EC Number | Activating Compound | Comment | Organism | Structure |
---|---|---|---|---|
1.6.5.4 | NADH | NADH is the preferred electron donor | Physcomitrium patens | |
1.6.5.4 | NADPH | NADH is the preferred electron donor | Physcomitrium patens |
EC Number | Cloned (Comment) | Organism |
---|---|---|
1.6.5.4 | expression in Escherichia coli | Physcomitrium patens |
EC Number | Protein Variants | Comment | Organism |
---|---|---|---|
1.6.5.4 | C69A | mutation has a negligible effect on enzyme activity under standard reaction conditions. The C69A mutant is more resistant to the inhibitory effects of beta-chloromercuribenzoate than the wild type PpMDHAR2 protein | Physcomitrium patens |
EC Number | Inhibitors | Comment | Organism | Structure |
---|---|---|---|---|
1.6.5.4 | beta-chloromercuribenzoate | PpMDHAR1 is almost completely inactivated after a 20 min preincubation with 0.25 mM beta-chloromercuribenzoate. At 0.05 mM the enzyme retains 11% of the initial activity. | Physcomitrium patens | |
1.6.5.4 | chloromercuribenzoate | at 0.05 mM PpMDHAR3 retains 80% of the initial activity; PpMDHAR2 is almost completely inactivated after a 20 min preincubation with 0.25 mM chloromercuribenzoate. At 0.05 mM the enzyme retains 14% of the initial activity. The C69A mutant is more resistant to the inhibitory effects of chloromercuribenzoate than the wild type PpMDHAR2 protein | Physcomitrium patens |
EC Number | KM Value [mM] | KM Value Maximum [mM] | Substrate | Comment | Organism | Structure |
---|---|---|---|---|---|---|
1.6.5.4 | 0.0078 | - |
NADH | - |
Physcomitrium patens | |
1.6.5.4 | 0.0096 | - |
NADH | - |
Physcomitrium patens | |
1.6.5.4 | 0.0178 | - |
NADH | - |
Physcomitrium patens | |
1.6.5.4 | 0.088 | - |
NADPH | - |
Physcomitrium patens | |
1.6.5.4 | 0.223 | - |
NADPH | - |
Physcomitrium patens | |
1.6.5.4 | 0.99 | - |
NADPH | - |
Physcomitrium patens |
EC Number | Organism | UniProt | Comment | Textmining |
---|---|---|---|---|
1.6.5.4 | Physcomitrium patens | Q2I826 | - |
- |
1.6.5.4 | Physcomitrium patens | Q2I827 | - |
- |
1.6.5.4 | Physcomitrium patens | Q2I828 | - |
- |
EC Number | Reaction | Comment | Organism | Reaction ID |
---|---|---|---|---|
1.6.5.4 | NADH + H+ + 2 monodehydroascorbate = NAD+ + 2 ascorbate | PpMDHARs follow a ping-pong kinetic mechanism | Physcomitrium patens |
EC Number | Specific Activity Minimum [µmol/min/mg] | Specific Activity Maximum [µmol/min/mg] | Comment | Organism |
---|---|---|---|---|
1.6.5.4 | 152 | - |
- |
Physcomitrium patens |
1.6.5.4 | 164 | - |
- |
Physcomitrium patens |
EC Number | Substrates | Comment Substrates | Organism | Products | Comment (Products) | Rev. | Reac. |
---|---|---|---|---|---|---|---|
1.6.5.4 | NADH + monodehydroascorbate | - |
Physcomitrium patens | NAD+ + ascorbate | - |
? | |
1.6.5.4 | NADPH + monodehydroascorbate | NADH is the preferred electron donor | Physcomitrium patens | NADP+ + ascorbate | - |
? |
EC Number | Synonyms | Comment | Organism |
---|---|---|---|
1.6.5.4 | MDHAR1 | - |
Physcomitrium patens |
1.6.5.4 | MDHAR2 | - |
Physcomitrium patens |
1.6.5.4 | MDHAR3 | - |
Physcomitrium patens |
1.6.5.4 | monodehydroascorbate reductase | - |
Physcomitrium patens |
1.6.5.4 | PpMDHAR1 | - |
Physcomitrium patens |
1.6.5.4 | PpMDHAR2 | - |
Physcomitrium patens |
1.6.5.4 | PpMDHAR3 | - |
Physcomitrium patens |
EC Number | Turnover Number Minimum [1/s] | Turnover Number Maximum [1/s] | Substrate | Comment | Organism | Structure |
---|---|---|---|---|---|---|
1.6.5.4 | 119 | - |
NADH | - |
Physcomitrium patens | |
1.6.5.4 | 128 | - |
NADH | - |
Physcomitrium patens | |
1.6.5.4 | 170 | - |
NADH | - |
Physcomitrium patens |
EC Number | pH Optimum Minimum | pH Optimum Maximum | Comment | Organism |
---|---|---|---|---|
1.6.5.4 | 8.1 | - |
- |
Physcomitrium patens |
EC Number | pH Minimum | pH Maximum | Comment | Organism |
---|---|---|---|---|
1.6.5.4 | 7.6 | 8.7 | 85% or greater activity between pH 7.6 and pH 8.7 | Physcomitrium patens |
EC Number | Cofactor | Comment | Organism | Structure |
---|---|---|---|---|
1.6.5.4 | FAD | contains a single non-covalently bound FAD coenzyme molecule | Physcomitrium patens | |
1.6.5.4 | NADH | NADH is the preferred electron donor | Physcomitrium patens | |
1.6.5.4 | NADPH | NADH is the preferred electron donor | Physcomitrium patens |