Any feedback?
Literature summary for 1.14.12.11 extracted from
- The alpha subunit of toluene dioxygenase from Pseudomonas putida F1 can accept electrons from reduced FerredoxinTOL but is catalytically inactive in the absence of the beta subunit (1999), Appl. Environ. Microbiol., 65, 315-318.
Organism
| Organism | UniProt | Comment | Textmining |
|---|---|---|---|
| Pseudomonas putida | - |
F1 | - |
Purification (Commentary)
| Purification (Comment) | Organism |
|---|---|
| recombinant alpha-subunit of the oxygenase component | Pseudomonas putida |
Specific Activity [micromol/min/mg]
| Specific Activity Minimum [µmol/min/mg] | Specific Activity Maximum [µmol/min/mg] | Comment | Organism |
|---|---|---|---|
| 2.46 | - |
units per mg of alpha-subunit of oxygenase | Pseudomonas putida |
Substrates and Products (Substrate)
| Substrates | Comment Substrates | Organism | Products | Comment (Products) | Rev. | Reac. |
|---|---|---|---|---|---|---|
| additional information | the purified alpha-subunit of oxygenase component is reduced by NADH and catalytic amounts of reductaseTOL and ferredoxinTOL. Reduced alpha-subunit can not oxidize toluene and catalysis is strictly dependent on the presence of beta-subunit | Pseudomonas putida | ? | - |
? |  |
| toluene + NADH + O2 | - |
Pseudomonas putida | (1S,2R)-3-methylcyclohexa-3,5-diene-1,2-diol + NAD+ | - |
? | |
Cofactor
| Cofactor | Comment | Organism | Structure |
|---|---|---|---|
| NADH | - |
Pseudomonas putida | |
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
