Funding Agency

Agency
National Institute of Health (NIH)
Institute
National Institute of General Medical Sciences (NIGMS)
Type
Research Project (R01)
Project #
5R01GM043043-08
Application #
2181767
Study Section
Physical Biochemistry Study Section (PB)
Project Start
1989-06-01
Project End
1997-08-31
Budget Start
1996-06-01
Budget End
1997-08-31
Support Year
8
Fiscal Year
1996
Total Cost
Indirect Cost

  Institution

Name
University of Nebraska Lincoln
Department
Biochemistry
Type
Schools of Earth Sciences/Natur
DUNS #
555456995
City
Lincoln
State
NE
Country
United States
Zip Code
68588

  Publications

Swanson, T; Brooks, H B; Osterman, A L et al. (1998) Carbon-13 isotope effect studies of Trypanosoma brucei ornithine decarboxylase. Biochemistry 37:14943-7
Waldrop, G L; Turnbull, J L; Parmentier, L E et al. (1992) Steady-state kinetics and isotope effects on the mutant catalytic trimer of aspartate transcarbamoylase containing the replacement of histidine 134 by alanine. Biochemistry 31:6585-91
Parmentier, L E; O'Leary, M H; Schachman, H K et al. (1992) 13C isotope effects as a probe of the kinetic mechanism and allosteric properties of Escherichia coli aspartate transcarbamylase. Biochemistry 31:6570-6
Waldrop, G L; Turnbull, J L; Parmentier, L E et al. (1992) The contribution of threonine 55 to catalysis in aspartate transcarbamoylase. Biochemistry 31:6592-7
Parmentier, L E; O'Leary, M H; Schachman, H K et al. (1992) 13C isotope effect studies of Escherichia coli aspartate transcarbamylase in the presence of the bisubstrate analog N-(phosphonoacetyl)-L-aspartate. Biochemistry 31:6598-602
Parmentier, L E; Weiss, P M; O'Leary, M H et al. (1992) 13C and 15N isotope effects as a probe of the chemical mechanism of Escherichia coli aspartate transcarbamylase. Biochemistry 31:6577-84
Smiley, J A; Paneth, P; O'Leary, M H et al. (1991) Investigation of the enzymatic mechanism of yeast orotidine-5'-monophosphate decarboxylase using 13C kinetic isotope effects. Biochemistry 30:6216-23