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Microviridin
The microviridins are a class of serine protease inhibitors produced by various genera of cyanobacteria. Recent genome mining has shown that the biosynthetic gene cluster responsible for microviridin biosynthesis is much more prevalent, found in many species of Pseudomonadota (formerly Proteobacteria) and Bacteriodota (formerly Bacteriodetes). Microviridins are members of the RiPP family of natural products. The first microviridin was isolated from ''Microcystis viridis'' (NIES-102) and its structure was reported in 1990. Microviridins are characterized by a tricyclic depsipeptide structure resulting from the enzymatic activity of two dedicated ATP-grasp ligases, which form two lactone and one lactam rings in the core region of the precursor peptide. Toxicity Microviridin J has been found to disrupt molting in the invertebrate ''Daphnia pulicaria'', probably as a result of its protease inhibitory effects See also *Cyanotoxin *Cyanopeptolin Cyanopeptolins (CPs) are a class o ... [...More Info...] [...Related Items...] OR: [Wikipedia] [Google] [Baidu] |
Ribosomally Synthesized And Post-translationally Modified Peptides
Ribosomally synthesized and post-translationally modified peptides (RiPPs), also known as ribosomal natural products, are a diverse class of natural products of ribosomal origin. Consisting of more than 20 sub-classes, RiPPs are produced by a variety of organisms, including prokaryotes, eukaryotes, and archaea, and they possess a wide range of biological activity, biological functions. As a consequence of the falling cost of genome sequencing and the accompanying rise in available genomic data, scientific interest in RiPPs has increased in the last few decades. Because the chemical structures of RiPPs are more closely predictable from genomic data than are other natural products (e.g. alkaloids, terpenoids), their presence in sequenced organisms can, in theory, be identified rapidly. This makes RiPPs an attractive target of modern natural product discovery efforts. Definition RiPPs consist of any peptides (i.e. molecular weight below 10 kDa) that are ribosomally-produced and unde ... [...More Info...] [...Related Items...] OR: [Wikipedia] [Google] [Baidu] |
Cyanotoxin
Cyanotoxins are toxins produced by cyanobacteria (also known as blue-green algae). Cyanobacteria are found almost everywhere, but particularly in lakes and in the ocean where, under high concentration of phosphorus conditions, they reproduce exponentially to form blooms. Blooming cyanobacteria can produce cyanotoxins in such concentrations that they can poison and even kill animals and humans. Cyanotoxins can also accumulate in other animals such as fish and shellfish, and cause poisonings such as shellfish poisoning. Some of the most powerful natural poisons known are cyanotoxins. They include potent neurotoxins, hepatotoxins, cytotoxins, and endotoxins. The ''cyano'' in the term cyanobacteria refers to its colour, not to its relation to cyanides, though cyanobacteria can catabolize hydrogen cyanide during nitrogen fixation. Exposure to cyanobacteria can result in gastro-intestinal and hayfever symptoms or pruritic skin rashes. Exposure to the cyanobacteria neurotoxin ... [...More Info...] [...Related Items...] OR: [Wikipedia] [Google] [Baidu] |
Cyanopeptolin
Cyanopeptolins (CPs) are a class of oligopeptides produced by Microcystis and Planktothrix algae strains, and can be neurotoxic. The production of cyanopeptolins occurs through nonribosomal peptides synthases (NRPS). Chemistry CPs are, in general, a six-residue peptide formed into a ring by a beta-lactone bridge, making them chemically depsipeptides (peptidolactones). The first position is usually threonine, which links to one or two residues via an ester bound on the beta-hydroxyl group; the third position is conserved to be 3-amino-6-hydroxy-2-piperidone (Ahp) or a derivative. All other positions are highly variable. There is not a single, unified nomenclature, for CPs. Names such as CP1020 and CP1138 refer to the molar mass. Others, such as aeruginopeptins, micropeptins, microcystilide, nostopeptins, and oscillapeptins, refer to the organism the substance is originally found in. Factors affecting production Increased water temperatures, because of climate change and eutrophic ... [...More Info...] [...Related Items...] OR: [Wikipedia] [Google] [Baidu] |
Protease Inhibitor (biology)
In biology and biochemistry, protease inhibitors, or antiproteases, are molecules that inhibit the function of proteases (enzymes that aid proteolysis, the breakdown of proteins). Many naturally occurring protease inhibitors are proteins. In medicine, ''protease inhibitor'' is often used interchangeably with alpha 1-antitrypsin (A1AT, which is abbreviated PI for this reason). A1AT is indeed the protease inhibitor most often involved in disease, namely in alpha-1 antitrypsin deficiency. Classification Protease inhibitors may be classified either by the type of protease they inhibit, or by their mechanism of action. In 2004 Rawlings and colleagues introduced a classification of protease inhibitors based on similarities detectable at the level of amino acid sequence. This classification initially identified 48 families of inhibitors that could be grouped into 26 related superfamily (or clans) by their structure. According to the MEROPS database there are now 81 families of inhibito ... [...More Info...] [...Related Items...] OR: [Wikipedia] [Google] [Baidu] |
Cyanobacteria
Cyanobacteria ( ) are a group of autotrophic gram-negative bacteria that can obtain biological energy via oxygenic photosynthesis. The name "cyanobacteria" () refers to their bluish green (cyan) color, which forms the basis of cyanobacteria's informal common name, blue-green algae. Cyanobacteria are probably the most numerous taxon to have ever existed on Earth and the first organisms known to have produced oxygen, having appeared in the middle Archean eon and apparently originated in a freshwater or terrestrial environment. Their photopigments can absorb the red- and blue-spectrum frequencies of sunlight (thus reflecting a greenish color) to split water molecules into hydrogen ions and oxygen. The hydrogen ions are used to react with carbon dioxide to produce complex organic compounds such as carbohydrates (a process known as carbon fixation), and the oxygen is released as a byproduct. By continuously producing and releasing oxygen over billions of years, cyanobacte ... [...More Info...] [...Related Items...] OR: [Wikipedia] [Google] [Baidu] |
Gene Cluster
A gene cluster is a group of two or more genes found within an organism's DNA that encode similar peptide, polypeptides or proteins which collectively share a generalized function and are often located within a few thousand base pairs of each other. The size of gene clusters can vary significantly, from a few genes to several hundred genes. Portions of the DNA sequence of each gene within a gene cluster are found to be identical; however, the protein encoded by each gene is distinct from the proteins encoded by the other genes within the cluster. Gene clusters often result from expansions of a single gene caused by repeated duplication events, and may be observed near one another on the same chromosome or on different, but homologous chromosomes. An example of a gene cluster is the Hox gene, which is made up of eight genes and is part of the Homeobox gene family. Formation Historically, four models have been proposed for the formation and persistence of gene clusters. Gene dupli ... [...More Info...] [...Related Items...] OR: [Wikipedia] [Google] [Baidu] |
Pseudomonadota
Pseudomonadota (synonym "Proteobacteria") is a major phylum of gram-negative bacteria. Currently, they are considered the predominant phylum within the domain of bacteria. They are naturally found as pathogenic and free-living (non- parasitic) genera. The phylum comprises six classes ''Acidithiobacillia, Alphaproteobacteria, Betaproteobacteria, Gammaproteobacteria, Hydrogenophilia'', and '' Zetaproteobacteria.'' The Pseudomonadota are widely diverse, with differences in morphology, metabolic processes, relevance to humans, and ecological influence. Classification American microbiologist Carl Woese established this grouping in 1987, calling it informally the "purple bacteria and their relatives". The group was later formally named the 'Proteobacteria' after the Greek god Proteus, who was known to assume many forms. In 2021 the International Committee on Systematics of Prokaryotes designated the synonym Pseudomonadota, and renamed many other prokaryotic phyla as well. Th ... [...More Info...] [...Related Items...] OR: [Wikipedia] [Google] [Baidu] |
Microcystis
''Microcystis'' is a genus of freshwater cyanobacteria that includes the harmful algal bloom-forming '' Microcystis aeruginosa''. Over the last few decades, cyanobacterial blooms caused by eutrophication have become a major environmental problem in aquatic ecosystems worldwide, and the most representative and harmful cyanobacteria is ''Microcystis''.'''' ''Microcystis'' blooms have increased due to global climate change, spanning six continents and causing increased health risks to wildlife and humans. This article will address the conditions for the growth of ''Microcystis,'' physical characteristics, ecology, geographic distribution'','' and health risks of ''Microcystis.'' Conditions for ''Microcystis'' During the summer in temperate systems, ''Microcystis'' can rise to form blooms on the water surface. These blooms, linked to anthropogenic nutrient loading, occur generally when water temperatures exceed 15 °C. But, as the global climate changes, the intensity and oc ... [...More Info...] [...Related Items...] OR: [Wikipedia] [Google] [Baidu] |
Depsipeptide
A depsipeptide is a peptide in which one or more of its amide, -C(O)NHR-, groups are replaced by the corresponding ester, -C(O)OR-. Many depsipeptides have both peptide and ester linkages. Elimination of the N–H group in a peptide structure results in a decrease of H-bonding capability, which is responsible for secondary structure and folding patterns of peptides, thus inducing structural deformation of the helix and β-sheet structures. Because of decreased resonance delocalization in esters relative to amides, depsipeptides have lower rotational barriers for cis-trans isomerization and therefore they have more flexible structures than their native analogs. They are mainly found in marine and microbial natural products. Depsipeptide natural products 222px, Enterochelin is a depsipeptide that is an iron-transporter. Several depsipeptides have been found to exhibit anti-cancer properties. A depsipeptide enzyme inhibitor includes romidepsin, a member of the bicyclic peptide clas ... [...More Info...] [...Related Items...] OR: [Wikipedia] [Google] [Baidu] |
ATP-grasp
In molecular biology, the ATP-grasp fold is a unique ATP-binding protein structural motif made of two α+ β subdomains that "grasp" a molecule of ATP between them. ATP-grasp proteins have ATP-dependent carboxylate-amine/thiol ligase activity. Structure Proteins of the ATP-grasp family have an overall structural configuration organised into three domains referred to as the N-terminal domain (or A-domain), the central domain (or B-domain), and the C-terminal domain (or C-domain). Function ATP-grasp enzymes catalyse the ATP-dependent ligation of a carboxylate-containing molecule to an amino or thiol group-containing molecule. The reactions typically involve formation of acylphosphate intermediates. These enzymes are involved in various metabolic pathways including purine biosynthesis, fatty acid synthesis, and gluconeogenesis. Examples of proteins containing this domain * D-alanine-D-alanine ligase * glutathione synthetase * biotin carboxylase * carbamoyl phosphate s ... [...More Info...] [...Related Items...] OR: [Wikipedia] [Google] [Baidu] |
