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Schwefeltransferasen: Essentielle Enzyme Taschenbuch Nagahara Enzymologie 2023-

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Sulfurtransferases : Essential Enzymes paperback Nagahara enzymology 2023
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Artikelzustand
Neuwertig: Buch, das wie neu aussieht, aber bereits gelesen wurde. Der Einband weist keine ...
ISBN
9780443188275
Publication Year
2023
Series
Foundations and Frontiers in Enzymology Ser.
Type
Textbook
Format
Trade Paperback
Language
English
Publication Name
Sulfurtransferases : Essential Enzymes for Life
Author
Noriyuki Nagahara
Item Length
9.2in
Publisher
Elsevier Science & Technology
Item Width
7.5in
Number of Pages
472 Pages

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Product Information

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.

Product Identifiers

Publisher
Elsevier Science & Technology
ISBN-10
0443188270
ISBN-13
9780443188275
eBay Product ID (ePID)
19058368837

Product Key Features

Author
Noriyuki Nagahara
Publication Name
Sulfurtransferases : Essential Enzymes for Life
Format
Trade Paperback
Language
English
Publication Year
2023
Series
Foundations and Frontiers in Enzymology Ser.
Type
Textbook
Number of Pages
472 Pages

Dimensions

Item Length
9.2in
Item Width
7.5in

Additional Product Features

Lc Classification Number
Qp606.S85
Table of Content
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, 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
Copyright Date
2023
Topic
Life Sciences / Biochemistry, Life Sciences / Biophysics
Dewey Decimal
612.015192
Intended Audience
Scholarly & Professional
Dewey Edition
23
Genre
Science

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