Enzyme Active Sites and their Reaction Mechanisms
معرفی کتاب «Enzyme Active Sites and their Reaction Mechanisms» نوشتهٔ Harry Morrison، منتشرشده توسط نشر Academic Press در سال 2021. این کتاب در فرمت pdf، زبان انگلیسی ارائه شده است.
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 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 Copyright Dedication Contents Preface Acknowledgments 1. Acetylcholinesterase 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 2. Aconitase 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 3. Adenosine deaminase 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 4. Alcohol dehydrogenase (horse liver) 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 5. Aldehyde dehydrogenase 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 6. Arginase I 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 7. Carbonic anhydrase II 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 8. Carboxypeptidase A 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 9. Chymotrypsin 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 10. Citrate synthase 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 11. Cytochrome P450cam 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 12. m5C Cytosine methyltransferase 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 13. Deoxyribodipyrimidine photolyase 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 14. Dihydrolipoamide dehydrogenase 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 15. Dihydrolipoyl transacetylase 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 16. Farnesyl pyrophosphate synthase 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 17. Fructose-1,6-bisphosphate aldolase 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 18. Hepatitis C NS2/3 protease 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 19. HIV-1 protease 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 20. Indoleamine 2,3-dioxygenase-1 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 21. Lysine 2,3-aminomutase 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 22. Lysozyme 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 23. Methyl-coenzyme M reductase 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 24. Methylmalonyl coenzyme A mutase 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 25. Nonheme iron halogenase 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 26. Peptidyl arginine deiminase 4 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 reading 27. Peptidylglycine α-hydroxylating monooxygenase 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 28. Phosphatidylinositol-specific phospholipase C 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 29. Protein kinase A 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 30. Pyruvate carboxylase 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 31. Pyruvate dehydrogenase 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 32. Ribonuclease A 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 33. Ribonucleotide reductase 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 34. Serine racemase 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 35. Soluble quinoprotein glucose dehydrogenase 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 36. Tetrachloroethene reductive dehalogenase—PceA 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 37. Thymidylate synthase 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 38. The 20S proteasome 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 39. Uracil-DNA glycosylase 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 40. Vanadium-dependent chloroperoxidase 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 "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 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 sitesSupports new research in academic, medical and industrial labs, connecting discoveries powered by recent advances in technology and experimental approaches to areas of applicationFeatures short, carefully structured, actionable chapters on various enzyme classes, thus allowing for easy-use and searchability"--EBSCO
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