Sulfurtransferases

Essential Enzymes for Life
Erscheinungsjahr 2023
ISBN: 978-0-443-18827-5
Verlag: Elsevier Science & Technology

Buch, Englisch, Format (B × H): 191 mm x 235 mm, Gewicht: 450 g

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.

Autoren/Hrsg.

Nagahara, Noriyuki

Weitere Mitwirkende

Gupta, Munishwar Nath

Fachgebiete

• Naturwissenschaften Physik Angewandte Physik Biophysik
• Naturwissenschaften Biowissenschaften Biochemie (nichtmedizinisch)

Inhaltsverzeichnis

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 Pilsyk

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, Tsuy

Über Autor(innen)

Gupta, Munishwar Nath
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.

Nagahara, Noriyuki
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.