| Literature DB >> 3448086 |
Y Sagara1, Y Takata, T Miyata, T Hara, T Horiuchi.
Abstract
cDNA clones for bovine adrenodoxin reductase were isolated, and the primary structure of the enzyme precursor was deduced from their nucleotide sequences. The precursor consists of 492 amino acids including an extrapeptide of 32 amino acids at the amino terminus. The extrapeptide is hydrophilic [corrected] and rich in arginine. The amino terminal sequence of the precursor is homologous with that of the adrenodoxin precursor. A possible FAD- or NADPH-binding site is present near the amino terminus of the mature enzyme.Entities:
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Year: 1987 PMID: 3448086 DOI: 10.1093/oxfordjournals.jbchem.a122178
Source DB: PubMed Journal: J Biochem ISSN: 0021-924X Impact factor: 3.387