Molecular characterization of glutathione reductase cDNAs from pea (Pisum sativum L.).
A cDNA for pea glutathione reductase has been cloned and sequenced. The derived amino acid sequence of 562 residues shows a high degree of homology to the previously published GR sequences from human erythrocytes and from two prokaryotes: Escherichia coli and Pseudomonas aeruginosa. The pea enzyme differs from other GRs in having an N-terminal leader sequence of about 60-70 residues which may be a chloroplast transit peptide and a 20 amino acid C-terminal extension of unknown function.
Creissen
G
G
John Innes Institute, AFRC Institute of Plant Science Research, John Innes Centre, Norwich, UK.
Edwards
E A
EA
Enard
C
C
Wellburn
A
A
Mullineaux
P
P
D000595:Amino Acid Sequence; D003001:Cloning, Molecular; D004247:DNA / Q000235:genetics*; D004926:Escherichia coli / Q000201:enzymology / Q000235:genetics; D007887:Fabaceae / Q000201:enzymology / Q000235:genetics; D005980:Glutathione Reductase / Q000235:genetics*; D006801:Humans; D008969:Molecular Sequence Data; D010944:Plants / Q000201:enzymology* / Q000235:genetics*; D010946:Plants, Medicinal; D011550:Pseudomonas aeruginosa / Q000201:enzymology / Q000235:genetics; D017386:Sequence Homology, Amino Acid; D013045:Species Specificity
D004247:DNA; D005980:Glutathione Reductase