Choose an application

• Reference Manager
• EndNote
• RefWorks (Direct export to RefWorks)

Many plants produce enzymes collectively known as ribosome-inactivating proteins (RIPs). RIPs catalyze the removal of an adenine residue from a conserved loop in the large ribosomal RNA. The adenine residue removed by this depurination is crucial for the binding of elongation factors. Ribosomes modified in this way are no longer able to carry out protein synthesis. Most RIPs exist as single polypeptides (Type 1 RIPs) which are largely non-toxic to mammalian cells because they are unable to enter them and thus cannot reach their ribosomal substrate. In some instances, however, the RIP forms part of a heterodimer where its partner polypeptide is a lectin (Type 2 RIPs). These heterodimeric RIPs are able to bind to and enter mammalian cells. Their ability to reach and modify ribosomes in target cells means these proteins are some of the most potently cytotoxic poisons found in nature, and are widely assumed to play a protective role as part of the host plant’s defenses. RIPs are able to further damage target cells by inducing apoptosis. In addition, certain plants produce lectins lacking an RIP component but which are also cytotoxic. This book focuses on the structure/function and some potential applications of these toxic plant proteins.

Plant proteins. --- Polypeptides. --- Plant proteins --- Polypeptides --- Plant Proteins --- Lectins --- N-Glycosyl Hydrolases --- Proteins --- Glycoside Hydrolases --- Plant Lectins --- Ribosome Inactivating Proteins --- Amino Acids, Peptides, and Proteins --- Hydrolases --- Enzymes --- Chemicals and Drugs --- Enzymes and Coenzymes --- Botany --- Earth & Environmental Sciences --- Plant Physiology --- Life sciences. --- Plant biochemistry. --- Cell biology. --- Plant science. --- Botany. --- Plant physiology. --- Life Sciences. --- Plant Biochemistry. --- Cell Biology. --- Plant Physiology. --- Plant Sciences. --- Biopolymers --- Peptides --- Plant polymers --- Biochemistry. --- Cytology. --- Biological chemistry --- Chemical composition of organisms --- Organisms --- Physiological chemistry --- Biology --- Chemistry --- Medical sciences --- Botanical science --- Phytobiology --- Phytography --- Phytology --- Plant biology --- Plant science --- Natural history --- Plants --- Physiology --- Cell biology --- Cellular biology --- Cells --- Cytologists --- Composition --- Floristic botany --- Phytochemistry --- Plant biochemistry --- Plant chemistry --- Biochemistry --- Phytochemicals --- Plant biochemical genetics

Choose an application

• Reference Manager
• EndNote
• RefWorks (Direct export to RefWorks)

The intent of this volume of Current Topics in Microbiology and Immunology was to bring together a collection of in-depth and cutting edge reviews that highlight our current understanding of the biology of ricin and Shiga toxin (Stx), with the long term goal of advancing the development of countermeasures against these toxic agents.  In May of 2011, Western Europe experienced a severe outbreak of Stx-producing E. coli (STEC) that culminated in more than 3200 cases and 39 deaths.  While Stx is not the only virulence factor associated with STEC, it is certainly the primary determinant associated with the onset of hemolytic uremic syndrome (HUS).  At the present time, there are no clinically approved measures to neutralize Stx in individuals suffering from STEC infection.  Nor are there any preventatives or therapeutics for ricin toxin.  Although incidents of ricin exposure are largely unheard of, federal agencies and public health officials consider it a significant threat.  It is well documented that domestic and international terrorist groups have stockpiled, and in some cases weaponized ricin with the intent of releasing it into the public sphere and causing panic, illness and/or death on a local, regional, or possibly national scale. As the title of this volume indicates, the chapters, written by leading experts in the field, are organized so as to cover all aspects of ricin and Stx, including pathogenesis, immunity, vaccines and therapeutics. This outstanding collection of reviews will serve as an important and readily accessible resource for the research community in the coming years.   .

Antigens and antibodies. --- Chemical agents (Munitions) -- Toxicology. --- Ricin. --- Toxins. --- Verocytotoxins. --- Ricin --- Verocytotoxins --- Chemical agents (Munitions) --- Immunoglobulins --- Ribosome Inactivating Proteins, Type 2 --- Enterotoxins --- Plant Lectins --- Bacterial Toxins --- Albumins --- Ribosome Inactivating Proteins --- Proteins --- Toxins, Biological --- Lectins --- Biological Factors --- N-Glycosyl Hydrolases --- Amino Acids, Peptides, and Proteins --- Plant Proteins --- Glycoside Hydrolases --- Chemicals and Drugs --- Hydrolases --- Enzymes --- Enzymes and Coenzymes --- Shiga Toxins --- Biology --- Health & Biological Sciences --- Microbiology & Immunology --- Pharmacy, Therapeutics, & Pharmacology --- Toxicology --- Immunotherapy. --- Vaccines. --- Therapeutic immunology --- Natural toxicants --- Toxicants, Natural --- Toxins and antitoxins --- Castor bean lectin --- Ricinus lectin --- Medicine. --- Pharmacology. --- Biomedicine. --- Pharmacology/Toxicology. --- Drug effects --- Medical pharmacology --- Medical sciences --- Chemicals --- Chemotherapy --- Drugs --- Pharmacy --- Clinical sciences --- Medical profession --- Human biology --- Life sciences --- Pathology --- Physicians --- Physiological effect --- Biologicals --- Clinical immunology --- Therapeutics --- Antigens --- Metabolites --- Poisons --- Antitoxins --- Detoxification (Health) --- Plant lectins --- Plant toxins --- Toxalbumins --- Toxicology. --- Medicine --- Pharmacology --- Poisoning

Choose an application

• Reference Manager
• EndNote
• RefWorks (Direct export to RefWorks)

This Brief reports on the interplay of an amino-acid mutation towards substrate which could lead to enhanced effects on mutant. These effects need  to  be given consideration in  the  engineering  processes of protein stability and further exploration of such learning are required to provide novel indication for selection of an enzymes.  There  are  very  few  reports  showing  such  stable,  energy  efficient  model  towards  improved  protein function prediction screening in-silico structure based mutagenesis of xylanases from Thermomyces lanuginosus.

Biochemistry. --- Computational biology. --- Life sciences. --- Xylanases -- Biotechnology. --- Computational biology --- Xylanases --- Proteins --- Fungi --- Protein Stability --- Technology, Pharmaceutical --- Glycoside Hydrolases --- Investigative Techniques --- Eukaryota --- Hydrolases --- Amino Acids, Peptides, and Proteins --- Biochemical Phenomena --- Enzymes --- Organisms --- Analytical, Diagnostic and Therapeutic Techniques and Equipment --- Chemical Phenomena --- Chemicals and Drugs --- Enzymes and Coenzymes --- Phenomena and Processes --- Ascomycota --- Fungal Proteins --- Enzyme Stability --- Xylosidases --- Human Anatomy & Physiology --- Biology --- Health & Biological Sciences --- Biology - General --- Animal Biochemistry --- Biotechnology --- Xylanases. --- Analysis. --- Structure-activity relationships. --- Endoxylanases --- Xylan endoxylosidases --- Proteids --- Proteins. --- Enzymology. --- Bioinformatics. --- Life Sciences. --- Protein Science. --- Bio-informatics --- Biological informatics --- Information science --- Systems biology --- Biochemistry --- Biomolecules --- Polypeptides --- Proteomics --- Biosciences --- Sciences, Life --- Science --- Data processing --- Glycosidases --- Enzymes. --- Biocatalysts --- Ferments --- Soluble ferments --- Catalysts --- Enzymology --- Biological chemistry --- Chemical composition of organisms --- Physiological chemistry --- Chemistry --- Medical sciences --- Composition --- Proteins .

Choose an application

• Reference Manager
• EndNote
• RefWorks (Direct export to RefWorks)

The concept of a circular economy relies on waste reduction, valorization, and recycling. Global trends for “green” synthesis of chemicals have positioned the field of enzyme technology and biocatalysis (multi-enzymes and whole-cells) as an alternative for the synthesis of more social- and environmentally-responsible bio-based chemicals. Recent advances in synthetic biology, computational tools, and metabolic engineering have supported the discovery of new enzymes and the rational design of whole-cell biocatalysts. In this book, we highlight these current advances in the field of biocatalysis, with special emphasis on novel enzymes and whole-cell biocatalysts for applications in several industrial biotechnological applications.

Technology: general issues --- 2G ethanol --- hemicellulose usage --- S. cerevisiae --- enzyme immobilization --- cell immobilization --- SHIF --- mannonate dehydratase --- mannose metabolism --- Thermoplasma acidophilum --- mannono-1,4-lactone --- 2-keto-3-deoxygluconate --- aldohexose dehydrogenase --- cyclodextrin glucanotransferases --- large-ring cyclodextrins --- semi rational mutagenesis --- carbohydrate active enzymes --- archaea --- glycosidase --- Sulfolobus solfataricus --- Saccharolobus solfataricus --- Lactobacillus --- β-galactosidase --- immobilization --- cell surface display --- LysM domains --- biocatalysis --- extremophile --- 5-hydroxymethylfurfural --- 5-hydroxymethylfuroic acid --- platform chemicals --- whole cells --- New Delhi metallo-β-lactamase --- NDM-24 --- kinetic profile --- secondary structure --- glycoside hydrolase --- thioglycosides --- Fervidobacterium --- endo-β-1,3-glucanase --- laminarinase --- thermostable --- gene duplication --- cofactor F420 --- deazaflavin --- oxidoreductase --- hydride transfer --- hydrogenation --- asymmetric synthesis --- cofactor biosynthesis --- ω-transaminase --- α-methylbenzylamine --- chiral amine --- biotransformation --- biodiesel --- waste cooking oil --- lipase immobilization --- interfacial activation --- functionalized magnetic nanoparticles --- DNase --- kinetic profiles --- RNase --- semi-rational mutagenesis --- substrate specificity --- engineered Escherichia coli --- flavonoid glucuronides --- multienzyme whole-cell biocatalyst --- organic solvents --- psychrophilic yeast --- hormone-sensitive lipase --- Glaciozyma antarctica --- Antarctica and homology modelling --- keratinase --- serine protease --- metalloprotease --- peptidase --- keratin hydrolysis --- keratin waste --- valorisation --- bioactive peptides --- ene reductase --- enzyme sourcing --- old yellow enzyme --- solvent stability --- machine learning --- flux optimization --- artificial neural network --- synthetic biology --- glycolysis --- metabolic pathways optimization --- cell-free systems --- hydrolase --- lipase --- esterase --- Bacillus subtilis lipase A --- transesterification --- organic solvent --- water activity --- immobilized lipase --- RSM --- fuel properties --- chemo-enzymatic synthesis --- glycosyl transferases --- protein engineering --- carbohydrates --- industrial enzymes --- thermostable enzymes --- glycoside hydrolases --- cell-free biocatalysis --- natural and non-natural multi-enzyme pathways --- bio-based chemicals