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Phloroglucinol Synthase (EC 2)
Phloroglucinol synthase is an acetyltransferase enzyme involved in the synthesis of phloroglucinol (also known as ''1,3,5-trihydroxybenzene'' or ''cyclohexane-1,3,5-trione''), a pharmaceutically and industrially important benzentriol molecule used in medicines and explosives. The enzyme, as taken from the bacterium pseudomonas protegens (Pf-5), is a type III polyketide synthase. The enzyme cyclizes the activated form of 3,5-dioxoheptanedioate. Phloroglucinol synthase exhibits broad substrate specificity, able to accept C4-C12 aliphatic acyl-CoAs and phenylacetyl-CoAs, yielding polyoxoalkylated alpha-pyrones by condensation with malonyl-CoA. The enzyme catalyzes the following reaction, :3 malonyl-CoA + 3 H+ = Phloroglucinol Phloroglucinol is an organic compound with the formula C6H3(OH)3. It is a colorless solid. It is used in the organic synthesis, synthesis of pharmaceuticals and explosives. Phloroglucinol is one of three isomeric benzenetriols. The other two isom ... + 3 CO ... [...More Info...] [...Related Items...] OR: [Wikipedia] [Google] [Baidu] |
AlphaFold
AlphaFold is an artificial intelligence (AI) program developed by DeepMind, a subsidiary of Alphabet, which performs predictions of protein structure. It is designed using deep learning techniques. AlphaFold 1 (2018) placed first in the overall rankings of the 13th Critical Assessment of Structure Prediction (CASP) in December 2018. It was particularly successful at predicting the most accurate structures for targets rated as most difficult by the competition organizers, where no existing template structures were available from proteins with partially similar sequences. AlphaFold 2 (2020) repeated this placement in the CASP14 competition in November 2020. It achieved a level of accuracy much higher than any other entry. It scored above 90 on CASP's global distance test (GDT) for approximately two-thirds of the proteins, a test measuring the similarity between a computationally predicted structure and the experimentally determined structure, where 100 represents a complete matc ... [...More Info...] [...Related Items...] OR: [Wikipedia] [Google] [Baidu] |
Acetyltransferase
An acetyltransferase (also referred to as a transacetylase) is any of a class of transferase enzymes that transfers an acetyl group in a reaction called acetylation. In biological organisms, post-translational modification of a protein via acetylation can profoundly transform its functionality by altering various properties like hydrophobicity, solubility, and surface attributes. These alterations have the potential to influence the protein's conformation and its interactions with substrates, cofactors, and other macromolecules. Types of acetyltransferases Additional examples of acetyltransferases found in nature include: * Chloramphenicol acetyltransferase Structure The predicted three-dimensional structures of histone, choline, and serotonin acetyltransferases are shown below. As with all enzymes, the structures of acetyltransferases are essential for interactions between them and their substrates; alterations to the structures of these enzymes often result in a loss o ... [...More Info...] [...Related Items...] OR: [Wikipedia] [Google] [Baidu] |
Enzyme
An enzyme () is a protein that acts as a biological catalyst by accelerating chemical reactions. The molecules upon which enzymes may act are called substrate (chemistry), substrates, and the enzyme converts the substrates into different molecules known as product (chemistry), products. Almost all metabolism, metabolic processes in the cell (biology), cell need enzyme catalysis in order to occur at rates fast enough to sustain life. Metabolic pathways depend upon enzymes to catalyze individual steps. The study of enzymes is called ''enzymology'' and the field of pseudoenzyme, pseudoenzyme analysis recognizes that during evolution, some enzymes have lost the ability to carry out biological catalysis, which is often reflected in their amino acid sequences and unusual 'pseudocatalytic' properties. Enzymes are known to catalyze more than 5,000 biochemical reaction types. Other biocatalysts include Ribozyme, catalytic RNA molecules, also called ribozymes. They are sometimes descr ... [...More Info...] [...Related Items...] OR: [Wikipedia] [Google] [Baidu] |
Phloroglucinol
Phloroglucinol is an organic compound with the formula C6H3(OH)3. It is a colorless solid. It is used in the organic synthesis, synthesis of pharmaceuticals and explosives. Phloroglucinol is one of three isomeric benzenetriols. The other two isomers are hydroxyquinol (1,2,4-benzenetriol) and pyrogallol (1,2,3-benzenetriol). Phloroglucinol, and its benzenetriol isomers, are still defined as "natural phenol, phenols" according to the IUPAC official nomenclature rules of chemical compounds. Many such monophenolics are often termed polyphenols. The enzyme is biosynthesized by phloroglucinol synthase. Synthesis and occurrence In 1855, phloroglucinol was first prepared from phloretin by the Austrian chemist Heinrich Hlasiwetz (1825–1875). A modern synthesis of phloroglucinol involves hydrolysis of benzene-1,3,5-triamine and its derivatives. Representative is the following route from 1,3,5-Trinitrobenzene, trinitrobenzene. : The synthesis is noteworthy because ordinary aniline deriv ... [...More Info...] [...Related Items...] OR: [Wikipedia] [Google] [Baidu] |
Pseudomonas Protegens
''Pseudomonas protegens'' are widespread Gram-negative, plant-protecting bacteria. Some of the strains of this novel bacterial species (CHA0 and Pf-5, for example) previously belonged to '' P. fluorescens''. They were reclassified since they seem to cluster separately from other fluorescent ''Pseudomonas'' species. ''P. protegens'' is phylogenetically related to the ''Pseudomonas'' species complexes '' P. fluorescens'', '' P. chlororaphis'', and '' P. syringae''. The bacterial species characteristically produces the antimicrobial compounds pyoluteorin and 2,4-diacetylphloroglucinol (DAPG) which are active against various plant pathogens. General characteristics Like '' P. fluorescens'', ''Pseudomonas protegens'' is a typical soil microorganism with an extremely versatile metabolism, and can be isolated from roots of various plant species. The microbe is strictly aerobe (no reduction of nitrate) and oxidase-positive. The bacterium grows at temperatures between 4 °C and 3 ... [...More Info...] [...Related Items...] OR: [Wikipedia] [Google] [Baidu] |
Polyketide
In organic chemistry, polyketides are a class of natural products derived from a Precursor (chemistry), precursor molecule consisting of a Polymer backbone, chain of alternating ketone (, or Carbonyl reduction, its reduced forms) and Methylene group, methylene () groups: . First studied in the early 20th century, discovery, biosynthesis, and application of polyketides has evolved. It is a large and diverse group of secondary metabolites caused by its complex biosynthesis which resembles that of fatty acid synthesis. Because of this diversity, polyketides can have various medicinal, agricultural, and industrial applications. Many polyketides are medicinal or exhibit acute toxicity. Biotechnology has enabled discovery of more naturally-occurring polyketides and evolution of new polyketides with novel or improved bioactivity. History Naturally produced polyketides by various plants and organisms have been used by humans since before studies on them began in the 19th and 20th century ... [...More Info...] [...Related Items...] OR: [Wikipedia] [Google] [Baidu] |
Polyketide Synthase
Polyketide synthases (PKSs) are a family of multi- domain enzymes or enzyme complexes that produce polyketides, a large class of secondary metabolites, in bacteria, fungi, plants, and a few animal lineages. The biosyntheses of polyketides share striking similarities with fatty acid biosynthesis. The PKS genes for a certain polyketide are usually organized in one operon or in gene clusters. Type I and type II PKSs form either large modular protein complexes or dissociable molecular assemblies; type III PKSs exist as smaller homodimeric proteins. Classification PKSs can be classified into three types: * Type I PKSs are large, complex protein structures with multiple modules which in turn consist of several domains that are usually covalently connected to each other and fulfill different catalytic steps. The minimal composition of a type I PKS module consists of an acyltransferase (AT) domain, which is responsible for choosing the building block to be used, a keto synthase (KS) do ... [...More Info...] [...Related Items...] OR: [Wikipedia] [Google] [Baidu] |
Substrate Specificity
Chemical specificity is the ability of binding site of a macromolecule (such as a protein) to bind specific ligands. The fewer ligands a protein can bind, the greater its specificity. Specificity describes the strength of binding between a given protein and ligand. This relationship can be described by a dissociation constant, which characterizes the balance between bound and unbound states for the protein-ligand system. In the context of a single enzyme and a pair of binding molecules, the two ligands can be compared as stronger or weaker ligands (for the enzyme) on the basis of their dissociation constants. (A lower value corresponds to a stronger binding.) Specificity for a set of ligands is unrelated to the ability of an enzyme to catalyze a given reaction, with the ligand as a substrate. If a given enzyme has a high chemical specificity, this means that the set of ligands to which it binds is limited, such that neither binding events nor catalysis can occur at an appreciabl ... [...More Info...] [...Related Items...] OR: [Wikipedia] [Google] [Baidu] |
Aliphatic
In organic chemistry, hydrocarbons ( compounds composed solely of carbon and hydrogen) are divided into two classes: aromatic compounds and aliphatic compounds (; G. ''aleiphar'', fat, oil). Aliphatic compounds can be saturated (in which all the C-C bonds are single, requiring the structure to be completed, or 'saturated', by hydrogen) like hexane, or unsaturated, like hexene and hexyne. Open-chain compounds, whether straight or branched, and which contain no rings of any type, are always aliphatic. Cyclic compounds can be aliphatic if they are not aromatic. Structure Aliphatics compounds can be saturated, joined by single bonds (alkanes), or unsaturated, with double bonds ( alkenes) or triple bonds ( alkynes). If other elements ( heteroatoms) are bound to the carbon chain, the most common being oxygen, nitrogen, sulfur, and chlorine, it is no longer a hydrocarbon, and therefore no longer an aliphatic compound. However, such compounds may still be referred to as aliph ... [...More Info...] [...Related Items...] OR: [Wikipedia] [Google] [Baidu] |
Acyl-CoA
Acyl-CoA is a group of coenzyme A, CoA-based coenzymes that metabolize carboxylic acids. Fatty acyl-CoA's are susceptible to beta oxidation, forming, ultimately, acetyl-CoA. The acetyl-CoA enters the citric acid cycle, eventually forming several equivalents of Adenosine triphosphate, ATP. In this way, fats are converted to ATP, the common biochemical energy carrier. Functions Fatty acid activation Fats are broken down by conversion to acyl-CoA. This conversion is one response to high energy demands such as exercise. The oxidative degradation of fatty acids is a two-step process, catalyzed by Long-chain-fatty-acid—CoA ligase, acyl-CoA synthetase. Fatty acids are converted to their acyl phosphate, the precursor to acyl-CoA. The latter conversion is mediated by acyl-CoA synthase" :acyl-P + HS-CoA → acyl-S-CoA + Pi + H+ Three types of acyl-CoA synthases are employed, depending on the chain length of the fatty acid. For example, the substrates for medium chain acyl-CoA synthas ... [...More Info...] [...Related Items...] OR: [Wikipedia] [Google] [Baidu] |
Phenylacetyl-CoA
Phenylacetyl-CoA (C29H42N7O17P3S) is a form of acetyl-CoA formed from the condensation of the thiol group from coenzyme A with the carboxyl group of phenylacetic acid. Its molecular-weight is 885.7 g/mol. and IUPAC name is ''S''- -[3-(2''R'')-4-[(2''R'',3''S'',4''R'',5''R'')-5-(6-aminopurin-9-yl)-4-hydroxy-3-phosphonooxyoxolan-2-ylethoxy-hydroxyphosphoryl]oxy-hydroxyphosphoryl]oxy-2-hydroxy-3,3-dimethylbutanoyl]amino]propanoylamino]ethyl] 2-phenylethanethioate. It is formed via the actions of Phenylacetate—CoA ligase. Phenylacetyl-CoA is often produced via the reduction of ATP to AMP and the conversion of phenylacetate and CoA to diphosphate and Phenylacetyl-CoA. : ATP + phenylacetate + CoA → AMP + diphosphate + phenylacetyl-CoA This reaction is catalyzed by phenylacetate-CoA ligase. Phenylacetyl-CoA combines with water and quinone to produce phenylglyoxylyl-CoA and quinol via a phenylacetyl-CoA dehydrogenase reaction acting as an oxidoreductase. Phenylacetyl-CoA ... [...More Info...] [...Related Items...] OR: [Wikipedia] [Google] [Baidu] |
Malonyl-CoA
Malonyl-CoA is a coenzyme A derivative of malonic acid. Biosynthesis Malonyl-CoA cannot cross membranes and there is no known malonyl-CoA import mechanism. The biosynthesis therefore takes place locally: * cytosol: Malonyl-CoA is formed by carboxylating acetyl-CoA using the highly regulated enzyme acetyl-CoA carboxylase 1 (ACC1). One molecule of acetyl-CoA joins with a molecule of bicarbonate, requiring energy rendered from ATP. * Mitochondrial outer membrane: Malonyl-CoA is formed by carboxylating acetyl-CoA using the highly regulated enzyme acetyl-CoA carboxylase 2 (ACC2). The reaction is the same as with ACC1. * mitochondrial matrix: Malonyl-CoA is formed in coordinated fashion by mtACC1, a mitochondrial isoform of ACC1, and acyl-CoA synthetase family member 3 (ACSF3), a mitochondrial malonyl-CoA synthetase. MtACC1, like cytosolic ACC1 catalyses the carboxylation of acetyl-CoA, while ACSF3 catalyses the thioesterification of malonate to coenzyme A. The latter serves ... [...More Info...] [...Related Items...] OR: [Wikipedia] [Google] [Baidu] |
