EC Number | Cloned (Comment) | Organism |
---|---|---|
1.1.1.61 | expressed as a histidine-tagged recombinant protein in Escherichia coli | Escherichia coli |
EC Number | KM Value [mM] | KM Value Maximum [mM] | Substrate | Comment | Organism | Structure |
---|---|---|---|---|---|---|
1.1.1.61 | 1 | - |
3-hydroxypropane sulfonate | - |
Escherichia coli | |
1.1.1.61 | 1 | - |
3-hydroxypropane sulfonate | in 100 mM Tris-HCl buffer (pH 8.8), at 37°C | Escherichia coli | |
1.1.1.61 | 4.3 | - |
Succinic semialdehyde | - |
Escherichia coli | |
1.1.1.61 | 4.3 | - |
Succinic semialdehyde | in 100 mM MOPS-KOH buffer (pH 7.2), at 37°C | Escherichia coli | |
1.1.1.61 | 9 | - |
methylglyoxal | - |
Escherichia coli | |
1.1.1.61 | 9 | - |
methylglyoxal | in 100 mM Tris-HCl buffer (pH 8.8), at 37°C | Escherichia coli | |
1.1.1.61 | 102 | - |
4-hydroxybutyrate | - |
Escherichia coli | |
1.1.1.61 | 102 | - |
gamma-hydroxybutyrate | in 100 mM Tris-HCl buffer (pH 8.8), at 37°C | Escherichia coli |
EC Number | Metals/Ions | Comment | Organism | Structure |
---|---|---|---|---|
1.1.1.61 | additional information | no significant differences in the activity are observed when using different divalent metals (Mg2+, Mn2+, Ca2+, Co2+, and Zn2+) | Escherichia coli |
EC Number | Molecular Weight [Da] | Molecular Weight Maximum [Da] | Comment | Organism |
---|---|---|---|---|
1.1.1.61 | 31154 | - |
4 * 31154, calculated from amino acid sequence | Escherichia coli |
1.1.1.61 | 143000 | - |
gel filtration | Escherichia coli |
EC Number | Natural Substrates | Organism | Comment (Nat. Sub.) | Natural Products | Comment (Nat. Pro.) | Rev. | Reac. |
---|---|---|---|---|---|---|---|
1.1.1.61 | gamma-hydroxybutyrate + NAD+ | Escherichia coli | - |
succinic semialdehyde + NADH + H+ | - |
r | |
1.1.1.61 | succinic semialdehyde + NADH + H+ | Escherichia coli | succinic semialdehyde is the preferred substrate | gamma-hydroxybutyrate + NAD+ | - |
r |
EC Number | Organism | UniProt | Comment | Textmining |
---|---|---|---|---|
1.1.1.61 | Escherichia coli | - |
- |
- |
1.1.1.61 | Escherichia coli | P0A9V8 | - |
- |
1.1.1.61 | Escherichia coli K12 BW25113 | P0A9V8 | - |
- |
EC Number | Purification (Comment) | Organism |
---|---|---|
1.1.1.61 | purified using cobalt-based immobilized TALON metal affinity chromatography resins with a gravity-flow column | Escherichia coli |
EC Number | Specific Activity Minimum [µmol/min/mg] | Specific Activity Maximum [µmol/min/mg] | Comment | Organism |
---|---|---|---|---|
1.1.1.61 | 0.062 | - |
substrate: gamma-hydroxybutyrate | Escherichia coli |
1.1.1.61 | 0.067 | - |
substrate: methylglyoxal | Escherichia coli |
1.1.1.61 | 0.2 | - |
substrate: succinic semialdehyde | Escherichia coli |
1.1.1.61 | 9 | - |
substrate: 3-hydroxypropane sulfonate | Escherichia coli |
EC Number | Substrates | Comment Substrates | Organism | Products | Comment (Products) | Rev. | Reac. |
---|---|---|---|---|---|---|---|
1.1.1.61 | 3-hydroxypropane sulfonate + NAD+ | - |
Escherichia coli | ? + NADH | - |
? | |
1.1.1.61 | 3-hydroxypropane sulfonate + NAD+ | - |
Escherichia coli K12 BW25113 | ? + NADH | - |
? | |
1.1.1.61 | 3-hydroxypropane sulfonate + NAD+ | - |
Escherichia coli | ? + NADH + H+ | - |
r | |
1.1.1.61 | gamma-hydroxybutyrate + NAD+ | - |
Escherichia coli | succinic semialdehyde + NADH + H+ | - |
r | |
1.1.1.61 | methylglyoxal + NAD+ | - |
Escherichia coli | ? + NADH | - |
? | |
1.1.1.61 | methylglyoxal + NAD+ | - |
Escherichia coli K12 BW25113 | ? + NADH | - |
? | |
1.1.1.61 | methylglyoxal + NAD+ | - |
Escherichia coli | ? + NADH + H+ | - |
r | |
1.1.1.61 | additional information | no activity with D-glycerate and 3-hydroxypropanoate | Escherichia coli | ? | - |
? | |
1.1.1.61 | succinic semialdehyde + NADH + H+ | - |
Escherichia coli | 4-hydroxybutyrate + NAD+ | - |
r | |
1.1.1.61 | succinic semialdehyde + NADH + H+ | - |
Escherichia coli K12 BW25113 | 4-hydroxybutyrate + NAD+ | - |
r | |
1.1.1.61 | succinic semialdehyde + NADH + H+ | succinic semialdehyde is the preferred substrate | Escherichia coli | gamma-hydroxybutyrate + NAD+ | - |
r |
EC Number | Subunits | Comment | Organism |
---|---|---|---|
1.1.1.61 | homotetramer | 4 * 31154, calculated from amino acid sequence | Escherichia coli |
EC Number | Synonyms | Comment | Organism |
---|---|---|---|
1.1.1.61 | gamma-hydroxybutyrate dehydrogenase | - |
Escherichia coli |
1.1.1.61 | GHBDH | - |
Escherichia coli |
1.1.1.61 | uncharacterized oxidoreductase YihU | - |
Escherichia coli |
1.1.1.61 | yihU | - |
Escherichia coli |
EC Number | Cofactor | Comment | Organism | Structure |
---|---|---|---|---|
1.1.1.61 | NAD+ | - |
Escherichia coli | |
1.1.1.61 | NADH | - |
Escherichia coli | |
1.1.1.61 | NADH | the NADH-dependent succinic semialdehyde reductase activity is 4fold higher than that with NADPH | Escherichia coli |
EC Number | General Information | Comment | Organism |
---|---|---|---|
1.1.1.61 | malfunction | a yihU deletion mutant displays reduced tolerance to the cytotoxic effects of exogenous addition of succinic semialdehyde | Escherichia coli |
1.1.1.61 | metabolism | the enzyme is involved in the metabolism of succinic semialdehyde, and other potentially toxic intermediates that may accumulate under stress conditions in Escherichia coli | Escherichia coli |