Document Detail

Spirulina ferredoxin-NADP+ reductase. The complete amino acid sequence.
MedLine Citation:
PMID:  6430889     Owner:  NLM     Status:  MEDLINE    
The amino acid sequence of ferredoxin-NADP+ oxidoreductase [EC, 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.
Y Yao; T Tamura; K Wada; H Matsubara; K Kodo
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Publication Detail:
Type:  Journal Article; Research Support, Non-U.S. Gov't    
Journal Detail:
Title:  Journal of biochemistry     Volume:  95     ISSN:  0021-924X     ISO Abbreviation:  J. Biochem.     Publication Date:  1984 May 
Date Detail:
Created Date:  1984-08-27     Completed Date:  1984-08-27     Revised Date:  2007-12-19    
Medline Journal Info:
Nlm Unique ID:  0376600     Medline TA:  J Biochem     Country:  JAPAN    
Other Details:
Languages:  eng     Pagination:  1513-6     Citation Subset:  IM    
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MeSH Terms
Amino Acid Sequence
Cyanobacteria / enzymology*
Cyanogen Bromide
Ferredoxin-NADP Reductase* / isolation & purification
Molecular Weight
NADH, NADPH Oxidoreductases* / isolation & purification
Peptide Fragments / analysis
Plants / enzymology
Species Specificity
Reg. No./Substance:
0/Peptide Fragments; 506-68-3/Cyanogen Bromide; EC Reductase; EC 1.6.-/NADH, NADPH Oxidoreductases; EC 3.4.-/Carboxypeptidases; EC 3.4.-/Endopeptidases; EC; EC 3.4.24.-/Metalloendopeptidases; EC protein, Staphylococcus aureus

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