| Autor: |
A, Rahier, P, Benveniste, T, Husselstein, M, Taton |
| Rok vydání: |
2001 |
| Předmět: |
|
| Zdroj: |
Biochemical Society transactions. 28(6) |
| ISSN: |
0300-5127 |
| Popis: |
This report describes recent work on the process of desaturation at C5(6) of sterol precursors in plants. Biochemical characterization of the plant Delta(7)-sterol C5(6)-desaturase (5-DES) indicates that the enzyme system involved shows important similarities to the soluble and membrane-bound non-haem iron desaturases found in eukaryotes, including cyanide and hydrophobic chelators sensitivity, CO resistance and a requirement for exogenous reductant and molecular oxygen. Site-directed mutational analysis of highly conserved residues in 5-DES indicated that eight histidine residues from three histidine-rich motifs were essential for the catalysis, possibly by providing the ligands for a putative Fe centre. This mutational analysis also revealed the catalytic role of the functionally conserved Thr-114. |
| Databáze: |
OpenAIRE |
| Externí odkaz: |
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