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Brain Neoplasms --- Glioma --- Phosphopyruvate Hydratase --- Isoenzymes --- enzymology --- enzymology --- metabolism --- metabolism

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This book is a collection of studies focused on the exploitation of enzyme stereoselectivity for the synthesis of relevant chemicals, such as innovative materials, chiral building blocks, natural products, and flavor and fragrance compounds. Different catalytic approaches are reported. The first study describes a resolution-based process for the stereoselective synthesis of the enantiomeric forms of the flavor compound linaloyl oxide, whereas other enantiomeric enriched aroma compounds were obtained through a novel microbial approach based on solid-state fermentation. Two relevant works exploit the potential of the biocatalyzed reduction reactions. The first of these contributions describes the enantioselective synthesis of ?-nitroalcohols by enzyme-mediated reduction of ?-nitroketones, whereas a second contribution reports the preparation of chiral 1,4-diaryl-1,4-diols through ADH-catalyzed bioreduction of the corresponding diketones. Concerning enantioenriched alcohol derivatives, natural hydroxy fatty acids are prepared by means of the biocatalytic hydration reaction of natural fatty acids using the probiotic bacterium Lactobacillus rhamnosus as a whole-cell biocatalyst. Further studies describe the use of modified pullulan polysaccharide for lipase immobilization and the recent advances in synthetic applications of ?-transaminases for the production of chiral amines.

enantioselective synthesis --- flavors --- n/a --- hydroxy fatty acids --- chiral amines --- diketones --- esters --- oleic acid --- Burkholderia cepacia lipase --- multi-enzymatic cascades --- solid-state fermentation --- biocatalysis --- agro-industrial side stream --- rapeseed cake --- enzyme-mediated resolution --- linolenic acid --- stereoselective biotransformation --- lipases --- kinetic resolution --- 1-phenylethanol --- linseed cake --- bioreduction --- Lactobacillus rhamnosus --- alcohol-dehydrogenase --- enantioselectivity --- hydratase --- reaction engineering --- immobilization --- ?-transaminases --- linoleic acid --- cyclization --- monoterpenes --- 1 --- lactones --- protein engineering --- asymmetric synthesis --- alcohol dehydrogenases --- linaloyl oxide --- chiral resolution --- aroma compounds --- 4-diols --- pullulan --- linalool --- reduction --- nitroketone

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Iron–sulfur (FeS) centers are essential protein cofactors in all forms of life. They are involved in many key biological processes. In particular, Fe-S centers not only serve as enzyme cofactors in catalysis and electron transfer, they are also indispensable for the biosynthesis of complex metal-containing cofactors. Among these cofactors are the molybdenum (Moco) and tungsten (Wco) cofactors. Both Moco/Wco biosynthesis and Fe-S cluster assembly are highly conserved among all kingdoms of life. After formation, Fe-S clusters are transferred to carrier proteins, which insert them into recipient apo-proteins. Moco/Wco cofactors are composed of a tricyclic pterin compound, with the metal coordinated to its unique dithiolene group. Moco/Wco biosynthesis starts with an Fe-S cluster-dependent step involving radical/S-adenosylmethionine (SAM) chemistry. The current lack of knowledge of the connection of the assembly/biosynthesis of complex metal-containing cofactors is due to the sheer complexity of their synthesis with regard to both the (genetic) regulation and (chemical) metal center assembly. Studies on these metal-cofactors/cofactor-containing enzymes are important for understanding fundamental cellular processes. They will also provide a comprehensive view of the complex biosynthesis and the catalytic mechanism of metalloenzymes that underlie metal-related human diseases.

Research & information: general --- Biology, life sciences --- CO dehydrogenase --- dihydrogen --- hydrogenase --- quantum/classical modeling --- density functional theory --- metal–dithiolene --- pyranopterin molybdenum enzymes --- fold-angle --- tungsten enzymes --- electronic structure --- pseudo-Jahn–Teller effect --- thione --- molybdenum cofactor --- Moco --- mixed-valence complex --- dithiolene ligand --- tetra-nuclear nickel complex --- X-ray structure --- magnetic moment --- formate hydrogenlyase --- hydrogen metabolism --- energy conservation --- MRP (multiple resistance and pH)-type Na+/H+ antiporter --- CCCP—carbonyl cyanide m-chlorophenyl-hydrazone --- EIPA—5-(N-ethyl-N-isopropyl)-amiloride --- nicotinamide adenine dinucleotide (NADH) --- electron transfer --- enzyme kinetics --- enzyme structure --- formate dehydrogenase --- carbon assimilation --- Moco biosynthesis --- Fe-S cluster assembly --- l-cysteine desulfurase --- ISC --- SUF --- NIF --- iron --- molybdenum --- sulfur --- tungsten cofactor --- aldehyde:ferredoxin oxidoreductase --- benzoyl-CoA reductase --- acetylene hydratase --- [Fe]-hydrogenase --- FeGP cofactor --- guanylylpyridinol --- conformational changes --- X-ray crystallography --- iron-sulfur cluster --- persulfide --- metallocofactor --- frataxin --- Friedreich’s ataxia --- n/a --- metal-dithiolene --- pseudo-Jahn-Teller effect --- CCCP-carbonyl cyanide m-chlorophenyl-hydrazone --- EIPA-5-(N-ethyl-N-isopropyl)-amiloride --- Friedreich's ataxia

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Biotransformation has accompanied mankind since the Neolithic community, when people settled down and began to engage in agriculture. Modern biocatalysis started in the mid-1850s with the pioneer works of Pasteur. Today, biotransformations have become an indispensable part of our lives, similar to other hi-tech products. Now, in 2019, biocatalysis “received” the Nobel Prize in Chemistry due to prof. Frances H. Arnold’s achievements in the area of the directed evolution of enzymes. This book deals with some major topics of biotransformation, such as the application of enzymatic methods in glycobiology, including the synthesis of hyaluronan, complex glycoconjugates of N-acetylmuramic acid, and the enzymatic deglycosylation of rutin. Enzymatic redox reactions were exemplified by the enzymatic synthesis of indigo from indole, oxidations of β-ketoesters and the engineering of a horse radish peroxidase. The enzymatic reactions were elegantly employed in biosensors, such as glucose oxidase, in the case of electrochemical glucose sensors. Nitrilases are important enzymes for nitrile metabolism in plants and microorganisms have already found broad application in industry—here, these enzymes were for the first time described in Basidiomyceta. This book nicely describes molecular biocatalysis as a pluripotent methodology—“A jack of all trades...”—which strongly contributes to the high quality and sustainability of our daily lives.

E. coli --- recombinant horseradish peroxidase --- site-directed mutagenesis --- periplasm --- glycosylation sites --- Aspergillus niger --- quercetin --- rutin --- rutinose --- rutinosidase --- “solid-state biocatalysis” --- hyaluronic acid --- in vitro synthesis --- one-pot multi-enzyme --- optimization --- enzyme cascade --- Basidiomycota --- Agaricomycotina --- nitrilase --- cyanide hydratase --- nitrile --- substrate specificity --- overproduction --- homology modeling --- substrate docking --- phylogenetic distribution --- indigo --- MISO library --- flavin --- monooxygenase --- FMO --- β-N-acetylhexosaminidases --- transglycosylation --- Glide docking --- Talaromyces flavus --- muramic acid --- non-reducing carbohydrate --- glucose oxidase --- direct electron transfer --- amine-reactive phenazine ethosulfate --- glucose sensor --- glycemic level monitoring --- Pseudomonas putida MnB1 --- biogenic manganese oxides --- abiotic manganese oxides --- α-Hydroxy-β-keto esters --- whole-cell biocatalysis --- surface display --- cell wall anchor --- Lactobacillus plantarum --- whole-cell biocatalyst --- n/a --- Fe(II)/2-ketoglutarate-dependent dioxygenase --- 2-ketoglutarate generation --- regio- and stereo-selective synthesis --- hydroxy amino acids --- sequential cascade reaction --- "solid-state biocatalysis"

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Biotransformation has accompanied mankind since the Neolithic community, when people settled down and began to engage in agriculture. Modern biocatalysis started in the mid-1850s with the pioneer works of Pasteur. Today, biotransformations have become an indispensable part of our lives, similar to other hi-tech products. Now, in 2019, biocatalysis “received” the Nobel Prize in Chemistry due to prof. Frances H. Arnold’s achievements in the area of the directed evolution of enzymes. This book deals with some major topics of biotransformation, such as the application of enzymatic methods in glycobiology, including the synthesis of hyaluronan, complex glycoconjugates of N-acetylmuramic acid, and the enzymatic deglycosylation of rutin. Enzymatic redox reactions were exemplified by the enzymatic synthesis of indigo from indole, oxidations of β-ketoesters and the engineering of a horse radish peroxidase. The enzymatic reactions were elegantly employed in biosensors, such as glucose oxidase, in the case of electrochemical glucose sensors. Nitrilases are important enzymes for nitrile metabolism in plants and microorganisms have already found broad application in industry—here, these enzymes were for the first time described in Basidiomyceta. This book nicely describes molecular biocatalysis as a pluripotent methodology—“A jack of all trades...”—which strongly contributes to the high quality and sustainability of our daily lives.

Technology: general issues --- E. coli --- recombinant horseradish peroxidase --- site-directed mutagenesis --- periplasm --- glycosylation sites --- Aspergillus niger --- quercetin --- rutin --- rutinose --- rutinosidase --- "solid-state biocatalysis" --- hyaluronic acid --- in vitro synthesis --- one-pot multi-enzyme --- optimization --- enzyme cascade --- Basidiomycota --- Agaricomycotina --- nitrilase --- cyanide hydratase --- nitrile --- substrate specificity --- overproduction --- homology modeling --- substrate docking --- phylogenetic distribution --- indigo --- MISO library --- flavin --- monooxygenase --- FMO --- β-N-acetylhexosaminidases --- transglycosylation --- Glide docking --- Talaromyces flavus --- muramic acid --- non-reducing carbohydrate --- glucose oxidase --- direct electron transfer --- amine-reactive phenazine ethosulfate --- glucose sensor --- glycemic level monitoring --- Pseudomonas putida MnB1 --- biogenic manganese oxides --- abiotic manganese oxides --- α-Hydroxy-β-keto esters --- whole-cell biocatalysis --- surface display --- cell wall anchor --- Lactobacillus plantarum --- whole-cell biocatalyst --- Fe(II)/2-ketoglutarate-dependent dioxygenase --- 2-ketoglutarate generation --- regio- and stereo-selective synthesis --- hydroxy amino acids --- sequential cascade reaction --- E. coli --- recombinant horseradish peroxidase --- site-directed mutagenesis --- periplasm --- glycosylation sites --- Aspergillus niger --- quercetin --- rutin --- rutinose --- rutinosidase --- "solid-state biocatalysis" --- hyaluronic acid --- in vitro synthesis --- one-pot multi-enzyme --- optimization --- enzyme cascade --- Basidiomycota --- Agaricomycotina --- nitrilase --- cyanide hydratase --- nitrile --- substrate specificity --- overproduction --- homology modeling --- substrate docking --- phylogenetic distribution --- indigo --- MISO library --- flavin --- monooxygenase --- FMO --- β-N-acetylhexosaminidases --- transglycosylation --- Glide docking --- Talaromyces flavus --- muramic acid --- non-reducing carbohydrate --- glucose oxidase --- direct electron transfer --- amine-reactive phenazine ethosulfate --- glucose sensor --- glycemic level monitoring --- Pseudomonas putida MnB1 --- biogenic manganese oxides --- abiotic manganese oxides --- α-Hydroxy-β-keto esters --- whole-cell biocatalysis --- surface display --- cell wall anchor --- Lactobacillus plantarum --- whole-cell biocatalyst --- Fe(II)/2-ketoglutarate-dependent dioxygenase --- 2-ketoglutarate generation --- regio- and stereo-selective synthesis --- hydroxy amino acids --- sequential cascade reaction