Characterization of spinach ferredoxin-thioredoxin reductase.
Ferredoxin-thioredoxin reductase (FTR) is an iron-sulfur protein which, in the presence of ferredoxin and thioredoxin, catalyses the activation of photosynthetic enzymes such as fructose-1,6-bisphosphatase, NADP-malate dehydrogenase and several others. The results from amino acid composition and N- and C-terminal sequences show that spinach FTR is composed of two nonidentical subunits (mol.wt. = 17,200: A; 15,500:B) present in equal amounts. Other components (mol. wt. = 16,300 and 14,200) observed in preparations are most likely derived from subunit A losing its amino terminal part. We report the amino acid compositions of the two subunits A and B of FTR including their partial terminal sequences. Subunit A has an additional amino-terminal serine-rich sequence which is phosphorylated.
Research Institute for Biosciences, Science University of Tokyo, Chiba, Japan.
A
A
Tsugita
K
K
Yano
L
L
Gardet-Salvi
P
P
Schürmann
D000595:Amino Acid Sequence; D007506:Iron-Sulfur Proteins; D008969:Molecular Sequence Data; D010088:Oxidoreductases / Q000737:chemistry* / Q000302:isolation & purification; D010446:Peptide Fragments / Q000737:chemistry; D010766:Phosphorylation; D010940:Plant Proteins / Q000737:chemistry* / Q000302:isolation & purification; D011487:Protein Conformation
D007506:Iron-Sulfur Proteins; D010446:Peptide Fragments; D010940:Plant Proteins; D010088:Oxidoreductases; C021588:ferredoxin-thioredoxin reductase