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Literature summary for 1.14.14.11 extracted from

  • Heine, T.; Tucker, K.; Okonkwo, N.; Assefa, B.; Conrad, C.; Scholtissek, A.; Schloemann, M.; Gassner, G.; Tischler, D.
    Engineering styrene monooxygenase for biocatalysis reductase-epoxidase fusion proteins (2017), Appl. Biochem. Biotechnol., 181, 1590-1610 .
    View publication on PubMed
Search for more literature for 1.14.14.11

Application

Application Comment Organism
synthesis construcution of fusion proteins that join the C-terminus of the epoxidase StyA to the N-terminus of FAD reductase StyB through a linker peptide and application in the synthesis of of a broad range of substituted indoles to indigoid chromophores. The fusion proteins are self-regulated and couple efficiently NADH oxidation to styrene epoxidation Rhodococcus opacus

Cloned(Commentary)

Cloned (Comment) Organism
-
 Rhodococcus opacus

Protein Variants

Protein Variants Comment Organism
additional information construcution of fusion proteins that join the C-terminus of the epoxidase StyA to the N-terminus of FAD reductase StyB through a linker peptide and application in the synthesis of of a broad range of substituted indoles to indigoid chromophores. The fusion proteins are self-regulated and couple efficiently NADH oxidation to styrene epoxidation Rhodococcus opacus

Organism

Organism UniProt Comment Textmining
Rhodococcus opacus A0A076JVU4 isoform StyA
-

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
1-methylindole + FADH2 + O2
-
 Rhodococcus opacus 1-methyl-1,2-dihydro-3H-indol-3-one + FAD + H2O
-
 ?
1-methylindole-5-carboxylate + FADH2 + O2
-
 Rhodococcus opacus 1-methyl-3-oxo-2,3-dihydro-1H-indole-5-carboxylic acid + FAD + H2O
-
 ?
4-methoxyindole + FADH2 + O2
-
 Rhodococcus opacus 4-methoxy-1,2-dihydro-3H-indol-3-one + FAD + H2O
-
 ?
5-methoxyindole + FADH2 + O2
-
 Rhodococcus opacus 5-methoxy-1,2-dihydro-3H-indol-3-one + FAD + H2O
-
 ?
6-bromoindole + FADH2 + O2
-
 Rhodococcus opacus 6-bromo-1,2-dihydro-3H-indol-3-one + FAD + H2O
-
 ?
6-chloroindole + FADH2 + O2
-
 Rhodococcus opacus 6-chloro-1,2-dihydro-3H-indol-3-one + FAD + H2O
-
 ?
6-methoxyindole + FADH2 + O2
-
 Rhodococcus opacus 6-methoxy-1,2-dihydro-3H-indol-3-one + FAD + H2O
-
 ?
7-azaindole + FADH2 + O2
-
 Rhodococcus opacus 1,2-dihydro-3H-pyrrolo[2,3-b]pyridin-3-one + FAD + H2O
-
 ?
7-methoxyindole + FADH2 + O2
-
 Rhodococcus opacus 7-methoxy-1,2-dihydro-3H-indol-3-one + FAD + H2O
-
 ?
indole + FADH2 + O2
-
 Rhodococcus opacus 1,2-dihydro-3H-indol-3-one + FAD + H2O
-
 ?

Cofactor

Cofactor Comment Organism Structure
FAD
-
 Rhodococcus opacus

General Information

General Information Comment Organism
physiological function the FAD-to-FAD hydride transfer of the reductase StyB has a rate constant of about 8 per s. This step is rate limiting in the styrene epoxidation reaction and helps to ensure that flavin reduction and styrene epoxidation reactions proceed without wasteful side reactions Rhodococcus opacus