Sulfurtransferases

Essential Enzymes for Life

1st Edition - May 2, 2023
Imprint: Academic Press
Editors: Noriyuki Nagahara, Munishwar Nath Gupta
Language: English
Paperback ISBN:
9 7 8 - 0 - 4 4 3 - 1 8 8 2 7 - 5
eBook ISBN:
9 7 8 - 0 - 4 4 3 - 1 8 8 2 8 - 2

Sulfurtransferases: Essential Enzymes for Life stands as the first comprehensive resource on this increasingly important class of enzymes. Following an introduction to the field… Read more

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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.

Cover image
Title page
Table of Contents
Foundations and frontiers in enzymology series
Copyright
Contributors
Preface
1. 3-Mercaptopyruvate sulfurtransferase: the molecular and functional properties
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 MST
Properties of the promoter region of the MST gene
Multiple functions of MST related to catalysis
Possible production mechanism of H2S and polysulfide from MST
Localization of MST in rat and mouse
MST expression in mouse developmental stages
MST-knockout mouse
Future perspective
2. 3-Mercaptopyruvate sulfurtransferase: a review of past and present perspectives
Discovery and earlier characterization of 3-MST
Comparison of 3-MST with thiosulfate sulfur transferase (rodanase)
Purification and catalytic reaction
Amino acid sequence and protein structure
Physiological role of 3-MST
3-MST and rhodanese in selenium metabolism
Methods for measuring 3-MP and 3-MST activities
Clinical studies on 3-MST and the construction of 3-MST knockout mice
Localization and significance of 3-MST in the central nervous system
Involvement of 3-MST in sulfane sulfur (bound sulfur) generation
3. The tales of fungal sulfurtransferases: lost, found, and stolen
4. 3-Mercaptopyruvate sulfurtransferase produces hydrogen sulfide (H2S), polysulfides (H2Sn), and other S-sulfurated signaling molecules
Introduction
3MST 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 stress
Involvement of 3MST and H2S in the pathogenesis of schizophrenia
Perspectives
5. A persulfide shield: an endogenous reactive sulfur species in the forefront in the electrophile detoxification pathway
Introduction
Biosynthesis of biological polysulfides
A “persulfide shield”: proposed as an electrophile defense mechanism
RSS versus heavy metals
RSS versus alkylating agents and xenobiotics
Future directions of RSS-based research
6. Thiosulfate sulfurtransferase: a model of essential enzyme with potential applications in medicine and biotechnology
Introduction
TST/rhodanese structure: a model for studying the protein folding
TST in the cell metabolism
Diseases related to TST dysregulation
TST in biotechnology
7. Chemical approaches to discover selective inhibitors of sulfurtransferases and transsulfuration enzymes
Introduction
Widely used inhibitors of CBS, CSE, 3MST, and rhodanese
Chemical approaches to discover new inhibitors
Conclusions
8. New insight into the role of TST-derived hydrogen sulfide, a key regulator of mesenteric homeostasis in health and during chronic fructose intake
Introduction
The beneficial role of TST-derived hydrogen sulfide
Summary
9. The S-adenosyl-l-methionine radical enzymes: the lipoic acid synthase and the biotin synthase
Metabolic role of lipoic acid
Biosynthesis of lipoic acid
Metabolic role of biotin
The biosynthetic pathway of biotin
Radical S-adenosyl-l-methionine superfamily of enzymes
The lipoyl synthase
The biotin synthase
10. Sulfur transferases in the pathways of molybdenum cofactor biosynthesis and tRNA thiolation in humans
Introduction
Thiolation of tRNA
Thiocarboxylate formation on the URM1 protein
Moco biosynthesis
MOCS3
NFS1
TUM1
MTU1
CTU1
Conclusions
Index

Noriyuki Nagahara

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.

Affiliations and expertise

MD, PhD, Associate Professor, Isotope Research Institute, Nippon Medical School, Tokyo, Japan

Munishwar Nath Gupta

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.

Affiliations and expertise

Formerly post-doctoral positions: Massachusetts Institute of Technology, USA, University of Minnesota, USA, Lund University, Sweden, University of Technology of Compiegne, France

Life Sciences

Physical Sciences & Engineering

Social Sciences & Humanities

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