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Department of Chemistry & Biochemistry
The University of Texas at Austin
1 University Station A5300
Austin, TX 78712-0165
Contact Information
Office: MBB: 2.106
Phone: 471-1181
Lab
Office:
Phone:
Fax: 471-5680
Lester J. Reed
preed@mail.utexas.edu
Professor Emeritus
Ashbel Smith Professor Emeritus
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Research GroupNo information for this group. |
EducationNo information for this group. |
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AwardsMerck Award, American Society for Biochemistry and Molecular Biology, 1994 Fellow, American Academy of Arts and Sciences, 1981 Member, National Academy of Sciences, USA, 1973 Eli Lilly & Co. Award in Biological Chemistry, ACS, 1958 |
Enzyme structure, function, and regulation
Research is directed toward elucidating the structure, function, and regulation of the alpha-keto acid dehydrogenase multienzyme complexes from eukaryotic and prokaryotic cells. My group has isolated pyruvate, alpha-ketoglutarate and branched chain alpha-keto acid dehydrogenase in a highly purified state. These enzyme complexes, which have molecular weights ranging from 2.5 to 9.5 million, have been separated into their component enzymes. The individual enzymes have been characterized, and the complexes have been reconstituted from the isolated enzymes. Structural studies, including electron microscopy, X-ray diffraction, and protein engineering are directed toward elucidating the manner in which the individual enzymes are held together and interact in these complexes. We have shown that the activity of the mammalian pyruvate dehydrogenase complex is regulated by a phosphorylation-dephosphorylation cycle, catalyzed by a specific protein kinase and a protein phosphatase. The kinase and the phosphatase have been isolated in a near homogeneous state from bovine kidney mitochondria. cDNAs, encoding the two subunits, catalytic and regulatory, comprising the phosphatase have been cloned, sequenced, and expressed. Structure-function relationships in the phosphatase are being investigated by protein engineering. Determination of the crystal structure of the catalytic subunit is in progress.
Representative Publications
"On the Unique Structural Organization of the Saccharomyces cerevisiae Pyruvate Dehydrogenase Complex" J. Biol. Chem. 272 (1997): 5757-64.
"Role of the regulatory subunit of bovine pyruvate dehydrogenase phosphatase" Proc. Natl. Acad. Sci., USA 93 (1996): 4953-6.
"Molecular Cloning and Expression of the Catalytic Subunit of Bovine Pyruvate Dehydrogenase Phosphatase and Sequence Similarity with Protein Phosphatase 2C" Biochemistry 32 (1993): 8987-93.
"Structure-Function Relationships in Dihydrolipoamide Acetyltransferases" J.Biol.Chem. 265 (1990): 8971-4.