
The amino acid sequence of ferredoxin-NADP+ oxidoreductase [EC 1.18.1.2, FNR] from Spirulina sp., a blue-green alga, was determined. Spirulina ferredoxin-NADP+ oxidoreductase was composed of 294 amino acid residues and the molecular weight of the holoenzyme was 34,135. An apparent homology of the amino(N)-terminal region was found between ferredoxin-NADP+ reductases from Spirulina and spinach. We also found some sequence similarities in human erythrocyte glutathione reductase and p-hydroxybenzoate hydroxylase from Pseudomonas fluorescens, both of which are NADPH-dependent FAD enzymes.
Metalloendopeptidases, Carboxypeptidases, Plants, Cyanobacteria, Peptide Fragments, Ferredoxin-NADP Reductase, Molecular Weight, Species Specificity, Endopeptidases, NADH, NADPH Oxidoreductases, Trypsin, Amino Acid Sequence, Cyanogen Bromide
Metalloendopeptidases, Carboxypeptidases, Plants, Cyanobacteria, Peptide Fragments, Ferredoxin-NADP Reductase, Molecular Weight, Species Specificity, Endopeptidases, NADH, NADPH Oxidoreductases, Trypsin, Amino Acid Sequence, Cyanogen Bromide
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