Agency
National Institute of Health (NIH)
Institute
National Institute of Diabetes and Digestive and Kidney Diseases (NIDDK)
Type
Modified Research Career Development Award (K04)
Project #
5K04DK001721-04
Application #
3072478
Study Section
Biochemistry Study Section (BIO)
Project Start
1987-03-01
Project End
1991-06-30
Budget Start
1990-07-01
Budget End
1991-06-30
Support Year
4
Fiscal Year
1990
Total Cost
Indirect Cost
Name
Boston University
Department
Type
Schools of Arts and Sciences
DUNS #
604483045
City
Boston
State
MA
Country
United States
Zip Code
02118
Goldsmith, J O; Kuo, L C (1993) Protonation of arginine 57 of Escherichia coli ornithine transcarbamoylase regulates substrate binding and turnover. J Biol Chem 268:18485-90
Goldsmith, J O; Kuo, L C (1993) Utilization of conformational flexibility in enzyme action-linkage between binding, isomerization, and catalysis. J Biol Chem 268:18481-4
Kuo, L C (1991) Generation of allosteric enzymes from nonallosteric forms. Methods Enzymol 202:706-27
Goldsmith, J O; Lee, S; Zambidis, I et al. (1991) Control of L-ornithine specificity in Escherichia coli ornithine transcarbamoylase. Site-directed mutagenic and pH studies. J Biol Chem 266:18626-34
Kuo, L C; Caron, C; Lee, S et al. (1990) Zn2+ regulation of ornithine transcarbamoylase. II. Metal binding site. J Mol Biol 211:271-80
Miller, A W; Kuo, L C (1990) Ligand-induced isomerizations of Escherichia coli ornithine transcarbamoylase. An ultraviolet difference analysis. J Biol Chem 265:15023-7
Lee, S; Shen, W H; Miller, A W et al. (1990) Zn2+ regulation of ornithine transcarbamoylase. I. Mechanism of action. J Mol Biol 211:255-69
Zambidis, I; Kuo, L C (1990) Substrate specificity and protonation state of Escherichia coli ornithine transcarbamoylase as determined by pH studies. Binding of carbamoyl phosphate. J Biol Chem 265:2620-3
Kuo, L C; Seaton, B A (1989) X-ray diffraction analysis on single crystals of recombinant Escherichia coli ornithine transcarbamoylase. J Biol Chem 264:16246-8
Kuo, L C; Zambidis, I; Caron, C (1989) Triggering of allostery in an enzyme by a point mutation: ornithine transcarbamoylase. Science 245:522-4

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