|
Cinnamyl-alcohol Dehydrogenase
In enzymology, a cinnamyl-alcohol dehydrogenase () is an enzyme that catalyzes the chemical reaction :cinnamyl alcohol + NADP+ \rightleftharpoons cinnamaldehyde + NADPH + H+ Thus, the two substrates of this enzyme are cinnamyl alcohol and NADP+, whereas its 3 products are cinnamaldehyde, NADPH, and H+. This enzyme belongs to the family of oxidoreductases, specifically those acting on the CH-OH group of donor with NAD+ or NADP+ as acceptor. The systematic name of this enzyme class is cinnamyl-alcohol:NADP+ oxidoreductase. Other names in common use include cinnamyl alcohol dehydrogenase, and CAD. This enzyme participates in phenylpropanoid biosynthesis. Structural studies As of late 2007, 4 structures A structure is an arrangement and organization of interrelated elements in a material object or system, or the object or system so organized. Material structures include man-made objects such as buildings and machines and natural objects such as ... have been solved for this c ... [...More Info...] [...Related Items...] OR: [Wikipedia] [Google] [Baidu] |
Enzymology
Enzymes () are proteins that act as biological catalysts by accelerating chemical reactions. The molecules upon which enzymes may act are called substrates, and the enzyme converts the substrates into different molecules known as products. Almost all metabolic processes in the 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 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 are catalytic RNA molecules, called ribozymes. Enzymes' specificity comes from their unique three-dimensional structures. Like all catalysts, enzymes increase the reacti ... [...More Info...] [...Related Items...] OR: [Wikipedia] [Google] [Baidu] |
Oxidoreductase
In biochemistry, an oxidoreductase is an enzyme that catalyzes the transfer of electrons from one molecule, the reductant, also called the electron donor, to another, the oxidant, also called the electron acceptor. This group of enzymes usually utilizes NADP+ or NAD+ as cofactors. Transmembrane oxidoreductases create electron transport chains in bacteria, chloroplasts and mitochondria, including respiratory complexes I, II and III. Some others can associate with biological membranes as peripheral membrane proteins or be anchored to the membranes through a single transmembrane helix. in |
Protein Data Bank
The Protein Data Bank (PDB) is a database for the three-dimensional structural data of large biological molecules, such as proteins and nucleic acids. The data, typically obtained by X-ray crystallography, NMR spectroscopy, or, increasingly, cryo-electron microscopy, and submitted by biologists and biochemists from around the world, are freely accessible on the Internet via the websites of its member organisations (PDBe, PDBj, RCSB, and BMRB). The PDB is overseen by an organization called the Worldwide Protein Data Bank, wwPDB. The PDB is a key in areas of structural biology, such as structural genomics. Most major scientific journals and some funding agencies now require scientists to submit their structure data to the PDB. Many other databases use protein structures deposited in the PDB. For example, SCOP and CATH classify protein structures, while PDBsum provides a graphic overview of PDB entries using information from other sources, such as Gene ontology. History Two ... [...More Info...] [...Related Items...] OR: [Wikipedia] [Google] [Baidu] |
Tertiary Structure
Protein tertiary structure is the three dimensional shape of a protein. The tertiary structure will have a single polypeptide chain "backbone" with one or more protein secondary structures, the protein domains. Amino acid side chains may interact and bond in a number of ways. The interactions and bonds of side chains within a particular protein determine its tertiary structure. The protein tertiary structure is defined by its atomic coordinates. These coordinates may refer either to a protein domain or to the entire tertiary structure.Branden C. and Tooze J. "Introduction to Protein Structure" Garland Publishing, New York. 1990 and 1991. A number of tertiary structures may fold into a quaternary structure.Kyte, J. "Structure in Protein Chemistry." Garland Publishing, New York. 1995. History The science of the tertiary structure of proteins has progressed from one of hypothesis to one of detailed definition. Although Emil Fischer had suggested proteins were made of poly ... [...More Info...] [...Related Items...] OR: [Wikipedia] [Google] [Baidu] |
Phenylpropanoid Biosynthesis
The biosynthesis of phenylpropanoids involves a number of enzymes. From amino acids to cinnamates In plants, all phenylpropanoids are derived from the amino acids phenylalanine and tyrosine. Phenylalanine ammonia-lyase (PAL, a.k.a. phenylalanine/tyrosine ammonia-lyase) is an enzyme that transforms L-phenylalanine and tyrosine into trans-cinnamic acid and ''p''-coumaric acid, respectively. Trans-cinnamate 4-monooxygenase (cinnamate 4-hydroxylase) is the enzyme that transforms trans-cinnamate into 4-hydroxycinnamate (''p''-coumaric acid). 4-Coumarate-CoA ligase is the enzyme that transforms 4-coumarate (''p''-coumaric acid) into 4-coumaroyl-CoA. Enzymes associated with biosynthesis of hydroxycinnamic acids * Cinnamyl-alcohol dehydrogenase (CAD), an enzyme that transforms cinnamyl alcohol into cinnamaldehyde * Sinapine esterase, an enzyme that transforms sinapoylcholine into sinapate ( sinapic acid) and choline * Trans-cinnamate 2-monooxygenase, an enzyme that transforms ... [...More Info...] [...Related Items...] OR: [Wikipedia] [Google] [Baidu] |
List Of Enzymes
This article lists enzymes by their classification in the International Union of Biochemistry and Molecular Biology's Enzyme Commission (EC) numbering system. * List of EC numbers (EC 5) * List of EC numbers (EC 6) :Oxidoreductases (EC 1) ( Oxidoreductase) * Dehydrogenase *Luciferase * DMSO reductase :EC 1.1 (act on the CH-OH group of donors) * :EC 1.1.1 (with NAD+ or NADP+ as acceptor) ** Alcohol dehydrogenase (NAD) ** Alcohol dehydrogenase (NADP) ** Homoserine dehydrogenase ** Aminopropanol oxidoreductase **Diacetyl reductase ** Glycerol dehydrogenase ** Propanediol-phosphate dehydrogenase **glycerol-3-phosphate dehydrogenase (NAD+) **D-xylulose reductase ** L-xylulose reductase ** Lactate dehydrogenase ** Malate dehydrogenase ** Isocitrate dehydrogenase **HMG-CoA reductase * :EC 1.1.2 (with a cytochrome as acceptor) * :EC 1.1.3 (with oxygen as acceptor) ** Glucose oxidase ** L-gulonolactone oxidase ** Thiamine oxidase ** Xanthine oxidase * :EC 1.1. ... [...More Info...] [...Related Items...] OR: [Wikipedia] [Google] [Baidu] |
Hydrogen Ion
A hydrogen ion is created when a hydrogen atom loses or gains an electron. A positively charged hydrogen ion (or proton) can readily combine with other particles and therefore is only seen isolated when it is in a gaseous state or a nearly particle-free space. Due to its extremely high charge density of approximately 2×1010 times that of a sodium ion, the bare hydrogen ion cannot exist freely in solution as it readily hydrates, i.e., bonds quickly. The hydrogen ion is recommended by IUPAC as a general term for all ions of hydrogen and its isotopes. Depending on the charge of the ion, two different classes can be distinguished: positively charged ions and negatively charged ions. Cation (positively charged) A hydrogen atom is made up of a nucleus with charge +1, and a single electron. Therefore, the only positively charged ion possible has charge +1. It is noted H+. Depending on the isotope in question, the hydrogen cation has different names: * Hydron: general name r ... [...More Info...] [...Related Items...] OR: [Wikipedia] [Google] [Baidu] |
Enzyme
Enzymes () are proteins that act as biological catalysts 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 are Ribozyme, catalytic RNA molecules, called ribozymes. Enzymes' Chemical specificity, specific ... [...More Info...] [...Related Items...] OR: [Wikipedia] [Google] [Baidu] |
Cinnamaldehyde
Cinnamaldehyde is an organic compound with the formula(C9H8O) C6H5CH=CHCHO. Occurring naturally as predominantly the ''trans'' (''E'') isomer, it gives cinnamon its flavor and odor. It is a phenylpropanoid that is naturally synthesized by the shikimate pathway. This pale yellow, viscous liquid occurs in the bark of cinnamon trees and other species of the genus ''Cinnamomum''. The essential oil of cinnamon bark is about 90% cinnamaldehyde. Cinnamaldehyde decomposes to styrene because of oxidation as a result of bad storage or transport conditions. Styrene especially forms in high humidity and high temperatures. This is the reason why cinnamon contains small amounts of styrene. Structure and synthesis Cinnamaldehyde was isolated from cinnamon essential oil in 1834 by Jean-Baptiste Dumas and Eugène-Melchior Péligot and synthesized in the laboratory by the Italian chemist Luigi Chiozza in 1854. The natural product is ''trans''-cinnamaldehyde. The molecule consists of a benz ... [...More Info...] [...Related Items...] OR: [Wikipedia] [Google] [Baidu] |
Product (chemistry)
Products are the species formed from chemical reactions. During a chemical reaction, reactants are transformed into products after passing through a high energy transition state. This process results in the consumption of the reactants. It can be a spontaneous reaction or mediated by catalysts which lower the energy of the transition state, and by solvents which provide the chemical environment necessary for the reaction to take place. When represented in chemical equations, products are by convention drawn on the right-hand side, even in the case of reversible reactions. The properties of products such as their energies help determine several characteristics of a chemical reaction, such as whether the reaction is exergonic or endergonic. Additionally, the properties of a product can make it easier to extract and purify following a chemical reaction, especially if the product has a different state of matter than the reactants. Spontaneous reaction : R \rightarrow P *Where ... [...More Info...] [...Related Items...] OR: [Wikipedia] [Google] [Baidu] |
