Agency
National Institute of Health (NIH)
Institute
National Institute of General Medical Sciences (NIGMS)
Type
Research Project (R01)
Project #
5R01GM032410-06
Application #
3281204
Study Section
Physiological Chemistry Study Section (PC)
Project Start
1983-07-01
Project End
1988-08-31
Budget Start
1988-07-01
Budget End
1988-08-31
Support Year
6
Fiscal Year
1988
Total Cost
Indirect Cost
Name
University of Mississippi Medical Center
Department
Type
Schools of Medicine
DUNS #
928824473
City
Jackson
State
MS
Country
United States
Zip Code
39216
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Allen, K N; Lavie, A; Glasfeld, A et al. (1994) Role of the divalent metal ion in sugar binding, ring opening, and isomerization by D-xylose isomerase: replacement of a catalytic metal by an amino acid. Biochemistry 33:1488-94
Lavie, A; Allen, K N; Petsko, G A et al. (1994) X-ray crystallographic structures of D-xylose isomerase-substrate complexes position the substrate and provide evidence for metal movement during catalysis. Biochemistry 33:5469-80
Allen, K N; Lavie, A; Farber, G K et al. (1994) Isotopic exchange plus substrate and inhibition kinetics of D-xylose isomerase do not support a proton-transfer mechanism. Biochemistry 33:1481-7
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Dignam, J D; Dignam, S S; Brumley, L L (1991) Alanyl-tRNA synthetase from Escherichia coli, Bombyx mori and Ratus ratus. Existence of common structural features. Eur J Biochem 198:201-10
Chang, P K; Dignam, J D (1990) Primary structure of alanyl-tRNA synthetase and the regulation of its mRNA levels in Bombyx mori. J Biol Chem 265:20898-906
Viswanathan, S; Dignam, J D (1988) Seryl-tRNA synthetase from Bombyx mori. Purification and properties. J Biol Chem 263:535-41
Viswanathan, S; Dignam, S S; Dignam, J D (1988) Control of the levels of alanyl-, glycyl-, and seryl-tRNA synthetases in the silkgland of Bombyx mori. Dev Biol 129:350-7