Abstract

The specific aims and long-term objectives of this proposal are the following: 1) The steady State Kinetics and Regulation of Allosteric Enzymes. What is the Steady State Rate Law for a Bisubstrate Reaction Catalyzed by an Enzyme Conforming to the Monod-Wyman-Changeaux (MWC) Model? 2) Do Enzymes Activate C-H Bonds for Proton Abstraction Through Bond Distortion? Can the Nitro Group by Further Exploited as a Carboxyl Analogue in Order to Generate Suicide Substrates and Ground and Transition State Inhibitors? 4) Is it Possible, by Raising Antibodies to Transition State Analogues, to Create Enzymes Using Hybridoma Technology? 5) Are N-Chloro Amino Acids or Amines Intermediates in the Mechanism of Killing of Phagocytosed Bacteria by Polymorphonuclear Leukocytes?

  Funding Agency

Agency
National Institute of Health (NIH)
Institute
National Institute of General Medical Sciences (NIGMS)
Type
Research Project (R01)
Project #
5R01GM011040-21
Application #
3268222
Study Section
Physiological Chemistry Study Section (PC)
Project Start
1978-01-01
Project End
1988-03-31
Budget Start
1985-04-01
Budget End
1986-03-31
Support Year
21
Fiscal Year
1985
Total Cost
Indirect Cost

  Institution

Name
University of Pennsylvania
Department
Type
Schools of Medicine
DUNS #
042250712
City
Philadelphia
State
PA
Country
United States
Zip Code
19104

  Publications

Reddy, Vijay S; Nemerow, Glen R (2014) Structures and organization of adenovirus cement proteins provide insights into the role of capsid maturation in virus entry and infection. Proc Natl Acad Sci U S A 111:11715-20
Porter, D J; Bright, H J (1987) Ethanenitronate is a peroxide-dependent suicide substrate for catalase. J Biol Chem 262:9608-14
Alston, T A; Porter, D J; Bright, H J (1987) Inactivation of GABA aminotransferase by 3-nitro-1-propanamine. J Enzyme Inhib 1:215-22
Porter, D J; Bright, H J (1987) The cyanogenic substrate for horseradish peroxidase is a conjugated enamine. J Biol Chem 262:9154-9
Porter, D J; Bright, H J (1987) Propionate-3-nitronate oxidase from Penicillium atrovenetum is a flavoprotein which initiates the autoxidation of its substrate by O2. J Biol Chem 262:14428-34
Porter, D J; Alston, T A; Bright, H J (1987) CO2 adducts as reactive analogues of carboxylate substrates for aconitase and other enzymes of carbohydrate metabolism. J Biol Chem 262:6552-63
Alston, T A; Porter, D J; Bright, H J (1985) Generation of nitric oxide by enzymatic oxidation of N-hydroxy-N-nitrosamines. J Biol Chem 260:4069-74