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This enzymology textbook for graduate and advanced undergraduate students covers the syllabi of most universities where this subject is regularly taught. It focuses on the synchrony between the two broad mechanistic facets of enzymology: the chemical and the kinetic, and also highlights the synergy between enzyme structure and mechanism. Designed for self-study, it explains how to plan enzyme experiments and subsequently analyze the data collected. The book is divided into five major sections: 1] Introduction to enzymes, 2] Practical aspects, 3] Kinetic Mechanisms, 4] Chemical Mechanisms, and 5] Enzymology Frontiers. Individual concepts are treated as stand-alone chapters; readers can explore any single concept with minimal cross-referencing to the rest of the book. Further, complex approaches requiring specialized techniques and involved experimentation (beyond the reach of an average laboratory) are covered in theory with suitable references to guide readers.
The book provides students, researchers and academics in the broad area of biology with a sound theoretical and practical knowledge of enzymes. It also caters to those who do not have a practicing enzymologist to teach them the subject.
Dr. N. S. Punekar is currently working as a Professor at prestigious Indian Institute of Technology (IIT) Bombay, Mumbai, India. He obtained his PhD from the coveted Indian Institute of Sciences, Bangalore, India in the year 1984 and subsequently worked as Post-doctoral fellow at University of Wisconsin, Madison, USA till 1988. He joined IIT Bombay as Assistant Professor in 1988 and subsequently got elevated to the rank of Professor in 2001.
Part I: Enzyme catalysis - a perspective.- Enzymes -Their place in Biology.- Enzymes - Historical aspects.- Exploiting enzymes - Technology.- On enzyme nomenclature and classification.- Hallmarks of an enzyme catalyst.- Origins of enzyme catalytic power.- Origins of enzyme catalytic power.- Which enzyme uses what trick? Some remarks.- Structure and catalysis: Conformational flexibility and protein motion.- Part II: Enzyme kinetic practice and measurements.- Chemical kinetics - Fundamentals.- Concepts of equilibrium and steady-state.- ES complex and pre-steady-state kinetics.- Principles of enzyme assays.- Good kinetic practices.- Quantification of catalysis and measures of enzyme purity.- Henri-Michaelis-Menten equation.- More complex rate expressions.- Enzyme kinetic data - Collection and analysis.- Part III: Elucidation of Kinetic mechanisms.- Approaches to kinetic mechanism - Overview.- Analysis of initial velocity patterns.- Enzyme inhibition analyses.- Irreversible inhibitions.- Reversible inhibitions.- Alternate substrate (product) interactions.- pH Studies with enzymes.- Isotopes in enzymology.- Isotope exchanges at equilibrium.- Isotope effects in enzymology.- From kinetic data to mechanism and back.- Part IV: Chemical mechanisms and catalysis.- Chemical reactivity and molecular interactions.- Acid-base chemistry and catalysis.- Nucleophilic catalysis and covalent reaction intermediates.- Phosphoryl group chemistry and importance of ATP.- Enzymatic oxidation-reduction reactions.- Carboxylations and decarboxylations.- Electrophilic catalysis and amino acid transformations.- Integrating kinetic and chemical mechanisms - A synthesis.- Part V: Frontiers in enzymology.- Regulation of enzyme activity.- In vitro versus in vivo - Concept and consequences.- Future of enzymology - An appraisal.- Closure - Whither Enzymology.
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