Molecular and biochemical characterization of an Arabidopsis thaliana arogenate dehydrogenase with two highly similar and active protein domains

Molecular and biochemical characterization of an Arabidopsis thaliana arogenate dehydrogenase... The present study reports the first molecular characterization of a plant arogenate dehydrogenase, the enzyme that catalyses the transformation of arogenate into tyrosine. The structure of the Arabidopsis thaliana tyrA gene is very peculiar since it encodes two highly similar, and putatively active, protein domains. PCR analyses confirmed the existence of a transcript encoding the two protein domains. The complete coding sequence and sequences corresponding to the two separate domains were independently cloned into Escherichia coli mutant AT 2471 lacking prephenate dehydrogenase activity. Our results revealed that the three recombinant enzymes are active. They all exhibit a high specificity toward arogenate and NADP, and have very similar kinetic properties. http://www.deepdyve.com/assets/images/DeepDyve-Logo-lg.png Plant Molecular Biology Springer Journals

Molecular and biochemical characterization of an Arabidopsis thaliana arogenate dehydrogenase with two highly similar and active protein domains

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Publisher
Kluwer Academic Publishers
Copyright
Copyright © 2002 by Kluwer Academic Publishers
Subject
Life Sciences; Biochemistry, general; Plant Sciences; Plant Pathology
ISSN
0167-4412
eISSN
1573-5028
D.O.I.
10.1023/A:1014018926676
Publisher site
See Article on Publisher Site

Abstract

The present study reports the first molecular characterization of a plant arogenate dehydrogenase, the enzyme that catalyses the transformation of arogenate into tyrosine. The structure of the Arabidopsis thaliana tyrA gene is very peculiar since it encodes two highly similar, and putatively active, protein domains. PCR analyses confirmed the existence of a transcript encoding the two protein domains. The complete coding sequence and sequences corresponding to the two separate domains were independently cloned into Escherichia coli mutant AT 2471 lacking prephenate dehydrogenase activity. Our results revealed that the three recombinant enzymes are active. They all exhibit a high specificity toward arogenate and NADP, and have very similar kinetic properties.

Journal

Plant Molecular BiologySpringer Journals

Published: Oct 13, 2004

References

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