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Molecular Characterization of Glutathione Reductase CDNAs from Pea (Pisum Sativum L.)

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Journal Plant J
Date 1992 Jan 1
PMID 1303792
Citations 25
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Abstract

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.

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