{"product_id":"new-experimental-probes-for-enzyme-specificity-and-mechanism-9780443152764","title":"New Experimental Probes for Enzyme Specificity and Mechanism","description":"\u003cp\u003e\u003c\/p\u003e\u003cblockquote\u003e\n\u003cbr\u003eThe latest release in the Methods of Enzymology series, New Experimental Probes for Enzyme Specificity and Mechanism, Volume 685, highlights new advances in the field with interesting chapters on a variety of topics. \u003c\/blockquote\u003e\u003cp\u003e\u003cstrong\u003eFormat\u003c\/strong\u003e: Hardback\u003cbr\u003e\u003cstrong\u003eLength\u003c\/strong\u003e: 570 pages\u003cbr\u003e\u003cstrong\u003ePublication date\u003c\/strong\u003e: 26 May 2023\u003cbr\u003e\u003cstrong\u003ePublisher\u003c\/strong\u003e: Elsevier Science Publishing Co Inc\u003cbr\u003e\u003c\/p\u003e \u003cp\u003e\u003cbr\u003eThe Methods of Enzymology series, Volume 685, the most recent publication, showcases the most recent developments in the field with this new volume, which includes fascinating chapters on a wide range of subjects, including:\u003cbr\u003e\u003cbr\u003eSubverting Hedgehog Protein Autoprocessing by Chemical Induction of Paracatalysis: This chapter explores innovative strategies for manipulating the activity of hedgehog proteins, which are important regulators of cellular processes. By inducing paracatalysis, researchers can develop new therapeutics and therapies for diseases such as cancer.\u003cbr\u003e\u003cbr\u003eNew Mechanistic Probes to Identify Novel Substrates for N-Myristoyltransferases: This chapter discusses the development of novel probes that can identify and characterize novel substrates for N-myristoyltransferases, which are enzymes involved in the synthesis of proteins with specific post-translational modifications. These probes can help researchers better understand the function and regulation of these enzymes in various biological processes.\u003cbr\u003e\u003cbr\u003ePhosphonate and a Fluorophosphonate Analogues of D-Glucose 6-Phosphate as Active-Site Probes of 1L-Myo-Inositol 1 Phosphate Synthase: This chapter describes the use of phosphonate and fluorophosphonate analogues of D-glucose 6-phosphate as active-site probes of 1L-myo-inositol 1 phosphate synthase, an enzyme involved in the synthesis of inositol, a critical cellular compound. These probes can provide valuable insights into the mechanism and regulation of this enzyme.\u003cbr\u003e\u003cbr\u003eKinetic Mechanism of Nicotine-Degrading Enzyme Probed by Stopped-Flow Kinetic Analyses: This chapter explores the kinetic mechanism of nicotine-degrading enzyme, which is important for the degradation of nicotine, a toxic substance found in tobacco products. By using stopped-flow kinetic analyses, researchers can gain a deeper understanding of the enzymatic reaction and identify potential drug targets for the treatment of nicotine addiction.\u003cbr\u003e\u003cbr\u003eKinetics and Mechanism for Enzyme-Catalyzed Reactions of Substrate Pieces: This chapter discusses the kinetics and mechanism for enzyme-catalyzed reactions of substrate pieces, which are important in various biological processes such as metabolism and drug discovery. By understanding the mechanism of these reactions, researchers can develop new strategies for designing and optimizing enzymes for specific applications.\u003cbr\u003e\u003cbr\u003eAdditional chapters cover a wide range of topics, including:\u003cbr\u003e\u003cbr\u003eKinetics and Mechanism for Reactions of Enzyme Pieces: This chapter explores the kinetics and mechanism for reactions of enzyme pieces, which are important in various biological processes such as metabolism and drug discovery. By understanding the mechanism of these reactions, researchers can develop new strategies for designing and optimizing enzymes for specific applications.\u003cbr\u003e\u003cbr\u003eEvaluation of Allostery for the Bienzyme Assembly of a 3-Deoxy-D-Arabino Heptulosonate-7-Phosphate Synthase and Chorismate Mutase: This chapter discusses the evaluation of allostery for the bienzyme assembly of a 3-deoxy-D-arabino heptulosonate-7-phosphate synthase and chorismate mutase, which are enzymes involved in the synthesis of aromatic compounds. By understanding the allosteric mechanism, researchers can develop new strategies for designing and optimizing these enzymes for specific applications.\u003cbr\u003e\u003cbr\u003eRecognition and Catalysis of Reactions of Chiral Substrates by Mandelate Racemase: This chapter discusses the recognition and catalysis of reactions of chiral substrates by mandelate racemase, an enzyme involved in the synthesis of various natural products. By understanding the mechanism of this enzyme, researchers can develop new strategies for designing and optimizing enzymes for the synthesis of chiral compounds.\u003cbr\u003e\u003cbr\u003eInnovative and Emerging Modalities of EGFR Kinase Inhibitors: This chapter discusses the innovative and emerging modalities of EGFR kinase inhibitors, which are drugs used to treat cancer. By understanding the mechanism of these inhibitors, researchers can develop new strategies for improving their efficacy and reducing their side effects.\u003cbr\u003e\u003cbr\u003eCharacterization of the Aminoacrylate Intermediate of Tyrosine Phenol-Lyases: This chapter discusses the characterization of the aminoacrylate intermediate of tyrosine phenol-lyases, which are enzymes involved in the synthesis of various natural products. By understanding the structure and function of this intermediate, researchers can develop new strategies for designing and optimizing these enzymes for specific applications.\u003cbr\u003e\u003cbr\u003eAnd much more!\u003cbr\u003e\u003cbr\u003eThe Methods of Enzymology series, Volume 685, is a valuable resource for researchers and scientists interested in the field of enzymology. It provides comprehensive coverage of the latest advances in the field, with chapters written by leading experts in the field. The book is well-organized and easy to read, making it an essential tool for anyone working in this area.\u003c\/p\u003e\u003cp\u003e\u003cstrong\u003eWeight\u003c\/strong\u003e: 1032g\u003cbr\u003e\u003cstrong\u003eDimension\u003c\/strong\u003e: 239 x 158 x 33 (mm)\u003cbr\u003e\u003cstrong\u003eISBN-13\u003c\/strong\u003e: 9780443152764\u003c\/p\u003e","brand":"Shulph Ink","offers":[{"title":"Hardback","offer_id":44275755319546,"sku":"9780443152764","price":147.8,"currency_code":"GBP","in_stock":false}],"thumbnail_url":"\/\/cdn.shopify.com\/s\/files\/1\/0522\/4297\/2845\/products\/1686311422196_book.jpg?v=1686476486","url":"https:\/\/shulphink.com\/products\/new-experimental-probes-for-enzyme-specificity-and-mechanism-9780443152764","provider":"Shulph Ink","version":"1.0","type":"link"}