alexa Glucose-induced phosphorylation of the MDH2 isozyme of malate dehydrogenase in Saccharomyces cerevisiae.
Pharmaceutical Sciences

Pharmaceutical Sciences

Journal of Clinical & Experimental Pharmacology

Author(s): Minard KI, McAlisterHenn L

Abstract Share this page

Abstract The cytosolic isozyme of malate dehydrogenase, MDH2, was previously shown to be subject to rapid inactivation and proteolysis following the addition of glucose to yeast cultures growing on nonfermentable carbon sources. In this report, we show that MDH2 is phosphorylated during the process of glucose-induced degradation. A truncated active form of MDH2 lacking the first 12 residues of the amino terminus was previously found to be resistant to glucose-induced degradation and, as shown in this study, is not subject to phosphorylation. Site-directed mutagenesis was conducted to change Ser-12 in the authentic enzyme to Ala-12 and to Asp-12. The S12A substitution has little effect on glucose-induced phosphorylation and degradation, whereas the enzyme with the S12D substitution is subject to phosphorylation and inactivation but not to rapid degradation. This provides clear evidence that inactivation is not simply a result of degradation. Additional mutagenesis was conducted to change His-214, a critical active site residue, to Leu-214. Analysis of expression of full-length and truncated forms of the H214L enzyme demonstrated that catalytic inactivity is not a prerequisite for degradation and confirmed an essential role for the amino terminus of the authentic enzyme in this phenomenon.
This article was published in Arch Biochem Biophys and referenced in Journal of Clinical & Experimental Pharmacology

Relevant Expert PPTs

Recommended Conferences

Relevant Topics

Peer Reviewed Journals
 
Make the best use of Scientific Research and information from our 700 + peer reviewed, Open Access Journals
International Conferences 2017-18
 
Meet Inspiring Speakers and Experts at our 3000+ Global Annual Meetings

Contact Us

Agri, Food, Aqua and Veterinary Science Journals

Dr. Krish

[email protected]

1-702-714-7001 Extn: 9040

Clinical and Biochemistry Journals

Datta A

[email protected]

1-702-714-7001Extn: 9037

Business & Management Journals

Ronald

[email protected]

1-702-714-7001Extn: 9042

Chemical Engineering and Chemistry Journals

Gabriel Shaw

[email protected]

1-702-714-7001 Extn: 9040

Earth & Environmental Sciences

Katie Wilson

[email protected]

1-702-714-7001Extn: 9042

Engineering Journals

James Franklin

[email protected]

1-702-714-7001Extn: 9042

General Science and Health care Journals

Andrea Jason

[email protected]

1-702-714-7001Extn: 9043

Genetics and Molecular Biology Journals

Anna Melissa

[email protected]

1-702-714-7001 Extn: 9006

Immunology & Microbiology Journals

David Gorantl

[email protected]

1-702-714-7001Extn: 9014

Informatics Journals

Stephanie Skinner

[email protected]

1-702-714-7001Extn: 9039

Material Sciences Journals

Rachle Green

[email protected]

1-702-714-7001Extn: 9039

Mathematics and Physics Journals

Jim Willison

[email protected]

1-702-714-7001 Extn: 9042

Medical Journals

Nimmi Anna

[email protected]

1-702-714-7001 Extn: 9038

Neuroscience & Psychology Journals

Nathan T

[email protected]

1-702-714-7001Extn: 9041

Pharmaceutical Sciences Journals

John Behannon

[email protected]

1-702-714-7001Extn: 9007

Social & Political Science Journals

Steve Harry

[email protected]

1-702-714-7001 Extn: 9042

 
© 2008-2017 OMICS International - Open Access Publisher. Best viewed in Mozilla Firefox | Google Chrome | Above IE 7.0 version
adwords