Abstract
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.
MeSH terms
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Amino Acid Sequence
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Aminohydrolases
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Arabidopsis / enzymology*
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Arabidopsis / genetics
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Cloning, Molecular
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DNA, Complementary
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Histidine / metabolism*
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Molecular Sequence Data
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Multienzyme Complexes / biosynthesis
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Multienzyme Complexes / chemistry
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Multienzyme Complexes / metabolism*
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Mutagenesis, Site-Directed
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Mutation
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Open Reading Frames
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Recombinant Proteins / biosynthesis
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Recombinant Proteins / chemistry
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Recombinant Proteins / metabolism
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Restriction Mapping
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Saccharomyces cerevisiae / enzymology
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Saccharomyces cerevisiae / genetics
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Saccharomyces cerevisiae / growth & development*
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Sequence Alignment
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Sequence Homology, Amino Acid
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Transferases / biosynthesis
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Transferases / chemistry
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Transferases / metabolism*
Substances
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DNA, Complementary
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Multienzyme Complexes
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Recombinant Proteins
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Histidine
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Transferases
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imidazole glycerol phosphate synthase
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Aminohydrolases
Associated data
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GENBANK/AB006210
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GENBANK/AB016783