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Molecular characterization of glutathione reductase cDNAs from pea ( Pisum sativum L.)
Author(s) -
Creissen Gary,
Edwards E. Anne,
Enard Corine,
Wellburn Alan,
Mullineaux Phil
Publication year - 1992
Publication title -
the plant journal
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 3.058
H-Index - 269
eISSN - 1365-313X
pISSN - 0960-7412
DOI - 10.1046/j.1365-313x.1992.t01-52-00999.x
Subject(s) - pisum , escherichia coli , biology , sativum , peptide sequence , transit peptide , biochemistry , complementary dna , amino acid , glutathione reductase , homology (biology) , sequence alignment , enzyme , microbiology and biotechnology , glutathione , gene , chloroplast , botany , glutathione peroxidase , plastid
Summary 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 M‐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.