EC Number | Cloned (Comment) | Organism |
---|---|---|
1.2.1.24 | PCR product cloned into pCR2.1-Topo. Open reading frame ligated into vector QE30. Overexpressed in Escherichia coli M15. Subcloned into pMALc2x and expressed in Escherichia coli TB1 | Drosophila melanogaster |
EC Number | Protein Variants | Comment | Organism |
---|---|---|---|
1.2.1.24 | C196A | loss in specific activity of 55% | Drosophila melanogaster |
1.2.1.24 | C196S | loss in specific activity of 74% | Drosophila melanogaster |
1.2.1.24 | C243S | loss in specific activity of 70% | Drosophila melanogaster |
1.2.1.24 | C311A | decreased SSADH activity to undetectable levels | Drosophila melanogaster |
1.2.1.24 | C311S | decreased SSADH activity to undetectable levels | Drosophila melanogaster |
1.2.1.24 | C502S | loss in specific activity of 93% | Drosophila melanogaster |
1.2.1.24 | E277D | leads to a product with similar specific activity | Drosophila melanogaster |
1.2.1.24 | E277K | charge inversion, which results in recombinant protein totally devoid of detectable SSADH activity | Drosophila melanogaster |
1.2.1.24 | E277Q | concomitant loss of the negative charge, which results in recombinant protein totally devoid of detectable SSADH activity | Drosophila melanogaster |
EC Number | KM Value [mM] | KM Value Maximum [mM] | Substrate | Comment | Organism | Structure |
---|---|---|---|---|---|---|
1.2.1.24 | 0.0047 | - |
succinate semialdehyde | - |
Drosophila melanogaster | |
1.2.1.24 | 0.051 | - |
n-hexanal | - |
Drosophila melanogaster | |
1.2.1.24 | 0.057 | - |
n-Pentanal | - |
Drosophila melanogaster | |
1.2.1.24 | 0.0909 | - |
NAD+ | - |
Drosophila melanogaster | |
1.2.1.24 | 0.106 | - |
n-Butanal | - |
Drosophila melanogaster | |
1.2.1.24 | 1.2 | - |
NADP+ | - |
Drosophila melanogaster |
EC Number | Molecular Weight [Da] | Molecular Weight Maximum [Da] | Comment | Organism |
---|---|---|---|---|
1.2.1.24 | 98200 | - |
x * 98200, SDS-PAGE | Drosophila melanogaster |
EC Number | Organism | UniProt | Comment | Textmining |
---|---|---|---|---|
1.2.1.24 | Drosophila melanogaster | Q9VBP6 | - |
- |
EC Number | Purification (Comment) | Organism |
---|---|---|
1.2.1.24 | by Ni2+-NTA agarose chromatography | Drosophila melanogaster |
EC Number | Storage Stability | Organism |
---|---|---|
1.2.1.24 | 0°C, 100 mM sodium phosphate, pH 8.5, 1mM DTT, 43% glycerol, 3 years | Drosophila melanogaster |
EC Number | Substrates | Comment Substrates | Organism | Products | Comment (Products) | Rev. | Reac. |
---|---|---|---|---|---|---|---|
1.2.1.24 | m-carboxybenzaldehyde + NAD+ + H2O | - |
Drosophila melanogaster | m-carboxybenzoate + NADH + H+ | - |
? | |
1.2.1.24 | m-methylcarboxybenzaldehyde + NAD+ + H2O | - |
Drosophila melanogaster | m-methylcarboxybenzoate + NADH + H+ | - |
? | |
1.2.1.24 | additional information | no activity with formaldehyde, o-nitrobenzaldehyde, o-carboxybenzaldehyde, o-tolualdehyde, p-tolualdehyde, o-methoxybenzaldehyde, p-methoxybenzaldehyde o-hydroxybenzaldehyde, m-hydroxybenzaldehyde, phenylacetaldehyde and glyoxylic acid | Drosophila melanogaster | ? | - |
? | |
1.2.1.24 | n-butanal + NAD+ + H2O | - |
Drosophila melanogaster | butanoate + NADH + H+ | - |
? | |
1.2.1.24 | n-hexanal + NAD+ + H2O | - |
Drosophila melanogaster | hexanoate + NADH + H+ | - |
? | |
1.2.1.24 | n-octanal + NAD+ + H2O | - |
Drosophila melanogaster | n-octanoate + NADH + H+ | - |
? | |
1.2.1.24 | n-pentanal + NAD+ + H2O | - |
Drosophila melanogaster | n-pentanoate + NADH + H+ | - |
? | |
1.2.1.24 | succinate semialdehyde + NAD(P)+ + H2O | cysteine 311 and glutamic acid 277 are likely candidates for the active site residues directly involved in catalysis | Drosophila melanogaster | succinate + NAD(P)H + H+ | - |
? |
EC Number | Subunits | Comment | Organism |
---|---|---|---|
1.2.1.24 | ? | x * 98200, SDS-PAGE | Drosophila melanogaster |
EC Number | Synonyms | Comment | Organism |
---|---|---|---|
1.2.1.24 | SSADH | - |
Drosophila melanogaster |
1.2.1.24 | succinic semialdehyde dehydrogenase | - |
Drosophila melanogaster |
EC Number | Temperature Optimum [°C] | Temperature Optimum Maximum [°C] | Comment | Organism |
---|---|---|---|---|
1.2.1.24 | 22 | - |
optimal expression of pMalc2x-DmSSADH in Escherichia coli TB1 | Drosophila melanogaster |
EC Number | pH Minimum | pH Maximum | Comment | Organism |
---|---|---|---|---|
1.2.1.24 | 6 | 8.5 | at pH 8.5 MalE-DmSSADH is 10fold more active than at pH 6.0 | Drosophila melanogaster |
EC Number | Cofactor | Comment | Organism | Structure |
---|---|---|---|---|
1.2.1.24 | NAD+ | - |
Drosophila melanogaster | |
1.2.1.24 | NADP+ | is also accepted as coenzyme substrate but leads to 7fold lower reaction rates compared to NAD+ at saturating succinate semialdehyde concentrations | Drosophila melanogaster |