PMID:9618257
| Citation |
Zeghouf, M, Defaye, G, Fontecave, M and Coves, J (1998) The flavoprotein component of the Escherichia coli sulfite reductase can act as a cytochrome P450c17 reductase. Biochem. Biophys. Res. Commun. 246:602-5 |
|---|---|
| Abstract |
The flavoprotein component (SiR-FP) of the E. coli sulfite reductase was found to support 17 alpha-hydroxylation of pregnenolone in the presence of cytochrome P450c17. Half maximum activity is obtained for a 1:1 ratio of SiR-FP, expressed as monomer concentration, to P450c17. When compared to bovine NADPH-cytochrome P450 reductase, SiR-FP is about 12-15 times less efficient. P450c17 was demonstrated to interact specifically with the FMN-binding domain of the protein and the N-terminal part of SiR-FP is suspected to play a role in electron transfer. A cluster of negatively charged residues was found in SiR-FP by amino acid sequence comparison with rat cytochrome P450 reductase. These results argue in favour of the flavodoxin origin of the FMN-binding domain of SiR-FP. |
| Links |
PubMed Online version:10.1006/bbrc.1998.8671 |
| Keywords |
Amino Acid Sequence; Animals; Binding Sites; Cattle; Escherichia coli/enzymology; Evolution, Molecular; Flavin Mononucleotide; Flavodoxin/genetics; Flavoproteins/genetics; Flavoproteins/metabolism; Molecular Sequence Data; Oxidoreductases Acting on Sulfur Group Donors/genetics; Oxidoreductases Acting on Sulfur Group Donors/metabolism; Peptide Fragments/metabolism; Pregnenolone/metabolism; Protein Binding; Steroid 17-alpha-Hydroxylase/genetics; Steroid 17-alpha-Hydroxylase/metabolism; Substrate Specificity; Sulfite Reductase (NADPH) |
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