Any feedback?
Literature summary for 1.2.1.16 extracted from
- Kinetic characterization and molecular modeling of NAD(P)+-dependent succinic semialdehyde dehydrogenase from Bacillus subtilis as an ortholog YneI (2014), J. Microbiol. Biotechnol., 24, 954-958 .
Cloned(Commentary)
| Cloned (Comment) | Organism |
|---|---|
| recombinant overexpression of His-tagged enzyme in Escherichia coli strain BL21(DE3)pLysS | Bacillus subtilis |
Inhibitors
| Inhibitors | Comment | Organism | Structure |
|---|---|---|---|
| succinate semialdehyde | enzyme BsSSADH shows the substrate inhibition phenomenon in the presence of both NAD+ and NADP+ as cofactors at the concentration of succinate semialdehyde higher than 0.05 and 0.02 mM, respectively | Bacillus subtilis |  |
KM Value [mM]
| KM Value [mM] | KM Value Maximum [mM] | Substrate | Comment | Organism | Structure |
|---|---|---|---|---|---|
| additional information | - |
additional information | Michaelis-Menten kinetics | Bacillus subtilis | |
| 0.21 | - |
NAD+ | pH and temperature not specified in the publication | Bacillus subtilis | |
| 0.39 | - |
NADP+ | pH and temperature not specified in the publication | Bacillus subtilis | |
| 10.36 | - |
succinate semialdehyde | pH and temperature not specified in the publication, in presence of NAD+ | Bacillus subtilis | |
| 20.5 | - |
succinate semialdehyde | pH and temperature not specified in the publication, in presence of NADP+ | Bacillus subtilis | |
Natural Substrates/ Products (Substrates)
| Natural Substrates | Organism | Comment (Nat. Sub.) | Natural Products | Comment (Nat. Pro.) | Rev. | Reac. |
|---|---|---|---|---|---|---|
| succinate semialdehyde + NAD+ + H2O | Bacillus subtilis | - |
succinate + NADH + 2 H+ | - |
? | |
| succinate semialdehyde + NAD+ + H2O | Bacillus subtilis 168 | - |
succinate + NADH + 2 H+ | - |
? | |
| succinate semialdehyde + NADP+ + H2O | Bacillus subtilis | - |
succinate + NADPH + 2 H+ | - |
? | |
| succinate semialdehyde + NADP+ + H2O | Bacillus subtilis 168 | - |
succinate + NADPH + 2 H+ | - |
? | |
Organism
| Organism | UniProt | Comment | Textmining |
|---|---|---|---|
| Bacillus subtilis | - |
- |
- |
| Bacillus subtilis 168 | - |
- |
- |
Purification (Commentary)
| Purification (Comment) | Organism |
|---|---|
| recombinant His-tagged enzyme from Escherichia coli strain BL21(DE3)pLysS by nickel affinity chromatography and gel filtration | Bacillus subtilis |
Substrates and Products (Substrate)
| Substrates | Comment Substrates | Organism | Products | Comment (Products) | Rev. | Reac. |
|---|---|---|---|---|---|---|
| succinate semialdehyde + NAD+ + H2O | - |
Bacillus subtilis | succinate + NADH + 2 H+ | - |
? | |
| succinate semialdehyde + NAD+ + H2O | - |
Bacillus subtilis 168 | succinate + NADH + 2 H+ | - |
? | |
| succinate semialdehyde + NADP+ + H2O | - |
Bacillus subtilis | succinate + NADPH + 2 H+ | - |
? | |
| succinate semialdehyde + NADP+ + H2O | - |
Bacillus subtilis 168 | succinate + NADPH + 2 H+ | - |
? | |
Subunits
| Subunits | Comment | Organism |
|---|---|---|
| More | structure modeling | Bacillus subtilis |
Synonyms
| Synonyms | Comment | Organism |
|---|---|---|
| BsSSADH | - |
Bacillus subtilis |
| NAD(P)+-dependent succinic semialdehyde dehydrogenase | - |
Bacillus subtilis |
| SSADH | - |
Bacillus subtilis |
Turnover Number [1/s]
| Turnover Number Minimum [1/s] | Turnover Number Maximum [1/s] | Substrate | Comment | Organism | Structure |
|---|---|---|---|---|---|
| 5.26 | - |
NAD+ | pH and temperature not specified in the publication | Bacillus subtilis | |
| 5.61 | - |
succinate semialdehyde | pH and temperature not specified in the publication, in presence of NAD+ | Bacillus subtilis | |
| 7.24 | - |
succinate semialdehyde | pH and temperature not specified in the publication, in presence of NADP+ | Bacillus subtilis | |
| 9.93 | - |
NADP+ | pH and temperature not specified in the publication | Bacillus subtilis | |
Cofactor
| Cofactor | Comment | Organism | Structure |
|---|---|---|---|
| additional information | NAD(P)+-dependent succinic semialdehyde dehydrogenase, BsSSADH shows similar values of the catalytic efficiency (kcat/Km) in both NAD+ and NADP+ as cofactors. The affinity of enzyme BsSSADH to NAD+ is approximately 2fold higher than that to NADP+, but the values of kcat are almost 2fold higher in the presence of NADP+ than NAD+ | Bacillus subtilis | |
| NAD+ | - |
Bacillus subtilis | |
| NADP+ | - |
Bacillus subtilis | |
Ki Value [mM]
| Ki Value [mM] | Ki Value maximum [mM] | Inhibitor | Comment | Organism | Structure |
|---|---|---|---|---|---|
| 28.3 | - |
succinate semialdehyde | pH and temperature not specified in the publication, in presence of NADP+ | Bacillus subtilis | |
| 470.6 | - |
succinate semialdehyde | pH and temperature not specified in the publication, in presence of NAD+ | Bacillus subtilis | |
General Information
| General Information | Comment | Organism |
|---|---|---|
| metabolism | succinic semialdehyde dehydrogenase (SSADH) catalyzes the oxidation of succinic semialdehyde (SSA) into succinic acid in the final step of gamma-aminobutyric acid degradation | Bacillus subtilis |
kcat/KM [mM/s]
| kcat/KM Value [1/mMs-1] | kcat/KM Value Maximum [1/mMs-1] | Substrate | Comment | Organism | Structure |
|---|---|---|---|---|---|
| 0.362 | - |
succinate semialdehyde | pH and temperature not specified in the publication, in presence of NADP+ | Bacillus subtilis | |
| 0.598 | - |
succinate semialdehyde | pH and temperature not specified in the publication, in presence of NAD+ | Bacillus subtilis | |
| 25.1 | - |
NAD+ | pH and temperature not specified in the publication | Bacillus subtilis | |
| 25.4 | - |
NADP+ | pH and temperature not specified in the publication | Bacillus subtilis | |
Use of this online version of BRENDA is free under the CC BY 4.0 license. See terms of use for full details.
Release 2023.1 (January 2023)
Legal
Curated at
Member of
