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Literature summary extracted from
- Characterization of different biocatalyst formats for BVMO-catalyzed cyclohexanone oxidation (2021), Biotechnol. Bioeng., 118, 2719-2733 .
Application
| EC Number | Application | Comment | Organism |
|---|---|---|---|
| 1.14.13.22 | synthesis | analysis of conversion kinetics for isolated enzyme, suspended whole cells, and biofilms, the latter two based on recombinant CHMO-containing P. taiwanensis VLB120. Biofilms show less favorable values for KS (9.3fold higher) and kcat (4.8fold lower) compared with corresponding KM and kcat values of isolated CHMO, but a favorable KI for cyclohexanone (5.3fold higher). Suspended cells show only 1.8fold higher KS, but 1.3- and 4.2fold higher kcat and KI values than isolated CHMO | Acidovorax sp. CHX100 |
KM Value [mM]
| EC Number | KM Value [mM] | KM Value Maximum [mM] | Substrate | Comment | Organism | Structure |
|---|---|---|---|---|---|---|
| 1.14.13.22 | 0.0022 | - |
O2 | purified enzyme, pH not specified in the publication, temperature not specified in the publication | Acidovorax sp. CHX100 |  |
| 1.14.13.22 | 0.054 | - |
O2 | suspended cells, pH not specified in the publication, temperature not specified in the publication | Acidovorax sp. CHX100 | |
| 1.14.13.22 | 0.178 | - |
cyclohexanone | purified enzyme, pH not specified in the publication, temperature not specified in the publication | Acidovorax sp. CHX100 | |
| 1.14.13.22 | 0.316 | - |
cyclohexanone | suspended cells, pH not specified in the publication, temperature not specified in the publication | Acidovorax sp. CHX100 | |
| 1.14.13.22 | 0.372 | - |
NADPH | purified enzyme, pH not specified in the publication, temperature not specified in the publication | Acidovorax sp. CHX100 | |
| 1.14.13.22 | 1.648 | - |
cyclohexanone | biofilm, pH not specified in the publication, temperature not specified in the publication | Acidovorax sp. CHX100 | |
Organism
| EC Number | Organism | UniProt | Comment | Textmining |
|---|---|---|---|---|
| 1.14.13.22 | Acidovorax sp. CHX100 | A0A2D0WG32 | - |
- |
Substrates and Products (Substrate)
| EC Number | Substrates | Comment Substrates | Organism | Products | Comment (Products) | Rev. | Reac. |
|---|---|---|---|---|---|---|---|
| 1.14.13.22 | 3,3,5-trimethylcyclohexanone + NADPH + O2 + H+ | 90% conversion efficincy, purified enzyme | Acidovorax sp. CHX100 | 4,6,6-trimethyloxepan-2-one + 4,4,6-trimethyloxepan-2-one + NADP+ + H2O | - |
? | |
| 1.14.13.22 | 4-ethylcyclohexanone + NADPH + O2 + H+ | 95% conversion efficincy, purified enzyme | Acidovorax sp. CHX100 | (5S)-5-ethyloxepan-2-one + NADP+ + H2O | - |
? | |
| 1.14.13.22 | 4-methylcyclohexanone + NADPH + O2 + H+ | 70% conversion efficincy, purified enzyme | Acidovorax sp. CHX100 | (5S)-5-methyloxepan-2-one + NADP+ + H2O | - |
? | |
| 1.14.13.22 | beta-tetralonne + NADPH + H+ + O2 | 25% conversion efficincy, purified enzyme | Acidovorax sp. CHX100 | ? + NADP+ + H2O | - |
? | |
| 1.14.13.22 | cyclohexanone + NADPH + H+ + O2 | 100% conversion efficincy, purified enzyme | Acidovorax sp. CHX100 | hexano-6-lactone + NADP+ + H2O | - |
? | |
| 1.14.13.22 | cyclopentanone + NADPH + H+ + O2 | 100% conversion efficincy, purified enzyme | Acidovorax sp. CHX100 | 1-oxa-2-oxo-cyclohexane + NADP+ + H2O | - |
? | |
| 1.14.13.22 | methyl phenyl sulfoxide + NADPH + H+ + O2 | 55% conversion efficincy, purified enzyme | Acidovorax sp. CHX100 | ? + NADP+ + H2O | - |
? | |
Turnover Number [1/s]
| EC Number | Turnover Number Minimum [1/s] | Turnover Number Maximum [1/s] | Substrate | Comment | Organism | Structure |
|---|---|---|---|---|---|---|
| 1.14.13.22 | 0.24 | - |
cyclohexanone | biofilm, pH not specified in the publication, temperature not specified in the publication | Acidovorax sp. CHX100 | |
| 1.14.13.22 | 1.11 | - |
O2 | purified enzyme, pH not specified in the publication, temperature not specified in the publication | Acidovorax sp. CHX100 | |
| 1.14.13.22 | 1.16 | - |
cyclohexanone | purified enzyme, pH not specified in the publication, temperature not specified in the publication | Acidovorax sp. CHX100 | |
| 1.14.13.22 | 1.17 | - |
NADPH | purified enzyme, pH not specified in the publication, temperature not specified in the publication | Acidovorax sp. CHX100 | |
| 1.14.13.22 | 1.31 | - |
O2 | suspended cells, pH not specified in the publication, temperature not specified in the publication | Acidovorax sp. CHX100 | |
| 1.14.13.22 | 1.5 | - |
cyclohexanone | suspended cells, pH not specified in the publication, temperature not specified in the publication | Acidovorax sp. CHX100 | |
kcat/KM [mM/s]
| EC Number | kcat/KM Value [1/mMs-1] | kcat/KM Value Maximum [1/mMs-1] | Substrate | Comment | Organism | Structure |
|---|---|---|---|---|---|---|
| 1.14.13.22 | 0.15 | - |
cyclohexanone | biofilm, pH not specified in the publication, temperature not specified in the publication | Acidovorax sp. CHX100 | |
| 1.14.13.22 | 0.28 | - |
O2 | suspended cells, pH not specified in the publication, temperature not specified in the publication | Acidovorax sp. CHX100 | |
| 1.14.13.22 | 3.16 | - |
NADPH | purified enzyme, pH not specified in the publication, temperature not specified in the publication | Acidovorax sp. CHX100 | |
| 1.14.13.22 | 4.75 | - |
cyclohexanone | suspended cells, pH not specified in the publication, temperature not specified in the publication | Acidovorax sp. CHX100 | |
| 1.14.13.22 | 5.79 | - |
O2 | purified enzyme, pH not specified in the publication, temperature not specified in the publication | Acidovorax sp. CHX100 | |
| 1.14.13.22 | 6.54 | - |
cyclohexanone | purified enzyme, pH not specified in the publication, temperature not specified in the publication | Acidovorax sp. CHX100 | |
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