Sulfurtransferases

Essential Enzymes for Life

Buch | Softcover

256 Seiten

2023
Academic Press Inc (Verlag)
978-0-443-18827-5 (ISBN)

Artikel merken

Sulfurtransferases: Essential Enzymes for Life stands as the first comprehensive resource on this increasingly important class of enzymes. Following an introduction to the field from the Editors, each chapter covers a specific sulfurtransferase, including its basic biology and roles in healthy functioning, disease, drug discovery, and other biotechnological applications. The physiological function for each enzyme is considered in depth, along with regulation mechanisms, pharmacological inhibitors, and pathology and conditions related to altered enzymatic activity. Sulfurtransferases discussed include rhodanese, MST, thiosulfate-thiol sulfurtransferase, tRNA uracil 4-sulfurtransferase, thiosulfate-dithiol sulfurtransferases, biotin synthase, cysteine desulfurase, lipoyl synthase, molybdenum cofactor sulfurtransferase, thiazole synthase, molybdopterin synthase sulfurtransferase, molybdopterin synthase, tRNA-uridine 2-sulfurtransferase, tRNA-5-taurinomethyluridine 2-sulfurtransferase, tRNA-5-methyluridine (54) 2-sulfurtransferase, and L-aspartate semialdehyde sulfurtransferase, among others. Here, researchers will discover key knowledge and recent advances to bring forward new studies on this increasingly relevant class of enzymes, while clinicians may apply new findings in medical practice.

Dr. Noriyuki Nagahara is an Associate Professor at the Isotope Research Institute of Nippon Medical School in Tokyo, Japan. He studies the chemical pathogenesis of lung cancer, along with chemical enzymology and molecular biology in the Department of Biochemistry at Nippon Medical School, and environmental medicine in the Department of Environmental Medicine, Nippon Medical School. He has investigated several enzymes, including purine nucleoside phosphorylase, xanthine oxidase, porphobilinogen synthase, thiosulfate sulfurtransferase (rhodanese), and 3-mercaptopyruvate sulfurtransferase (MST). In the course of his research, he found that MST was evolutionally related to rhodanese using protein engineering techniques. He also clarified the cellular and subcellular localization of MST, its enzyme kinetics, antioxidant properties, the characteristics of a cysteine with low redox potential in its catalytic site, and its mechanisms of polysulfide and hydrogen sulfide production. Dr. Nagahara is the author of over 70 original publications, and 6 books, and serves on the editorial boards of several journals, including Scientific Reports. Dr. Munishwar Nath Gupta earned his PhD from Indian Institute of Science, Bengaluru, and completed post-doctoral positions at Massachusetts Institute of Technology (USA), University of Minnesota (USA), Lund University (Sweden), and University of Technology of Compiegne (France). He has taught chemistry, biochemistry, and biotechnology at Indian Institute of Technology, Delhi, between 1975-2016. He was awarded the National Science Talent fellowship (India) and Fellowships of National Academy of Sciences and Indian National Science Academy. He has edited three books on thermostability of enzymes, non-aqueous enzymology and affinity-based separation methods (published by Springer/Birkhauser). He was an Associate Editor of Biocatalysis and Biotransformation (Taylor and Francis) and founding and former editor-in-chief of Sustainable Chemical Processes (Springer). He’s served on editorial boards of several national and international journals and acted as a consultant to Novozyme (Denmark), Dabur (India), and other international companies. His research interests include applied biocatalysis and interfaces of biochemistry with nanotechnology.

ContributorsPreface

1. 3-Mercaptopyruvate sulfurtransferase: the molecular and functional propertiesNoriyuki Nagahara and Takaaki Ito

Adaptation of living organisms to oxidative and chemical environments Molecular evolution of sulfurtransferases MST and evolutionarily related enzymes of TST Molecular, kinetic, and functional properties of MSTProperties of the promoter region of the MST geneMultiple functions of MST related to catalysisPossible production mechanism of H2S and polysulfide from MSTLocalization of MST in rat and mouseMST expression in mouse developmental stagesMST-knockout mouseFuture perspectiveAcknowledgmentsReferencesFurther reading

2. 3-Mercaptopyruvate sulfurtransferase: a review of past and present perspectivesY. Ogasawara

Discovery and earlier characterization of 3-MSTComparison of 3-MST with thiosulfate sulfur transferase (rodanase)Purification and catalytic reactionAmino acid sequence and protein structurePhysiological role of 3-MST3-MST and rhodanese in selenium metabolismMethods for measuring 3-MP and 3-MST activitiesClinical studies on 3-MST and the construction of 3-MST knockout miceLocalization and significance of 3-MST in the central nervous systemInvolvement of 3-MST in sulfane sulfur (bound sulfur) generationReferences

3. The tales of fungal sulfurtransferases: lost, found, and stolenSebastian Piłsyk

References

4. 3-Mercaptopyruvate sulfurtransferase produces hydrogen sulfide (H2S), polysulfides (H2Sn), and other S-sulfurated signaling moleculesHideo Kimura

Introduction3MST produces H2S H2S and H2Sn regulate neuronal transmission 3MST as H2Sn producing enzyme Signaling via S-sulfuration of target proteins Energy formation versus its suppression by H2S Cytoprotection against oxidative stressInvolvement of 3MST and H2S in the pathogenesis of schizophreniaPerspectivesReferences

5. A persulfide shield: an endogenous reactive sulfur species in the forefront in the electrophile detoxification pathwayHisyam Abdul Hamid, Tsuyoshi Takata, Tetsuro Matsunaga and Takaaki Akaike

IntroductionBiosynthesis of biological polysulfidesA “persulfide shield: proposed as an electrophile defense mechanismRSS versus heavy metalsRSS versus alkylating agents and xenobioticsFuture directions of RSS-based researchAcknowledgmentReferences

6. Thiosulfate sulfurtransferase: a model of essential enzyme with potential applications in medicine and biotechnologySilvia Buonvino, Giulia Cinotti and Sonia Melino

IntroductionTST/rhodanese structure: a model for studying the protein foldingTST in the cell metabolismDiseases related to TST dysregulationTST in biotechnologyReferencesFurther reading

7. Chemical approaches to discover selective inhibitors of sulfurtransferases and transsulfuration enzymesEita Sasaki and Kenjiro Hanaoka

IntroductionWidely used inhibitors of CBS, CSE, 3MST, and rhodaneseChemical approaches to discover new inhibitorsConclusionsReferences

8. New insight into the role of TST-derived hydrogen sulfide, a key regulator of mesenteric homeostasis, in health and during chronic fructose intakeOleh Revenko, Yaroslav Pavlovsky, Iryna Kovalchuk, Maryana Savytska and Oksana Zayachkivska

IntroductionThe beneficial role of TST-derived hydrogen sulfideSummaryReferencesFurther reading

9. The S-adenosyl-L-methionine radical enzymes: the lipoic acid synthase and the biotin synthaseAnna Bilska-Wilkosz

Metabolic role of lipoic acidBiosynthesis of lipoic acidMetabolic role of biotinThe biosynthetic pathway of biotinRadical S-adenosyl-L-methionine superfamily of enzymesThe lipoyl synthaseThe biotin synthaseReferences

10. Sulfur transferases in the pathways of molybdenum cofactor biosynthesis and tRNA thiolation in humansSilke Leimkühler and Moses Olalekan Ogunkola

IntroductionThiolation of tRNAThiocarboxylate formation on the URM1 proteinMoco biosynthesisMOCS3NFS1TUM1MTU1CTU1ConclusionsReferencesIndex

Erscheinungsdatum	12.05.2023
Reihe/Serie	Foundations and Frontiers in Enzymology
Mitarbeit	Herausgeber (Serie): Munishwar Nath Gupta
Verlagsort	San Diego
Sprache	englisch
Maße	191 x 235 mm
Gewicht	450 g
Themenwelt	Naturwissenschaften ► Biologie ► Biochemie
Themenwelt	Naturwissenschaften ► Physik / Astronomie ► Angewandte Physik
ISBN-10	0-443-18827-0 / 0443188270
ISBN-13	978-0-443-18827-5 / 9780443188275
Zustand	Neuware