EC Number   |
Application |
Reference |
|---|
    1.14.15.1 | analysis |
the enzyme is useful in whole cell biocatalyst systems |
672742 |
| 1.14.15.1 | biotechnology |
bioengineered Escherichia coli cells possess a heterologous self-sufficient P450 catalytic system that may have advantages in terms of low cost and high yield for the production of fine chemicals |
702820 |
| 1.14.15.1 | more |
knowledge of the conformational landscape is central to understanding P450 activity, which has important practical ramifications for the design of therapeutics with optimized pharmacokinetics, and the manipulation of P450s, and possibly other enzymes, for biotechnological applications |
745613 |
| 1.14.15.1 | more |
P450cam is not an antifungal target, but is an excellent model in which to study the phenomenon of drug resistance |
676941 |
| 1.14.15.1 | synthesis |
camphor hydroxylation in reverse micelles depends on coexistence of enzyme with putidaredoxin, putidaredoxin reductase, and NADH, but not on H2O2 |
659825 |
| 1.14.15.1 | synthesis |
fusion of putidaredoxin reductase PdR to the carboxy-terminus of camphor monooxygenase CYP101A1 (P450cam) via a linker peptide and reconstitution of camphor hydroxylase activity with free putidaredoxin enables the production of the almost fully heme-incorporated CYP-FdR fusion that is catalytically active in vivo and in vitro |
744637 |
| 1.14.15.1 | synthesis |
selective enzymatic oxidation of (+)-alpha-pinene to verbenol, verbenone, or myrtenol by enzyme mutants |
658971 |
| 1.14.15.1 | synthesis |
the enzyme is useful in whole cell biocatalyst systems |
672742 |
