[reaction: see text] Cycloartenol synthase cyclizes and rearranges oxidosqualene to the protosteryl cation and then specifically deprotonates from C-19. To identify mutants that deprotonate differently, randomly generated mutant cycloartenol synthases were selected in a yeast lanosterol synthase mutant. A novel His477Asn mutant was uncovered that produces 88% lanosterol and 12% parkeol. The His477Gln mutant produces 73% parkeol, 22% lanosterol, and 5% Delta(7)-lanosterol. These are the most accurate lanosterol synthase and parkeol synthase that have been generated by mutagenesis.
| Predicate | Object |
|---|---|
| rdf:type | |
| rdfs:comment |
[reaction: see text] Cycloartenol synthase cyclizes and rearranges oxidosqualene to the protosteryl cation and then specifically deprotonates from C-19. To identify mutants that deprotonate differently, randomly generated mutant cycloartenol synthases were selected in a yeast lanosterol synthase mutant. A novel His477Asn mutant was uncovered that produces 88% lanosterol and 12% parkeol. The His477Gln mutant produces 73% parkeol, 22% lanosterol, and 5% Delta(7)-lanosterol. These are the most accurate lanosterol synthase and parkeol synthase that have been generated by mutagenesis.
|
| skos:exactMatch | |
| uniprot:name |
Org. Lett.
|
| uniprot:author |
Lodeiro S.,
Matsuda S.P.T.,
Meyer M.M.,
Patel A.J.,
Segura M.J.R.
|
| uniprot:date |
2002
|
| uniprot:pages |
4459-4462
|
| uniprot:title |
Directed evolution experiments reveal mutations at cycloartenol synthase residue His477 that dramatically alter catalysis.
|
| uniprot:volume |
4
|
| dc-term:identifier |
doi:10.1021/ol0269897
|