Abstract

Various physiological stimuli, e.g., hormones, neural excitation and pharmacological agents can influence glycogen metabolism in a variety of tissues by altering a cascade of enzymatic relations. Our objective is to show how enzyme catalyzed covalent modification reaction occur and are regulated to (1) better understand glycogen metabolism in normal, healthy tissues and in cases where metabolic disturbances occur due to deficiences of insulin or vitamin B6, and (2) provide a basis how post-translational modification of proteins can control other important cellular processes. Specifically four major research areas are proposed: I. Enzyme Catalyzed Covalent Modification of Glyoogen Phosphorylase - Relationships of Chemical and Physical Changes to Regulatory Phenomena. II. Phosphorylase Kinase - A Stucy of Structural, Chemical, Catalytic and Regulatory Features. III. Enzyme Catalyzed Covalent Modification Reactions of Phosphoprotein Phosphatases - Mechanism and Specificity of the Reactions.

  Funding Agency

Agency
National Institute of Health (NIH)
Institute
National Institute of General Medical Sciences (NIGMS)
Type
Research Project (R01)
Project #
5R01GM009587-27
Application #
3268035
Study Section
Biochemistry Study Section (BIO)
Project Start
1975-01-01
Project End
1989-12-31
Budget Start
1988-01-01
Budget End
1988-12-31
Support Year
27
Fiscal Year
1988
Total Cost
Indirect Cost

  Institution

Name
Iowa State University
Department
Type
Earth Sciences/Resources
DUNS #
City
Ames
State
IA
Country
United States
Zip Code
50011

  Publications

Yuan, C J; Huang, C Y; Graves, D J (1994) Oxidation and site-directed mutagenesis of the sulfhydryl groups of a truncated gamma catalytic subunit of phosphorylase kinase. Functional and structural effects. J Biol Chem 269:24367-73
Martin, B L; Graves, D J (1994) Isotope effects on the mechanism of calcineurin catalysis: kinetic solvent isotope and isotope exchange studies. Biochim Biophys Acta 1206:136-42
Graves, D J; Luo, S (1994) Use of photoacoustic Fourier-transform infrared spectroscopy to study phosphates in proteins. Biochem Biophys Res Commun 205:618-24
Huang, C Y; Yuan, C J; Luo, S et al. (1994) Mutational analyses of the metal ion and substrate binding sites of phosphorylase kinase gamma subunit. Biochemistry 33:5877-83
Luo, S; Huang, C Y; McClelland, J F et al. (1994) A study of protein secondary structure by Fourier transform infrared/photoacoustic spectroscopy and its application for recombinant proteins. Anal Biochem 216:67-76
Yuan, C J; Huang, C Y; Graves, D J (1993) Phosphorylase kinase, a metal ion-dependent dual specificity kinase. J Biol Chem 268:17683-6
Huang, C Y; Yuan, C J; Livanova, N B et al. (1993) Expression, purification, characterization, and deletion mutations of phosphorylase kinase gamma subunit: identification of an inhibitory domain in the gamma subunit. Mol Cell Biochem 127-128:7-18
Martin, B L; Graves, D J (1993) Hydrolysis of trifluoroethyl phosphate as evidence that the serine and tyrosine phosphatase activities of calcineurin share the same specificity determinant. Biochem Biophys Res Commun 194:150-6
Wang, H; Graves, D J (1991) Calcineurin-catalyzed reaction with phosphite and phosphate esters of tyrosine. Biochemistry 30:3019-24
Takrama, J F; Graves, D J (1991) Solution conformations of the N-terminal CNBr fragment of glycogen phosphorylase and its interaction with calmodulin. Biochim Biophys Acta 1077:371-8

Showing the most recent 10 out of 29 publications