Catalysis is the increase in rate of a chemical reaction due to an added substance known as a catalyst. Catalysts are not consumed by the reaction and remain unchanged after it. If the reaction is rapid and the catalyst recycles quickly, very small amounts of catalyst often suffice; mixing, surface area, and temperature are important factors in reaction rate. Catalysts generally react with one or more reactants to form intermediates that subsequently give the final reaction product, in the process of regenerating the catalyst.
Chymotrypsin (EC 3.4.21.1, chymotrypsins A and B, alpha-chymar ophth, avazyme, chymar, chymotest, enzeon, quimar, quimotrase, alpha-chymar, alpha-chymotrypsin A, alpha-chymotrypsin) is a digestive enzyme component of pancreatic juice acting in the duodenum, where it performs proteolysis, the breakdown of proteins and polypeptides. Chymotrypsin preferentially cleaves peptide amide bonds where the side chain of the amino acid N-terminal to the scissile amide bond (the P1 position) is a large hydrophobic amino acid (tyrosine, tryptophan, and phenylalanine). These amino acids contain an aromatic ring in their side chain that fits into a hydrophobic pocket (the S1 position) of the enzyme. It is activated in the presence of trypsin. The hydrophobic and shape complementarity between the peptide substrate P1 side chain and the enzyme S1 binding cavity accounts for the substrate specificity of this enzyme. Chymotrypsin also hydrolyzes other amide bonds in peptides at slower rates, particularly those containing leucine at the P1 position.
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.
The mole (symbol mol) is a unit of measurement, the base unit in the International System of Units (SI) for amount of substance, a quantity proportional to the number of elementary entities of a substance. One mole contains exactly 6.02214076×1023 elementary entities (approximately 602 sextillion or 602 billion times a trillion), which can be atoms, molecules, ions, or other particles. The number of particles in a mole is the Avogadro number (symbol N0) and the numerical value of the Avogadro constant (symbol NA) expressed in mol-1. The value was chosen on the basis of the historical definition of the mole as the amount of substance that corresponds to the number of atoms in 12 grams of 12C, which made the mass of a mole of a compound expressed in grams, numerically equal to the average molecular mass of the compound expressed in daltons. With the 2019 redefinition of the SI base units, the numerical equivalence is now only approximate but may be assumed for all practical purposes.
The metric system is a decimal-based system of measurement. The current international standard for the metric system is the International System of Units, in which all units can be expressed in terms of seven base units: the metre (m), kilogram (kg), second (s), ampere (A), kelvin (K), mole (mol), and candela (Cd). These can be made into larger or smaller units with the use of metric prefixes.
A protease is an enzyme that catalyzes proteolysis, breaking down proteins into smaller polypeptides or single amino acids, and spurring the formation of new protein products. They do this by cleaving the peptide bonds within proteins by hydrolysis, a reaction where water breaks bonds. Proteases are involved in numerous biological pathways, including digestion of ingested proteins, protein catabolism, and cell signaling.
The enzyme unit, or international unit for enzyme is a unit of enzyme's catalytic activity.
Serine proteases are enzymes that cleave peptide bonds in proteins. Serine serves as the nucleophilic amino acid at the (enzyme's) active site. They are found ubiquitously in both eukaryotes and prokaryotes. Serine proteases fall into two broad categories based on their structure: chymotrypsin-like (trypsin-like) or subtilisin-like.
In chemistry, dehydrogenation is a chemical reaction that involves the removal of hydrogen, usually from an organic molecule. It is the reverse of hydrogenation. Dehydrogenation is important, both as a useful reaction and a serious problem. At its simplest, it's a useful way of converting alkanes, which are relatively inert and thus low-valued, to olefins, which are reactive and thus more valuable. Alkenes are precursors to aldehydes, alcohols, polymers, and aromatics. As a problematic reaction, the fouling and inactivation of many catalysts arises via coking, which is the dehydrogenative polymerization of organic substrates.
In chemistry, homogeneous catalysis is catalysis where the catalyst is in same phase as reactants, principally by a soluble catalyst in a solution. In contrast, heterogeneous catalysis describes processes where the catalysts and substrate are in distinct phases, typically solid and gas, respectively. The term is used almost exclusively to describe solutions and implies catalysis by organometallic compounds. Homogeneous catalysis is an established technology that continues to evolve. An illustrative major application is the production of acetic acid. Enzymes are examples of homogeneous catalysts.
Reductive amination is a form of amination that involves the conversion of a carbonyl group to an amine via an intermediate imine. The carbonyl group is most commonly a ketone or an aldehyde. It is a common method to make amines and is widely used in green chemistry since it can be done catalytically in one-pot under mild conditions. In biochemistry, dehydrogenase enzymes use reductive amination to produce the amino acid, glutamate. Additionally, there is ongoing research on alternative synthesis mechanisms with various metal catalysts which allow the reaction to be less energy taxing, and require milder reaction conditions. Investigation into biocatalysts, such as imine reductases, have allowed for higher selectivity in the reduction of chiral amines which is an important factor in pharmaceutical synthesis.
In chemistry, a catalytic cycle is a multistep reaction mechanism that involves a catalyst. The catalytic cycle is the main method for describing the role of catalysts in biochemistry, organometallic chemistry, bioinorganic chemistry, materials science, etc.
Enzyme assays are laboratory methods for measuring enzymatic activity. They are vital for the study of enzyme kinetics and enzyme inhibition.
In chemistry, the term "turnover number" has two distinct meanings.
Enzyme kinetics is the study of the rates of enzyme-catalysed chemical reactions. In enzyme kinetics, the reaction rate is measured and the effects of varying the conditions of the reaction are investigated. Studying an enzyme's kinetics in this way can reveal the catalytic mechanism of this enzyme, its role in metabolism, how its activity is controlled, and how a drug or a modifier might affect the rate.
Enzyme catalysis is the increase in the rate of a process by an "enzyme", a biological molecule. Most enzymes are proteins, and most such processes are chemical reactions. Within the enzyme, generally catalysis occurs at a localized site, called the active site.
Filamentous carbon is a carbon-containing deposit structure that refers to several allotropes of carbon, including carbon nanotubes, carbon nanofibers, and microcoils. It forms from gaseous carbon compounds. Filamentous carbon structures all contain metal particles. These are either iron, cobalt, or nickel or their alloys. Deposits of it also significantly disrupt synthesis gas methanation. Acetylene is involved in a number of method of the production of filamentous carbon. The structures of filamentous carbon are mesoporous and on the micrometer scale in dimension. Most reactions that form the structures take place at or above 280 °C (536 °F).
Supramolecular catalysis is not a well-defined field but it generally refers to an application of supramolecular chemistry, especially molecular recognition and guest binding, toward catalysis. This field was originally inspired by enzymatic system which, unlike classical organic chemistry reactions, utilizes non-covalent interactions such as hydrogen bonding, cation-pi interaction, and hydrophobic forces to dramatically accelerate rate of reaction and/or allow highly selective reactions to occur. Because enzymes are structurally complex and difficult to modify, supramolecular catalysts offer a simpler model for studying factors involved in catalytic efficiency of the enzyme. Another goal that motivates this field is the development of efficient and practical catalysts that may or may not have an enzyme equivalent in nature.
Since its introduction in 1960, the base units for the International system of units, known as SI, have changed several times. Tables in this article summarize those changes.
René Peters is a German chemist and since 2008 Professor of Organic Chemistry at the University of Stuttgart.
