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George L. Kenyon

Affiliations: 
1998-2010 University of Michigan, Ann Arbor, Ann Arbor, MI 
Area:
Pharmaceutical Chemistry
Website:
http://faculty-history.dc.umich.edu/faculty/george-l-kenyon
Google:
"George Kenyon"
Bio:

http://chemistry.library.nd.edu/resources/genealogy/chemistry/documents/KenyonGL.pdf

Mean distance: 7.25
 		SNBCP
Cross-listing: MichiganTree

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Parents

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Frank H. Westheimer grad student 1965 Harvard
 (Studies on the mechanism of the alkaline decomposition of beta-haloalkylphosphonic acids)

Children

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JoAnne Stubbe grad student 1971 UC Berkeley
Michael A. Marletta grad student 1978 UCSF
Patricia C. Babbitt grad student 1988 UCSF
Simon H. Friedman grad student 1989-1996 UCSF
Christian P. Whitman post-doc 1987 UCSF
Sean M. Kerwin post-doc 1989-1991 UCSF
Jawad Alzeer post-doc 1998-2000 University of Michigan
Michael J. McLeish research scientist 1996-1997 UCSF

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Publications

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Brandt GS, Kneen MM, Chakraborty S, et al. (2009) Snapshot of a reaction intermediate: analysis of benzoylformate decarboxylase in complex with a benzoylphosphonate inhibitor. Biochemistry. 48: 3247-57
Chakraborty S, Nemeria NS, Balakrishnan A, et al. (2009) Detection and time course of formation of major thiamin diphosphate-bound covalent intermediates derived from a chromophoric substrate analogue on benzoylformate decarboxylase. Biochemistry. 48: 981-94
Wang PF, Yep A, Kenyon GL, et al. (2009) Using directed evolution to probe the substrate specificity of mandelamide hydrolase. Protein Engineering, Design & Selection : Peds. 22: 103-10
Brandt GS, Nemeria N, Chakraborty S, et al. (2008) Probing the active center of benzaldehyde lyase with substitutions and the pseudosubstrate analogue benzoylphosphonic acid methyl ester. Biochemistry. 47: 7734-43
Yeung CK, Yep A, Kenyon GL, et al. (2008) Physical, kinetic and spectrophotometric studies of a NAD(P)-dependent benzaldehyde dehydrogenase from Pseudomonas putida ATCC 12633. Biochimica Et Biophysica Acta. 1784: 1248-55
Yep A, Kenyon GL, McLeish MJ. (2008) Saturation mutagenesis of putative catalytic residues of benzoylformate decarboxylase provides a challenge to the accepted mechanism. Proceedings of the National Academy of Sciences of the United States of America. 105: 5733-8
Chakraborty S, Nemeria N, Yep A, et al. (2008) Mechanism of benzaldehyde lyase studied via thiamin diphosphate-bound intermediates and kinetic isotope effects. Biochemistry. 47: 3800-9
Nemeria N, Korotchkina L, McLeish MJ, et al. (2007) Elucidation of the chemistry of enzyme-bound thiamin diphosphate prior to substrate binding: defining internal equilibria among tautomeric and ionization states. Biochemistry. 46: 10739-44
Bera AK, Polovnikova LS, Roestamadji J, et al. (2007) Mechanism-based inactivation of benzoylformate decarboxylase, a thiamin diphosphate-dependent enzyme. Journal of the American Chemical Society. 129: 4120-1
Yep A, Kenyon GL, McLeish MJ. (2006) Determinants of substrate specificity in KdcA, a thiamin diphosphate-dependent decarboxylase. Bioorganic Chemistry. 34: 325-36
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