| OBSERVATION'S | This initial result already attracted the interest of ONE COMPANY which hopes to use the mutated enzyme to change solubility of SURFACTANTS |
| TECHNOLOGY |
In author's lab, the latest focus is on cytochro me P450, family of enzymes found in all living things. The enzymes perform some difficult OXIDATION chemistry, with regio- & stereoselectivity & substrate specificity. The enzymes traverse a complicated reaction pathway, requiring not only a COFACTOR but also at least one ELECTRON TRANSFER protein to perform; to harness it for industrial use would be expensive & complicated. Scientists have discovered that cytochrome P450s are also capable of bypassing all those steps by using a "SHUNT" pathway that requires NO cofactor & that uses HYDROGEN PEROXIDE as source of both electrons & O. Unfortunately this shunt pathway is extremely INEFFICIENT, & it requires H2O2 in Concn that inactivate the enzyme after short time So researchers are evolving cytochrome P450 to use this shunt pathway more efficiently. If such a feat were managed, they reasoned, it could set the stage for a wealth of interesting industrial & pharma chemistry. They selected a variety of cytochrome P450 known as BM-3 (for Bacillus megaterium, in which it is found), which catalyzes FATTY ACID HYDROXYLATION. A known MUTANT of the enzyme, F87A uses H2O2 more efficiently than the wild-type enzyme Researchers first created a library of randomly mutated, enzyme-coding DNA strands, then expressed them in bacteria. To search for promising mutants, they used a fatty acid surroga te substrate in which p-NITROPHENOLATE is incorporated at the acid's fatty end. If a mutant was effective, it released the p-NITROPHENOL, producing a signature YELLOW COLOR. After 5 rounds of evolution, researchers obtained a mutant that uses the shunt pathway 10 times more effectively than F87A & 100 times more effectively than the wild-type BM-3 |
| UPDATE | 12.01 |
| AUTHOR | This data is not available for free |
| LITERATURE REF. | This data is not available for free |
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