Any feedback?
Literature summary for 1.1.1.1 extracted from
- Insertion of a calcium-responsive beta-roll domain into a thermostable alcohol dehydrogenase enables tunable control over cofactor selectivity (2018), ACS Catal., 8, 1602-1613 .
No PubMed abstract available
Protein Variants
| Protein Variants | Comment | Organism |
|---|---|---|
| additional information | insertion of an RTX domain from the adenylate cyclase of Bordetella pertussis into a loop near the catalytic active site of the thermostable alcohol dehydrogenase D from Pyrococcus furiosus. The resultant chimera, beta-AdhD, gains the calcium-binding ability of the beta-roll, retains the thermostable activity of AdhD, and exhibits reduced overall alcohol dehydrogenase activity. The addition of calcium to beta-AdhD preferentially inhibits NAD+-dependent activity in comparison to NADP+-dependent activity. Calcium is a competitive inhibitor of AdhD, and the addition of the RTX domain introduces calcium-dependent noncompetitive inhibition to beta-AdhD affecting NAD+-dependent activity. Thus, the insertion of an intrinsically disordered calcium-binding domain into a key loop in a cofactor-dependent enzyme results in an enzyme with tunable cofactor selectivity, reminiscent of a calcium-controlled cofactor selectivity rheostat switch | Pyrococcus furiosus |
KM Value [mM]
| KM Value [mM] | KM Value Maximum [mM] | Substrate | Comment | Organism | Structure |
|---|---|---|---|---|---|
| additional information | - |
additional information | kinetic data füor wild-type enzyme and chimeric enzyme created by insertion of an RTX domain from the adenylate cyclase of Bordetella pertussis into a loop near the catalytic active site of the thermostable alcohol dehydrogenase D (AdhD) from Pyrococcus furiosus | Pyrococcus furiosus |
Metals/Ions
| Metals/Ions | Comment | Organism | Structure |
|---|---|---|---|
| Ca2+ | insertion of an RTX domain from the adenylate cyclase of Bordetella pertussis into a loop near the catalytic active site of the thermostable alcohol dehydrogenase D from Pyrococcus furiosus. The resultant chimera, beta-AdhD, gains the calcium-binding ability of the beta-roll, retains the thermostable activity of AdhD, and exhibits reduced overall alcohol dehydrogenase activity. The addition of calcium to beta-AdhD preferentially inhibits NAD+-dependent activity in comparison to NADP+-dependent activity. Calcium is a competitive inhibitor of AdhD, and the addition of the RTX domain introduces calcium-dependent noncompetitive inhibition to beta-AdhD affecting NAD+-dependent activity | Pyrococcus furiosus |  |
Molecular Weight [Da]
| Molecular Weight [Da] | Molecular Weight Maximum [Da] | Comment | Organism |
|---|---|---|---|
| 42000 | - |
fusion protein, bet-AshD | Pyrococcus furiosus |
Organism
| Organism | UniProt | Comment | Textmining |
|---|---|---|---|
| Pyrococcus furiosus | - |
- |
- |
Purification (Commentary)
| Purification (Comment) | Organism |
|---|---|
- |
Pyrococcus furiosus |
Substrates and Products (Substrate)
| Substrates | Comment Substrates | Organism | Products | Comment (Products) | Rev. | Reac. |
|---|---|---|---|---|---|---|
| 2,3-butanediol + NAD+ | the enzyme is most active with 2,3-butanediol, preference for NADH in the reductive direction. Insertion of an RTX domain from the adenylate cyclase of Bordetella pertussis into a loop near the catalytic active site of the thermostable alcohol dehydrogenase D from Pyrococcus furiosus. The resultant chimera, beta-AdhD, gains the calcium-binding ability of the beta-roll, retains the thermostable activity of AdhD, and exhibits reduced overall alcohol dehydrogenase activity. The addition of calcium to beta-AdhD preferentially inhibits NAD+-dependent activity in comparison to NADP+-dependent activity. Calcium is a competitive inhibitor of AdhD, and the addition of the RTX domain introduces calcium-dependent noncompetitive inhibition to beta-AdhD affecting NAD+-dependent activity | Pyrococcus furiosus | acetoin + NADH + H+ | - |
? | |
| 2,3-butanediol + NADP+ | the enzyme is most active with 2,3-butanediol, preference for NADH in the reductive direction. Isertion of an RTX domain from the adenylate cyclase of Bordetella pertussis into a loop near the catalytic active site of the thermostable alcohol dehydrogenase D from Pyrococcus furiosus. The resultant chimera, beta-AdhD, gains the calcium-binding ability of the beta-roll, retains the thermostable activity of AdhD, and exhibits reduced overall alcohol dehydrogenase activity. The addition of calcium to beta-AdhD preferentially inhibits NAD+-dependent activity in comparison to NADP+-dependent activity. Calcium is a competitive inhibitor of AdhD, and the addition of the RTX domain introduces calcium-dependent noncompetitive inhibition to beta-AdhD affecting NAD+-dependent activity | Pyrococcus furiosus | acetoin + NADPH + H+ | - |
? | |
Subunits
| Subunits | Comment | Organism |
|---|---|---|
| monomer | 1 * 34000 | Pyrococcus furiosus |
Synonyms
| Synonyms | Comment | Organism |
|---|---|---|
| AdhD | - |
Pyrococcus furiosus |
| alcohol dehydrogenase D | - |
Pyrococcus furiosus |
Temperature Optimum [°C]
| Temperature Optimum [°C] | Temperature Optimum Maximum [°C] | Comment | Organism |
|---|---|---|---|
| 45 | - |
assay at | Pyrococcus furiosus |
Turnover Number [1/s]
| Turnover Number Minimum [1/s] | Turnover Number Maximum [1/s] | Substrate | Comment | Organism | Structure |
|---|---|---|---|---|---|
| additional information | - |
additional information | kinetic data füor wild-type enzyme and chimeric enzyme created by insertion of an RTX domain from the adenylate cyclase of Bordetella pertussis into a loop near the catalytic active site of the thermostable alcohol dehydrogenase D (AdhD) from Pyrococcus furiosus | Pyrococcus furiosus |
pH Optimum
| pH Optimum Minimum | pH Optimum Maximum | Comment | Organism |
|---|---|---|---|
| 9.3 | - |
assay at | Pyrococcus furiosus |
Cofactor
| Cofactor | Comment | Organism | Structure |
|---|---|---|---|
| NAD+ | insertion of an RTX domain from the adenylate cyclase of Bordetella pertussis into a loop near the catalytic active site of the thermostable alcohol dehydrogenase D from Pyrococcus furiosus. The resultant chimera, beta-AdhD, gains the calcium-binding ability of the beta-roll, retains the thermostable activity of AdhD, and exhibits reduced overall alcohol dehydrogenase activity. The addition of calcium to beta-AdhD preferentially inhibits NAD+-dependent activity in comparison to NADP+-dependent activity. Calcium is a competitive inhibitor of AdhD, and the addition of the RTX domain introduces calcium-dependent noncompetitive inhibition to beta-AdhD affecting NAD+-dependent activity | Pyrococcus furiosus | |
| NADP+ | insertion of an RTX domain from the adenylate cyclase of Bordetella pertussis into a loop near the catalytic active site of the thermostable alcohol dehydrogenase D from Pyrococcus furiosus. The resultant chimera, beta-AdhD, gains the calcium-binding ability of the beta-roll, retains the thermostable activity of AdhD, and exhibits reduced overall alcohol dehydrogenase activity. The addition of calcium to beta-AdhD preferentially inhibits NAD+-dependent activity in comparison to NADP+-dependent activity. Calcium is a competitive inhibitor of AdhD, and the addition of the RTX domain introduces calcium-dependent noncompetitive inhibition to beta-AdhD affecting NAD+-dependent activity | Pyrococcus furiosus | |
kcat/KM [mM/s]
| kcat/KM Value [1/mMs-1] | kcat/KM Value Maximum [1/mMs-1] | Substrate | Comment | Organism | Structure |
|---|---|---|---|---|---|
| additional information | - |
additional information | kinetic data for wild-type enzyme and chimeric enzyme created by insertion of an RTX domain from the adenylate cyclase of Bordetella pertussis into a loop near the catalytic active site of the thermostable alcohol dehydrogenase D (AdhD) from Pyrococcus furiosus | Pyrococcus furiosus |
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
