Thiamine Pyrophosphate (TPP)-Dependent Enzymes

Inbunden, Engelska, 2026

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Methods in Enzymology: Thiamine pyrophosphate-dependent enzymes Thiamine pyrophosphate (TPP)-dependent enzymes are a diverse group of ubiquitous enzymes. They have in common the use of the biologically active form of vitamin B1 as a cofactor, which gives them the ability to catalyze the formation or cleavage of carbon-sulfur, carbon-oxygen, carbon-nitrogen, and especially carbon-carbon bonds. The specific characteristics of TPP-dependent enzymes, related to both the chemistry of thiamine pyrophosphate and their organization into multimeric subunits, have always aroused the interest of scientists. During these last years they developed original experimental approaches, and also new analytical tools to study, understand and modulate the activity of these enzymes. In the first section of this volume, we propose to address a wide range of methods related to TPP-dependent enzymes as target in health and agrochemistry. Then in a second section, we will focus more particularly on TPP-dependent enzymes in biocatalysis, and in particular on the associated techniques in the field of enzymatic engineering and repurposing. In a third section, we will then address an exciting topic, namely that of the assimilation of one-carbon compounds such as formaldehyde. We will see how TPP enzymes are a tool of choice in biotechnology to address this issue. Finally, we will focus on dual cofactor TPP-dependent enzymes and multi-enzyme complexes using structural and metabolic approaches.

Provides detailed descriptions of innovative and original methodological approaches described by the world’s leading experts in thiamine pyrophosphate-dependent enzymes
Each chapter of the volume will allow the reader to have a complete description of a panel of techniques associated with the subject addressed. The reader can easily adapt it if necessary to his own research theme
From the gene encoding a TPP-dependent enzyme to the enzyme optimized by directed evolution. From the three-dimensional structure of a TPP-dependent enzyme, to rational drug design for selective inhibition, or even from the knowledge of TPP-dependent enzymes to the implementation of artificial metabolic pathways for biotechnology. Here are some non-exhaustive examples that will allow the reader to understand this family of enzymes as well as the current methodological approaches implemented in this context

Produktinformation

Utgivningsdatum2026-12-05
Mått152 x 229 x undefined mm
FormatInbunden
SpråkEngelska
SerieMethods in Enzymology
Antal sidor258
FörlagElsevier Science
ISBN9780443521607

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After completing studies for the A.B., A.M., and Ph.D. degrees in chemistry at Harvard University, David W. Christianson joined the faculty of the University of Pennsylvania, where he is currently the Roy and Diana Vagelos Professor in Chemistry and Chemical Biology. At Penn, Christianson’s research focuses on the structural and chemical biology of the zinc-dependent histone deacetylases as well as enzymes of terpene biosynthesis. His research accomplishments have been recognized by several awards, including the Pfizer Award in Enzyme Chemistry and the Repligen Award in Chemistry of Biological Processes from the American Chemical Society, a Guggenheim Fellowship, and the Elizabeth S. and Richard M. Cashin Fellowship from the Radcliffe Institute for Advanced Study at Harvard University. Christianson is also a dedicated classroom teacher, and his accomplishments in this regard have been recognized by the Lindback Award for Distinguished Teaching at Penn and a Rhodes Trust Inspirational Educator Award from Oxford University. Christianson has also held visiting professorships in the Department of Biochemistry at Cambridge University and the Department of Chemistry and Chemical Biology at Harvard University. Christianson has served with Prof. Anna Pyle as Co-Editor-in-Chief of Methods in Enzymology since 2015.Dr. Karen N. Allen works at the Department of Chemistry of the Boston University, the Metcalf Center for Science and Engineering Franck CHARMANTRAY is a researcher in Biocatalysis at the CNRS. He carries out his research work at the Institute of Chemistry in Clermont-Ferrand (ICCF, UMR6296, Clermont Auvergne University, France). In 2001, he obtained a PhD in medicinal chemistry focusing on « A new family of DNA intercalating-alkylating agents » under the supervision of Dr. M. Demuynck, Grenoble 1 University, France. He then changed his research theme to focus on Studies on Homocitrate Synthase and other Lysine Pathway Enzymes during a postdoctoral internship funded by a BBRSC Fellowship, and carried out under the supervision of Prof. D. Young, at the University of Sussex, Brighton, UK. He returned to France to carry out a 2-year industrial postdoctoral internship in Biocatalysis financed by Laboratoires Fournier and which focused on the chemoenzymatic synthesis of antithrombotics. He was then recruited at the ICCF as a CNRS researcher in 2004. His research themes concern Biocatalysis, and in particular the study and optimization of transketolase by in vitro evolution for the synthesis of rare sugars and analogues in particular. He works in close collaboration with Dr. Bastien Doumèche with whom he recently developed an electrochemical screening for microbial transketolase inhibitors identification. Claude Bernard Lyon 1 and ICBMS (Institut de Chimie et Biochimie Moléculaires et Supramoléculaires, UMR 5246 CNRS, France).After biochemistry and biology studies in Rouen (France), he obtained a master degree in Amiens on a biocatalysis topic, followed by a PhD at the RWTH-Aachen university (Germany) working on immobilized enzymes in two-phase systems under Prof. W. Hartemeier supervision. He joined the group of Dr. Rolland Furstoss and Dr. Alain Archelas at the CNRS in Marseille (France) for a post-doc on multi-gram scale biocatalysis using epoxide hydrolases. After a two-years temporary associate professor position at the university of Cergy-Pontoise (France) with Prof. Véronique Larreta-Garde on sol-gel transitions of protein-polysaccharides mixtures catalysed by enzymes, he became a lecturer at the University Lyon 1in 2006 where he developed original research in heterogeneous biocatalysis (ionic liquids) and more recently electrochemical screening assays using screen-printed electrodes for oxidoreductases (dehydrogenases, oxidases, laccases) and transketolases in collaboration with Dr. Franck Charmantray.

1. Methods for Studying ThDP-dependent Mycobacterial MenDs (SEPHCHC Synthases).Ngoc Anh Thu Ho, Stéphanie Dawes, Ghader Bashiri, Fiona Given, Yuliana Yosaatmajda, Esther Bulloch and Jodie Margaret Johnston2. Mammalian 2-hydroxyacyl-CoA lyases, discovery and assays.Paul P. Van Veldhoven3. Anti-infective target 1-deoxy-d-xylulose-5-phosphate synthase (DXS) and drug design for enzyme inhibition.Matthew R. Groves4. Expression, Purification, and Mechanistic Studies of DXP synthases from Deinococcus radiodurans, Plasmodium falciparum, and Plasmodium vivax.David J. Merkler, Tyler Holets, Nathaniel O. Johnson and Imani S. McCalla5. Comparison of the catalysis of ThPP-dependent enzymes AHAS, ALS, and DXSHeng Li and Wenyun Gao Sr.6. Plant and fungal acetohydroxyacid synthases (AHAS): Methods for heterologous expression, kinetic characterization, and structural analysis.Mario Daniel Garcia Solis7. Biochemical and Structural characterization of novel ‘split-gene’ archeal transketolases.Jennifer Ann Littlechild8. 4-Hydroxybenzoylformate decarboxylase enzymes from Rhodococcus jostii RHA1 and Pseudomonas fluorescens Pf-5: characterisation and involvement in bacterial lignin degradation.Timothy David Bugg and Zhen Wei9. Engineering of phosphoketolase from Bifidobacterium adolescentis for increased activity on non-phosphorylated substrates and application in a cell-free reaction system for ATP regeneration.Thomas Walther, Franziska Kraußer, Christopher M. Topham, Anica Walther and Nadine Ihle10. Repurposing TPP-dependent enzymes with anodic oxidation for the conversion of aldehydes to enantioenriched carboxylic acids.Xiaoqiang Huang, Fengming Shi, Yuanyuan Xu and Binju Wang11. Enhanced ethanol formation by Clostridium thermocellum via pyruvate decarboxylase.Daniel G. Olson12. ArtiSt: an organocatalyst inspired by TPP installed in a steroid-carrying protein creates an artificial stetterase.Dominic J. Campopiano, Amanda Jarvis and Alice MacAulay13. Directed evolution of glycolaldehyde synthase using mass spectrometric screening.Tong Si, Yizhou Luo, Peikai lin, Jianzhi Zhang and Lihao Fu14. Protein engineering of formolase for the synthesis of 1,3-dihydroxyacetone from formaldehyde.Zijian Tan, Haifeng Liu and Leilei Zhu15. Manipulating activity and chemoselectivity of a benzaldehyde lyase to synthesize α-Hydroxyketones.Peiyuan Yao, Qiaqing Wu, Li Yu, Dunming Zhu, Yifan Zhang, Yangyang Chen, Weidong Liu and Jinhui Feng16. Use of dihydroxyacetone synthase for the assimilation of methanol in E. coli.Stéphanie Heux17. Synthesis of phosphonate analogs of 2-oxo acids for site-specific inhibition of 2-oxo acid dehydrogenases in vivo.Nikolaï V. Lukashev, Alexey V. Kazantsev and Victoria I. Bunik18. Biochemical and cryo-EM studies of the pyruvate dehydrogenase complex in native cell extracts.Fotis L. Kyrilis and Panagiotis L. Kastritis19. Metabolic Repurposing of Pyruvate Dehydrogenase and Branched-chain Ketoacid Dehydrogenase in Apicomplexan ParasitesNishith Gupta