Isolation of a gene encoding 3-isopropylmalate dehydrogenase from rice

Isolation of a gene encoding 3-isopropylmalate dehydrogenase from rice 3-Isopropylmalate dehydrogenase (IPMDH, EC 1.1.1.85) is a key enzyme in the biosynthesis of leucine and glucosinolates in plants. IPMDH is a bifunctional dimeric enzyme that catalyzes dehydrogenation and decarboxylation reactions in the presence of NAD+. The leuB gene encoding IPMDH has been identified in a variety of bacteria and some plants. In this study, we analyze the gene for IPMDH from Oryza sativa (OsIPMDH). The analysis of an EST sequence and rice genome revealed a full-length open reading frame encoding 389 amino acids that correspond to a protein of approximately 41.2 kD. The predicted amino acid sequence of OsIPMDH was highly homologous with the IPMDHs from plants and bacteria. The OsIPMDH expression analysis in a leuB mutant of Escherichia coli revealed that OsIPMDH was capable of functionally complementing the leuB mutant. These results indicate that OsIPMDH encodes for a protein of 3-isopropylmalate dehydrogenase in rice. http://www.deepdyve.com/assets/images/DeepDyve-Logo-lg.png Russian Journal of Plant Physiology Springer Journals

Isolation of a gene encoding 3-isopropylmalate dehydrogenase from rice

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Publisher
Springer Journals
Copyright
Copyright © 2011 by Pleiades Publishing, Ltd.
Subject
Life Sciences; Plant Sciences ; Plant Physiology
ISSN
1021-4437
eISSN
1608-3407
D.O.I.
10.1134/S1021443711010183
Publisher site
See Article on Publisher Site

Abstract

3-Isopropylmalate dehydrogenase (IPMDH, EC 1.1.1.85) is a key enzyme in the biosynthesis of leucine and glucosinolates in plants. IPMDH is a bifunctional dimeric enzyme that catalyzes dehydrogenation and decarboxylation reactions in the presence of NAD+. The leuB gene encoding IPMDH has been identified in a variety of bacteria and some plants. In this study, we analyze the gene for IPMDH from Oryza sativa (OsIPMDH). The analysis of an EST sequence and rice genome revealed a full-length open reading frame encoding 389 amino acids that correspond to a protein of approximately 41.2 kD. The predicted amino acid sequence of OsIPMDH was highly homologous with the IPMDHs from plants and bacteria. The OsIPMDH expression analysis in a leuB mutant of Escherichia coli revealed that OsIPMDH was capable of functionally complementing the leuB mutant. These results indicate that OsIPMDH encodes for a protein of 3-isopropylmalate dehydrogenase in rice.

Journal

Russian Journal of Plant PhysiologySpringer Journals

Published: Jan 8, 2011

References

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