Agency
National Institute of Health (NIH)
Institute
National Institute of General Medical Sciences (NIGMS)
Type
Research Project (R01)
Project #
7R01GM037056-04
Application #
3291987
Study Section
Biochemistry Study Section (BIO)
Project Start
1989-08-15
Project End
1991-06-30
Budget Start
1989-08-15
Budget End
1991-06-30
Support Year
4
Fiscal Year
1988
Total Cost
Indirect Cost
Name
North Dakota State University
Department
Type
Earth Sciences/Resources
DUNS #
City
Fargo
State
ND
Country
United States
Zip Code
58108
Betts, G F; Srivastava, D K (1991) The rationalization of high enzyme concentration in metabolic pathways such as glycolysis. J Theor Biol 151:155-67
Bernhard, S A; Tompa, P (1990) The mechanism of succinate or fumarate transfer in the tricarboxylic acid cycle allows molecular rotation of the intermediate. Arch Biochem Biophys 276:191-8
Malhotra, O P; Bernhard, S A (1989) Noncovalent modulation by ATP of the acyl transfer from acyl-glyceraldehyde-3-phosphate dehydrogenase to phosphate. Biochemistry 28:124-8
Srivastava, D K; Smolen, P; Betts, G F et al. (1989) Direct transfer of NADH between alpha-glycerol phosphate dehydrogenase and lactate dehydrogenase: fact or misinterpretation? Proc Natl Acad Sci U S A 86:6464-8
Srivastava, D K; Bernhard, S A (1987) Biophysical chemistry of metabolic reaction sequences in concentrated enzyme solution and in the cell. Annu Rev Biophys Biophys Chem 16:175-204
Srivastava, D K; Bernhard, S A (1987) Mechanism of transfer of reduced nicotinamide adenine dinucleotide among dehydrogenases. Transfer rates and equilibria with enzyme-enzyme complexes. Biochemistry 26:1240-6
Bernhard, S A; Srivastava, D K (1987) Functional consequences of the direct transfer of metabolites in muscle glycolysis. Biochem Soc Trans 15:977-81
Bernhard, S A; Srivastava, D K (1987) Functional role of enzyme conformational changes in metabolism. Indian J Biochem Biophys 24:suppl 11-5
Srivastava, D K; Bernhard, S A (1986) Metabolite transfer via enzyme-enzyme complexes. Science 234:1081-6