Mechanism in Protein Chemistry

This book examines the chemical methods used to study the mechanisms of enzymatically catalyzed reactions with an emphasis on the crystallographic molecular models of active sites. The book traces the development of enzymatic mechanisms from physical organic studies of nonenzymatic catalysis through detailed examination of the specific interactions between catalytic amino acids and intermediate analogues in crystallographic molecular models. The strategies of enzymatic catalysis, such as coenzymatic assistance, approximation, strain, the use of general acid-bases, the involvement of intermediates, and conformational control, are the central topics around which the book is organized.

"The modern standard against which both graduate and reference texts will be judged". -- Paul A. Bartlett, University of California, Berkeley

"Indispensable for the serious student of enzyme catalysis and a splendid resource for investigators in the field". -- Paul D. Bayer, University of California, Los Angeles, Emeritus

Describes proteins' physical and chemical nature and how their molecular structures can be determined experimentally. Intended for upper level undergraduate and graduate students with a background in chemistry or biochemistry.

1. Reaction Mechanisms 2. Coenzymes 3. Binding of Substrates to the Active Site 4. Transfer of Protons 5. Intermediates in Enzymatic Reactions 6. Conformational Changes

Jack Kyte, Professor Emeritus in the Chemistry Department at the University of California in San Diego, is well known for his research on the analysis of protein structure. He graduated magna cum laude from Carleton College with a degree in Chemistry. Under the tutelage of Guido Guidotti, he received his graduate degree in the Department of Biochemistry and Molecular Biology at Harvard University in Cambridge Massachusetts. Prof. Kyte joined the Department of Chemistry at the University of California at San Diego in 1974. Prof. Kyte has had a major impact in the prediction and analysis of protein structure. He ran a laboratory investigating the structure and mechanism of sodium and potassium ATPase, an enzyme from plasma membranes responsible for active transport; acetylcholine receptor, a protein in the plasma membrane that transports cations; the receptor for epidermal growth factor, a protein in the plasma membrane that controls cellular growth; and ribonucleotide reductase, a cytoplasmic enzyme responsible for the conversion of ribonucleotides into deoxyribonucleotides. This research was funded by grants from the National Institutes of Health, the National Science Foundation, and the American Heart Association. Prof. Kyte received a Career Development Award from the National Institutes of Health, and served on the editorial board of Biochemistry for six years.