-2, 25°C, pH 9.0 | Bos taurus | |
| 45 | - |
enol-oxaloacetate | enzyme form OAT-1, 25°C, pH 9.0 | Bos taurus | |
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