Enzyme Active Sites and their Reaction Mechanisms
- 1st Edition - December 2, 2020
- Author: Harry Morrison
- Language: English
- Paperback ISBN:9 7 8 - 0 - 1 2 - 8 2 1 0 6 7 - 3
- eBook ISBN:9 7 8 - 0 - 1 2 - 8 2 3 1 9 4 - 4
Enzyme Active Sites and their Reaction Mechanisms provides a one-stop reference on how enzymes "work." Here, Dr. Harry Morrison, PhD and Professor Emeritus at Purdue Universit… Read more
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Request a sales quoteEnzyme Active Sites and their Reaction Mechanisms provides a one-stop reference on how enzymes "work." Here, Dr. Harry Morrison, PhD and Professor Emeritus at Purdue University, provides a detailed overview of the origin and function of forty enzymes, the chemical details of their active sites, their mechanisms of action, and associated cofactors. The enzymes featured highlight a step forward, along with possible areas of application, thus supporting new research in academic and industrial labs. Each chapter is written in a clear format, including a brief summary of enzyme function and structure, a detailed description of their mechanisms of action and associated co-factors.
- Offers a comprehensive, biochemical understanding of enzyme mechanisms and their reaction sites
- Supports new research in academic, medical and industrial labs, connecting discoveries powered by recent advances in technology and experimental approaches to areas of application
- Features short, carefully structured, actionable chapters on various enzyme classes, thus allowing for easy-use and searchability
Active researchers in biochemistry, medical chemistry, organic chemistry, molecular biology, cell biology, pharmacology; clinician scientists; researchers in industry and pharma
- Cover image
- Title page
- Table of Contents
- Copyright
- Dedication
- Preface
- Acknowledgments
- Chapter 1. Acetylcholinesterase
- Abstract
- 1.1 Acetylcholinesterase
- 1.2 Physiological function
- 1.3 Key structural features
- 1.4 Reaction sequence
- 1.5 Mechanism and the role of active site residues
- Leading references
- Chapter 2. Aconitase
- Abstract
- 2.1 Aconitase
- 2.2 Physiological function
- 2.3 Key structural features
- 2.4 Reaction sequence
- 2.5 Detailed mechanism and the role of the active site residues
- Leading references
- Chapter 3. Adenosine deaminase
- Abstract
- 3.1 Adenosine deaminase (adenosine aminohydrolase)
- 3.2 Physiological function
- 3.3 Key structural features
- 3.4 Reaction sequence
- 3.5 Detailed mechanism and the role of active site residues
- Leading references
- Chapter 4. Alcohol dehydrogenase (horse liver)
- Abstract
- 4.1 Horse liver alcohol dehydrogenase
- 4.2 Physiological function
- 4.3 Key structural features
- 4.4 Reaction sequence
- 4.5 Detailed mechanism and the role of the active site residues
- Leading references
- Chapter 5. Aldehyde dehydrogenase
- Abstract
- 5.1 Aldehyde dehydrogenase
- 5.2 Physiological function
- 5.3 Key structural features
- 5.4 Reaction sequence
- 5.5 Detailed mechanism and the role of active site residues
- Leading references
- Chapter 6. Arginase I
- Abstract
- 6.1 Arginase
- 6.2 Physiological function
- 6.3 Key structural features
- 6.4 Reaction sequence
- 6.5 Detailed mechanism and the role of the active site residues
- Leading references
- Chapter 7. Carbonic anhydrase II
- Abstract
- 7.1 Human carbonic anhydrase II
- 7.2 Physiological function
- 7.3 Key structural features
- 7.4 Reaction sequence
- 7.5 Detailed mechanism and the role of active site residues
- Leading references
- Chapter 8. Carboxypeptidase A
- Abstract
- 8.1 Carboxypeptidase A
- 8.2 Physiological function
- 8.3 Key structural features
- 8.4 Reaction sequence
- 8.5 Detailed mechanism and the role of the active site residues. The “promoted water” mechanism
- Leading references
- Chapter 9. Chymotrypsin
- Abstract
- 9.1 α-Chymotrypsin
- 9.2 Physiological function
- 9.3 Key structural features
- 9.4 Reaction sequence
- 9.5 Detailed mechanism and the role of the active site residues
- Leading references
- Chapter 10. Citrate synthase
- Abstract
- 10.1 Citrate synthase
- 10.2 Physiological function
- 10.3 Key structural features
- 10.4 Reaction sequence
- 10.5 Detailed mechanism and the role of active site residues
- Leading references
- Chapter 11. Cytochrome P450cam
- Abstract
- 11.1 Cytochrome P450cam
- 11.2 Physiological function
- 11.3 Key structural features
- 11.4 Reaction sequence
- 11.5 Detailed mechanism and the role of the active site residues
- Leading references
- Chapter 12. m5C Cytosine methyltransferase
- Abstract
- 12.1 m5C Cytosine methyltransferase
- 12.2 Physiological function
- 12.3 Key structural features
- 12.4 Reaction sequence
- 12.5 Detailed mechanism(s) and the role of the active site residues
- Leading references
- Chapter 13. Deoxyribodipyrimidine photolyase
- Abstract
- 13.1 Deoxyribodipyrimidine photolyase
- 13.2 Physiological function
- 13.3 Key structural features
- 13.4 Reaction sequence
- 13.5 Detailed mechanism and the role of active site residues
- Leading references
- Chapter 14. Dihydrolipoamide dehydrogenase
- Abstract
- 14.1 Dihydrolipoamide dehydrogenase
- 14.2 Physiological function
- 14.3 Key structural features
- 14.4 Reaction sequence
- 14.5 Detailed mechanism and the role of the active site residues
- Leading references
- Chapter 15. Dihydrolipoyl transacetylase
- Abstract
- 15.1 Dihydrolipoyl transacetylase
- 15.2 Physiological function
- 15.3 Key structural features
- 15.4 Reaction sequence
- 15.5 Detailed mechanism and the role of the active site residues
- Leading references
- Chapter 16. Farnesyl pyrophosphate synthase
- Abstract
- 16.1 Farnesyl pyrophosphate synthase
- 16.2 Physiological function
- 16.3 Key structural features
- 16.4 Reaction sequence
- 16.5 Detailed mechanism and the role of active site residues
- Leading references
- Chapter 17. Fructose-1,6-bisphosphate aldolase
- Abstract
- 17.1 Fructose-1,6-bisphosphate aldolase
- 17.2 Physiological function
- 17.3 Key structural features
- 17.4 Reaction sequence
- 17.5 Detailed mechanism and the role of the active site residues
- Leading references
- Chapter 18. Hepatitis C NS2/3 protease
- Abstract
- 18.1 Hepatitis C NS2/3 protease
- 18.2 Physiological function
- 18.3 Key structural features
- 18.4 Reaction sequence
- 18.5 Detailed mechanism and the role of the active site residues
- Leading references
- Chapter 19. HIV-1 protease
- Abstract
- 19.1 HIV-1 protease
- 19.2 Physiological function
- 19.3 Key structural features
- 19.4 Reaction sequence
- 19.5 Detailed mechanism and the role of the active site residues
- Leading references
- Chapter 20. Indoleamine 2,3-dioxygenase-1
- Abstract
- 20.1 Indoleamine 2,3-dioxygenase-1
- 20.2 Physiological function
- 20.3 Key structural features
- 20.4 Reaction sequence
- 20.5 Detailed mechanism and the role of active-site residues
- Leading references
- Chapter 21. Lysine 2,3-aminomutase
- Abstract
- 21.1 Lysine 2,3-aminomutase
- 21.2 Physiological function
- 21.3 Key structural features
- 21.4 Reaction sequence
- 21.5 Detailed mechanism and the role of active site residues
- Leading references
- Chapter 22. Lysozyme
- Abstract
- 22.1 Lysozyme
- 22.2 Physiological function
- 22.3 Key structural features
- 22.4 Reaction sequence
- 22.5 Detailed mechanism and the role of the active site residues
- Leading references
- Chapter 23. Methyl-coenzyme M reductase
- Abstract
- 23.1 Methyl-coenzyme M reductase
- 23.2 Physiological function
- 23.3 Key structural features
- 23.4 Reaction sequence
- 23.5 Detailed mechanism and role of active site residues
- Leading references
- Chapter 24. Methylmalonyl coenzyme A mutase
- Abstract
- 24.1 Methylmalonyl coenzyme A mutase
- 24.2 Physiological function
- 24.3 Key structural features
- 24.4 Reaction sequence
- 24.5 Detailed mechanism and the role of active site residues
- Leading references
- Chapter 25. Nonheme iron halogenase
- Abstract
- 25.1 Syringomycin halogenase
- 25.2 Physiological function
- 25.3 Key structural features
- 25.4 Reaction sequence
- 25.5 Detailed mechanism and the role of active site residues
- Leading references
- Chapter 26. Peptidyl arginine deiminase 4
- Abstract
- 26.1 Peptidyl arginine deiminase 4
- 26.2 Physiological function
- 26.3 Key structural features
- 26.4 Reaction sequence
- 26.5 Detailed mechanism and the role of the active-site residues
- Leading references
- Chapter 27. Peptidylglycine α-hydroxylating monooxygenase
- Abstract
- 27.1 Peptidylglycine α-hydroxylating monooxygenase
- 27.2 Physiological function
- 27.3 Key structural features
- 27.4 Reaction sequence
- 27.5 Detailed mechanism and the role of the active site residues
- Leading references
- Chapter 28. Phosphatidylinositol-specific phospholipase C
- Abstract
- 28.1 Phosphatidylinositol-specific phospholipase C
- 28.2 Physiological function
- 28.3 Key structural features
- 28.4 Reaction sequence
- 28.5 Detailed mechanism and the role of the active site residues
- Leading references
- Chapter 29. Protein kinase A
- Abstract
- 29.1 Protein kinase A
- 29.2 Physiological function
- 29.3 Key structural features
- 29.4 Reaction sequence
- 29.5 Detailed mechanism and the role of the active site residues
- Leading references
- Chapter 30. Pyruvate carboxylase
- Abstract
- 30.1 Pyruvate carboxylase
- 30.2 Physiological function
- 30.3 Key structural features
- 30.4 Reaction sequence
- 30.5 Detailed mechanism and the role of active site residues
- Leading references
- Chapter 31. Pyruvate dehydrogenase
- Abstract
- 31.1 Pyruvate dehydrogenase
- 31.2 Physiological function
- 31.3 Key structural features
- 31.4 Reaction sequence
- 31.5 Detailed mechanism and role of the active site residues
- Leading references
- Chapter 32. Ribonuclease A
- Abstract
- 32.1 Bovine pancreatic ribonuclease A
- 32.2 Physiological function
- 32.3 Key structural features
- 32.4 Reaction sequence
- 32.5 Detailed mechanism including the role of His12 and His119 at the active site
- Leading references
- Chapter 33. Ribonucleotide reductase
- Abstract
- 33.1 Ribonucleotide reductase
- 33.2 Physiological function
- 33.3 Key structural features
- 33.4 Reaction sequence
- 33.5 Detailed mechanisms and the role of the active site residues
- Leading references
- Chapter 34. Serine racemase
- Abstract
- 34.1 Serine racemase
- 34.2 Physiological function
- 34.3 Key structural features
- 34.4 Reaction sequence
- 34.5 Detailed mechanism and the role of active site residues
- Leading references
- Chapter 35. Soluble quinoprotein glucose dehydrogenase
- Abstract
- 35.1 Soluble quinoprotein glucose dehydrogenase
- 35.2 Physiological function
- 35.3 Key structural features
- 35.4 Reaction sequence
- 35.5 Detailed mechanism and the role of active-site residues
- Leading references
- Chapter 36. Tetrachloroethene reductive dehalogenase—PceA
- Abstract
- 36.1 PceA
- 36.2 Physiological function
- 36.3 Key structural features
- 36.4 Reaction sequence
- 36.5 Detailed mechanism and the role of active-site residues
- Leading references
- Chapter 37. Thymidylate synthase
- Abstract
- 37.1 Thymidylate synthase
- 37.2 Physiological function
- 37.3 Key structural features
- 37.4 Reaction sequence
- 37.5 Detailed mechanism(s) and the roles of active site residues
- Leading references
- Chapter 38. The 20S proteasome
- Abstract
- 38.1 The 20S proteasome
- 38.2 Physiological function
- 38.3 Key structural features
- 38.4 Reaction sequence
- 38.5 Detailed mechanism and the role of active-site residues
- Leading references
- Chapter 39. Uracil-DNA glycosylase
- Abstract
- 39.1 Uracil-DNA glycosylase
- 39.2 Physiological function
- 39.3 Key structural features
- 39.4 Reaction sequence
- 39.5 Detailed mechanism and role of active-site residues
- Leading references
- Chapter 40. Vanadium-dependent chloroperoxidase
- Abstract
- 40.1 Vanadium chloroperoxidase
- 40.2 Physiological function
- 40.3 Key structural features
- 40.4 Reaction sequence
- 40.5 Detailed mechanism and the role of active-site residues
- Leading references
- Index
- No. of pages: 280
- Language: English
- Edition: 1
- Published: December 2, 2020
- Imprint: Academic Press
- Paperback ISBN: 9780128210673
- eBook ISBN: 9780128231944
HM
Harry Morrison
Harry Morrison, PhD is Emeritus Professor at Purdue University, West Lafayette, IN, USA. He joined the Purdue School of Science in 1963, and has since supervised nearly fifty Ph.D. students, and also served as Dean of the College of Science from 1992-2002. Dr. Morrison was instrumental in increasing the numbers and impact of women faculty in the College of Science. After earning a B.A. from Brandeis University in 1957 and a Ph.D. from Harvard in 1961, Dr. Morrison was a Postdoctoral Researcher at the Swiss Federal Institute in Zurich, Switzerland for two years, and following this was a Research Associate at the University of Wisconsin from 1962-1963. Dr. Morrison has published over 170 papers in peer reviewed journals and has edited two books on bioorganic chemistry.
Affiliations and expertise
Emeritus Professor, Bio-organic Chemistry, Purdue University, West Lafayette, IN, USARead Enzyme Active Sites and their Reaction Mechanisms on ScienceDirect