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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 interrelations
Website:
http://um2017.org/faculty-history/faculty/eugene-e-dekker
Google:
"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.

Mean distance: 8.82
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Parents

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William C. Rose grad student 1954 UIUC
 (Urea as a source of nitrogen for the biosynthesis of amino acids)

Children

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Sharon A. Boylan grad student The University of Michigan Medical School
Yen-Wen Chen grad student The University of Michigan Medical School
Paul A. Craig grad student The University of Michigan Medical School
Bill R. Epperly grad student The University of Michigan Medical School
John P. Marcus grad student The University of Michigan Medical School
Chris J. Vlahos grad student The University of Michigan Medical School
Umadas Maitra grad student 1963 University of Michigan
Adam R. Johnson grad student 1991-1996 University of Michigan

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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
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