An Arabidopsis cDNA encoding a bifunctional glutamine amidotransferase/cyclase suppresses the histidine auxotrophy of a Saccharomyces cerevisiae his7 mutant
Copyright policy )An Arabidopsis cDNA encoding a bifunctional glutamine amidotransferase/cyclase suppresses the histidine auxotrophy of a Saccharomyces cerevisiae his7 mutant
A cDNA encoding a glutamine amidotransferase and cyclase catalyzing the fifth and sixth steps of the histidine (His) biosynthetic pathway has been isolated from Arabidopsis thaliana. The N‐ and C‐terminal domains of the primary structure deduced from a full‐length Arabidopsis hisHF (At‐HF) cDNA showed significant homology to the glutamine amidotransferase and cyclase of microorganisms, respectively. Effective suppression of the His auxotrophy of a Saccharomyces cerevisiae his7 mutant with the At‐HF cDNA confirmed that the At‐HF protein has bifunctional glutamine amidotransferase (HisH) and cyclase (HisF) activities.
- Novartis (Switzerland) Switzerland
- Novartis (Japan) Japan
DNA, Complementary, Arabidopsis thaliana, Sequence Homology, Amino Acid, Molecular Sequence Data, Restriction Mapping, Arabidopsis, Saccharomyces cerevisiae, Histidine biosynthesis, Recombinant Proteins, Open Reading Frames, Aminohydrolases, Multienzyme Complexes, Transferases, Glutamine amidotransferase/cyclase, Mutation, Mutagenesis, Site-Directed, Histidine, Amino Acid Sequence, Cloning, Molecular, cDNA, Sequence Alignment
DNA, Complementary, Arabidopsis thaliana, Sequence Homology, Amino Acid, Molecular Sequence Data, Restriction Mapping, Arabidopsis, Saccharomyces cerevisiae, Histidine biosynthesis, Recombinant Proteins, Open Reading Frames, Aminohydrolases, Multienzyme Complexes, Transferases, Glutamine amidotransferase/cyclase, Mutation, Mutagenesis, Site-Directed, Histidine, Amino Acid Sequence, Cloning, Molecular, cDNA, Sequence Alignment
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