A novel-dehydroascorbate reductase from spinach chloroplasts homologous to plant trypsin inhibitor.
Dehydroascorbate reductase has been isolated from spinach chloroplasts and purified to apparent homogeneity. The N-terminal amino acid sequence of the enzyme is homologous to the Kunitz-type trypsin inhibitors from plant sources. It is shown that spinach DHA reductase and soybean trypsin inhibitor are both capable of reducing dehydroascorbate when in the reduced (thiol) form but acquire trypsin-inhibiting activity in the oxidized (disulfide) state. Reduced chloroplast thioredoxins also reduce dehydroascorbate.
Trümper
S
S
Fachbereich Biologie-Chemie, Universität Kassel, Germany.
Follmann
H
H
Häberlein
I
I
D000595:Amino Acid Sequence; D002736:Chloroplasts / Q000201:enzymology*; D003683:Dehydroascorbic Acid / Q000378:metabolism; D007700:Kinetics; D008969:Molecular Sequence Data; D008970:Molecular Weight; D010088:Oxidoreductases / Q000737:chemistry* / Q000235:genetics / Q000302:isolation & purification* / Q000378:metabolism; D016415:Sequence Alignment; D017421:Sequence Analysis; D017386:Sequence Homology, Amino Acid; D018724:Spinacia oleracea; D013879:Thioredoxins / Q000378:metabolism; D014361:Trypsin Inhibitors / Q000737:chemistry* / Q000235:genetics / Q000378:metabolism
D014361:Trypsin Inhibitors; D013879:Thioredoxins; D010088:Oxidoreductases; C020666:glutathione dehydrogenase (ascorbate); D003683:Dehydroascorbic Acid