Inhibitors | Comment | Organism | Structure |
---|---|---|---|
pyruvate | inhibited by an excess of substrate pyruvate; substrate inhibition, in excess, pyruvate enters in competition with the other substrate (glycine and/or NADH) preventing the site of reaction to take all the substrates to proceed with the enzymatic reaction. Its optimal concentration is determined to be round 2.0-2.3 mM | Suberites domuncula |
KM Value [mM] | KM Value Maximum [mM] | Substrate | Comment | Organism | Structure |
---|---|---|---|---|---|
0.34 | - |
pyruvate | pH 7.0, 30°C | Suberites domuncula | |
0.34 | - |
pyruvate | determined using constant cosubstrate concentrations (100 mM glycine and 0.3 mM NADH, pH 7.0) | Suberites domuncula |
Molecular Weight [Da] | Molecular Weight Maximum [Da] | Comment | Organism |
---|---|---|---|
35000 | - |
native PAGE | Suberites domuncula |
35000 | - |
semi-native PAGE | Suberites domuncula |
75000 | - |
native PAGE | Suberites domuncula |
75000 | - |
semi-native PAGE two bands at 35 kDa and 75 kDa are visible | Suberites domuncula |
Organism | UniProt | Comment | Textmining |
---|---|---|---|
Suberites domuncula | B1GT63 | - |
- |
Specific Activity Minimum [µmol/min/mg] | Specific Activity Maximum [µmol/min/mg] | Comment | Organism |
---|---|---|---|
0.079 | - |
- |
Suberites domuncula |
Substrates | Comment Substrates | Organism | Products | Comment (Products) | Rev. | Reac. |
---|---|---|---|---|---|---|
Gly + pyruvate + NADH | the enzyme is highly specific to glycine. No enzyme activity is observed when other amino acids (alanine and taurine) are used as substrates in the experiment | Suberites domuncula | D-Strombine + NAD+ + H2O | - |
? | |
glycine + pyruvate + NADH | enzyme is specific for glycine | Suberites domuncula | D-strombine + NAD+ + H2O | - |
? |
Subunits | Comment | Organism |
---|---|---|
dimer | native PAGE and semi-native PAGE, 2 * 35000 Da | Suberites domuncula |
dimer | native and semi-native PAGE analysis, 2 * 35000 | Suberites domuncula |
Synonyms | Comment | Organism |
---|---|---|
StDH | shows 68% sequence identity with the tauropine dehydrogenase protein from the marine demosponge Halichondria japonica | Suberites domuncula |
strombine dehydrogenase | - |
Suberites domuncula |
Temperature Optimum [°C] | Temperature Optimum Maximum [°C] | Comment | Organism |
---|---|---|---|
30 | - |
assay at | Suberites domuncula |
pH Optimum Minimum | pH Optimum Maximum | Comment | Organism |
---|---|---|---|
7 | - |
assay at | Suberites domuncula |
7 | - |
assay at and optimal pH | Suberites domuncula |
Cofactor | Comment | Organism | Structure |
---|---|---|---|
NADH | - |
Suberites domuncula | |
NADH | enzyme shows an absolute requirement for NADH | Suberites domuncula |