Eugene E. Dekker, Ph. D.
Affiliations: | Biological Chemistry | The University of Michigan Medical School |
Area:
mammalian and bacterial studies on the chemistry, metabolism, and enzymology of amino acids, the characterization of new enzymes, and establishing enzyme structure/function/regulation interrelationsWebsite:
http://um2017.org/faculty-history/faculty/eugene-e-dekkerGoogle:
"Eugene E. Dekker"Bio:
William C. Rose and Eugene E. Dekker, Urea as a source of nitrogen for the biosynthesis of amino acids, J. Biol. Chem. 1956 223: 107-121.
Cross-listing: Chemistry Tree
Parents
Sign in to add mentorWilliam C. Rose | grad student | 1954 | UIUC (Chemistry Tree) | |
(Urea as a source of nitrogen for the biosynthesis of amino acids) |
Children
Sign in to add traineeSharon A. Boylan | grad student | The University of Michigan Medical School (Chemistry Tree) | |
Yen-Wen Chen | grad student | The University of Michigan Medical School (Chemistry Tree) | |
Paul A. Craig | grad student | The University of Michigan Medical School (Chemistry Tree) | |
Bill R. Epperly | grad student | The University of Michigan Medical School (Chemistry Tree) | |
John P. Marcus | grad student | The University of Michigan Medical School (Chemistry Tree) | |
Chris J. Vlahos | grad student | The University of Michigan Medical School (Chemistry Tree) | |
Umadas Maitra | grad student | 1963 | University of Michigan (Chemistry Tree) |
Adam R. Johnson | grad student | 1991-1996 | University of Michigan (Chemistry Tree) |
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Publications
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Johnson AR, Chen YW, Dekker EE. (1998) Investigation of a catalytic zinc binding site in Escherichia coli L-threonine dehydrogenase by site-directed mutagenesis of cysteine-38. Archives of Biochemistry and Biophysics. 358: 211-21 |
Johnson AR, Dekker EE. (1998) Site-directed mutagenesis of histidine-90 in Escherichia coli L-threonine dehydrogenase alters its substrate specificity. Archives of Biochemistry and Biophysics. 351: 8-16 |
Clark-Baldwin K, Johnson AR, Chen YW, et al. (1998) Structural characterization of the zinc site in Escherichia coli L-threonine dehydrogenase using extended X-ray absorption fine structure spectroscopy Inorganica Chimica Acta. 275: 215-221 |
Johnson AR, Dekker EE. (1996) Woodward's reagent K inactivation of Escherichia coli L-threonine dehydrogenase: increased absorbance at 340-350 nm is due to modification of cysteine and histidine residues, not aspartate or glutamate carboxyl groups. Protein Science : a Publication of the Protein Society. 5: 382-90 |
Chen YW, Dekker EE, Somerville RL. (1995) Functional analysis of E. coli threonine dehydrogenase by means of mutant isolation and characterization. Biochimica Et Biophysica Acta. 1253: 208-14 |
Marcus JP, Dekker EE. (1995) Identification of a second active site residue in Escherichia coli L-threonine dehydrogenase: methylation of histidine-90 with methyl p-nitrobenzenesulfonate. Archives of Biochemistry and Biophysics. 316: 413-20 |
Marcus JP, Dekker EE. (1993) pH-dependent decarboxylation of 2-amino-3-ketobutyrate, the unstable intermediate in the threonine dehydrogenase-initiated pathway for threonine utilization. Biochemical and Biophysical Research Communications. 190: 1066-72 |
Marcus JP, Dekker EE. (1993) Threonine formation via the coupled activity of 2-amino-3-ketobutyrate coenzyme A lyase and threonine dehydrogenase. Journal of Bacteriology. 175: 6505-11 |
Marcus JP, Dekker EE. (1993) Identity and some properties of the L-threonine aldolase activity manifested by pure 2-amino-3-ketobutyrate ligase of Escherichia coli. Biochimica Et Biophysica Acta. 1164: 299-304 |
Dekker EE, Kitson RP. (1992) 2-Keto-4-hydroxyglutarate aldolase: purification and characterization of the homogeneous enzyme from bovine kidney. The Journal of Biological Chemistry. 267: 10507-14 |