- Enzymes are macromolecular biological catalysts that accelerate chemical reactions. The molecules upon which enzymes may act are called substrates, and the enzyme converts the substrates into different molecules known as products.
- Enzyme kinetics is the study of the chemical reactions that are catalysed by enzymes. In enzyme kinetics, the reaction rate is measured and the effects of varying the conditions of the reaction are investigated.
- Enzyme catalysis is the increase in the rate of a process by a biological molecule, an “enzyme”. 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.
- Serine proteases are enzymes that cleave peptide bonds in proteins, in which serine serves as the nucleophilic amino acid at the active site. They are found ubiquitously in both eukaryotes and prokaryotes. Serine proteases fall into two broad categories based on their structure: chymotrypsin-like or subtilisin-like.
- Specificity of cutting
- Common active site composition/ structure
- Mechanistically well studied
- Catalytic mechanisms are the crucial link between objectives and performance – they are a galvanizing, non-bureaucratic way to turn one into the other. They are the devices that translate lofty aspirations into concrete reality. They make big, hairy, audacious goals (BHAGs) reachable.
- Michaelis–Menten kinetics is one of the best-known models of enzyme kinetics. It is named after German biochemist Leonor Michaelis and Canadian physician Maud Menten.
- The value of the Michaelis constant is numerically equal to the substrate concentration at which the reaction rate is half of . Biochemical reactions involving a single substrate are often assumed to follow Michaelis–Menten kinetics, without regard to the model’s underlying assumptions.
Lineweaver Burk Plot
- is a graphical representation of the Lineweaver–Burk equation of enzyme kinetics, described by Hans Lineweaver and Dean Burk in 1934.
- Ping Pong is also called the double placement reaction and it means that one or more products are released before all substrates bind the enzyme. One key character of this reaction is the existence of a substituted enzyme intermediate, in which the enzyme is temporarily modified.
- 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.
- any one of a class of enzymes that enact the transfer of specific functional groups from one molecule to another. They are involved in hundreds of different biochemical pathways throughout biology, and are integral to some of life’s most important processes.
- is a class of enzyme that commonly perform as biochemical catalysts that use water to break a chemical bond, which typically results in dividing a larger molecule to smaller molecules.
- a lyase is an enzyme that catalyzes the breaking of various chemical bonds by means other than hydrolysis and oxidation, often forming a new double bond or a new ring structure. The reverse reaction is also possible.
- isomerization is the process by which one molecule is transformed into another molecule which has exactly the same atoms, but the atoms have a different arrangement e.g. A-B-C → B-A-C. In some molecules and under some conditions, isomerization occurs spontaneously.
- ligase is an enzyme that can catalyze the joining of two large molecules by forming a new chemical bond, usually with accompanying hydrolysis of a small pendant chemical group on one of the larger molecules or the enzyme catalyzing the linking together of two compounds
- An enzyme inhibitor is a molecule that binds to an enzyme and decreases its activity. Since blocking an enzyme’s activity can kill a pathogen or correct a metabolic imbalance, many drugs are enzyme inhibitors. They are also used in pesticides.