Mechanisms for Enzyme Catalysis of Heterolytic Reactions

Richard, John P.

Abstract

Funding Agency

• Agency: National Institute of Health (NIH)
• Institute: National Institute of General Medical Sciences (NIGMS)
• Type: Research Project (R01)
• Project #: 5R01GM047307-02
• Application #: 3306774
• Study Section: Physical Biochemistry Study Section (PB)
• Project Start: 1992-05-01
• Project End: 1993-07-31
• Budget Start: 1993-05-01
• Budget End: 1993-07-31
• Support Year: 2
• Fiscal Year: 1993

Institution

• Name: University of Kentucky
• Type: Schools of Arts and Sciences
• DUNS #: 832127323
• City: Lexington
• State: KY
• Country: United States
• Zip Code: 40506

Publications

Richard, J P (1998) The enhancement of enzymatic rate accelerations by Bronsted acid-base catalysis. Biochemistry 37:4305-9

Richard, J P; Huber, R E; Lin, S et al. (1996) Structure-reactivity relationships for beta-galactosidase (Escherichia coli, lac Z). 3. Evidence that Glu-461 participates in Bronsted acid-base catalysis of beta-D-galactopyranosyl group transfer. Biochemistry 35:12377-86

Richard, J P; Westerfeld, J G; Lin, S (1995) Structure-reactivity relationships for beta-galactosidase (Escherichia coli, lac Z). 1. Bronsted parameters for cleavage of alkyl beta-D-galactopyranosides. Biochemistry 34:11703-12

Richard, J P (1993) Mechanism for the formation of methylglyoxal from triosephosphates. Biochem Soc Trans 21:549-53