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Literature summary extracted from
- Anchoring effects in a wide binding pocket: The molecular basis of regioselectivity in engineered cytochrome P450 monooxygenase from B. megaterium (2008), Proteins, 73, 597-607.
Cloned(Commentary)
| EC Number | Cloned (Comment) | Organism |
|---|---|---|
| 1.14.14.1 | expression in Escherichia coli BL21 (DE3) using the pET281 expression system | Priestia megaterium |
Crystallization (Commentary)
| EC Number | Crystallization (Comment) | Organism |
|---|---|---|
| 1.14.14.1 | molecular dynamics simulations on two CYP102A1 mutants in complex with (-)-alpha-pinene to explore the molecular mechanism of substrate recognition and to predict regioselectivity. | Priestia megaterium |
Protein Variants
| EC Number | Protein Variants | Comment | Organism |
|---|---|---|---|
| 1.14.14.1 | A74G/F87G/L188Q | site-directed mutagenesis. The introduction of a smaller amino acid at position 87 results in a more active monooxygenase and a different product profile for the oxidation of substrate (-)-alpha-pinene. | Priestia megaterium |
| 1.14.14.1 | A74G/F87V/L188Q | site-directed mutagenesis. The introduction of a smaller amino acid at position 87 results in a more active monooxygenase and a different product profile for the oxidation of substrate (-)-alpha-pinene. | Priestia megaterium |
| 1.14.14.1 | A74G/L188Q | site-directed mutagenesis. MD simulations of the double mutant A74G L188Q (GQ) show that the substrate is blocked from accessing the heme oxygen by the side chain of the F87, when it adopts the conformation found in the X-ray structure. | Priestia megaterium |
Organism
| EC Number | Organism | UniProt | Comment | Textmining |
|---|---|---|---|---|
| 1.14.14.1 | Priestia megaterium | P14779 | expression in Escherichia coli BL21 (DE3) using the pET281 expression system | - |
Substrates and Products (Substrate)
| EC Number | Substrates | Comment Substrates | Organism | Products | Comment (Products) | Rev. | Reac. |
|---|---|---|---|---|---|---|---|
| 1.14.14.1 | (-)-alpha-pinene + [reduced NADPH-hemoprotein reductase] + O2 | mutant A74G/F87G/L188Q | Priestia megaterium | myrtenol + [oxidized NADPH-hemoprotein reductase] + H2O | mutant A74G/F87G/L188Q, 13% pinene oxide, 77% verbenol, 10% myrtenol | ? |  |
| 1.14.14.1 | (-)-alpha-pinene + [reduced NADPH-hemoprotein reductase] + O2 | mutant A74G/F87V/L188Q | Priestia megaterium | myrtenol + [oxidized NADPH-hemoprotein reductase] + H2O | mutant A74G/F87V/L188Q, 70% pinene oxide, 20% verbenol, 10% myrtenol | ? | |
| 1.14.14.1 | (-)-alpha-pinene + [reduced NADPH-hemoprotein reductase] + O2 | mutant A74G/F87G/L188Q | Priestia megaterium | pinene oxide + [oxidized NADPH-hemoprotein reductase] + H2O | mutant A74G/F87V/L188Q, 13% pinene oxide, 77% verbenol, 10% myrtenol | ? | |
| 1.14.14.1 | (-)-alpha-pinene + [reduced NADPH-hemoprotein reductase] + O2 | mutant A74G/F87V/L188Q | Priestia megaterium | pinene oxide + [oxidized NADPH-hemoprotein reductase] + H2O | mutant A74G/F87V/L188Q, 70% pinene oxide, 20% verbenol, 10% myrtenol | ? | |
| 1.14.14.1 | (-)-alpha-pinene + [reduced NADPH-hemoprotein reductase] + O2 | mutant A74G/L188Q | Priestia megaterium | pinene oxide + [oxidized NADPH-hemoprotein reductase] + H2O | mutant A74G/L188Q, 85% pinene oxide, 15% verbenol | ? | |
| 1.14.14.1 | (-)-alpha-pinene + [reduced NADPH-hemoprotein reductase] + O2 | mutant A74G/F87G/L188Q | Priestia megaterium | verbenol + [oxidized NADPH-hemoprotein reductase] + H2O | mutant A74G/F87G/L188Q, 13% pinene oxide, 77% verbenol, 10% myrtenol | ? | |
| 1.14.14.1 | (-)-alpha-pinene + [reduced NADPH-hemoprotein reductase] + O2 | mutant A74G/F87V/L188Q | Priestia megaterium | verbenol + [oxidized NADPH-hemoprotein reductase] + H2O | mutant A74G/F87V/L188Q, 70% pinene oxide, 20% verbenol, 10% myrtenol | ? | |
| 1.14.14.1 | (-)-alpha-pinene + [reduced NADPH-hemoprotein reductase] + O2 | mutant A74G/L188Q | Priestia megaterium | verbenol + [oxidized NADPH-hemoprotein reductase] + H2O | mutant A74G/L188Q, 85% pinene oxide, 15% verbenol | ? | |
| 1.14.14.1 | (-)-beta-pinene + [reduced NADPH-hemoprotein reductase] + O2 | mutant A74G/F87G/L188Q | Priestia megaterium | myrtanal + [oxidized NADPH-hemoprotein reductase] + H2O | mutant A74G/F87G/L188Q, 40% pino-carveol, 60% myrtanal | ? | |
| 1.14.14.1 | (-)-beta-pinene + [reduced NADPH-hemoprotein reductase] + O2 | mutant A74G/F87V/L188Q | Priestia megaterium | myrtanal + [oxidized NADPH-hemoprotein reductase] + H2O | mutant A74G/F87V/L188Q, 68% pino-carveol, 32% myrtanal | ? | |
| 1.14.14.1 | (-)-beta-pinene + [reduced NADPH-hemoprotein reductase] + O2 | mutant A74G/F87G/L188Q | Priestia megaterium | pino-carveol + [oxidized NADPH-hemoprotein reductase] + H2O | mutant A74G/F87G/L188Q, 40% pino-carveol, 60% myrtanal | ? | |
| 1.14.14.1 | (-)-beta-pinene + [reduced NADPH-hemoprotein reductase] + O2 | mutant A74G/F87V/L188Q | Priestia megaterium | pino-carveol + [oxidized NADPH-hemoprotein reductase] + H2O | mutant A74G/F87V/L188Q, 68% pino-carveol, 32% myrtanal | ? | |
| 1.14.14.1 | additional information | wild type CYP102A1 has no oxidizing activity toward ()-alpha- and ()-beta-pinene | Priestia megaterium | ? | - |
? | |
Synonyms
| EC Number | Synonyms | Comment | Organism |
|---|---|---|---|
| 1.14.14.1 | CYP102A1 | - |
Priestia megaterium |
| 1.14.14.1 | P450 BM3 | - |
Priestia megaterium |
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