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proteins. Crystal structure of Trypsin, a typical serine protease. Serine proteases (or serine endopeptidases) are enzymes that cleave peptide bonds in proteins. Serine serves as the nucleophilic amino acid at the (enzyme's) active site. [1] They are found ubiquitously in both eukaryotes and prokaryotes.
The active site consists of amino acid residues that form temporary bonds with the substrate, the binding site, and residues that catalyse a reaction of that substrate, the catalytic site. Although the active site occupies only ~10–20% of the volume of an enzyme, [1]: 19 it is the most important part as it directly catalyzes the chemical ...
Michaelis–Menten kinetics. Curve of the Michaelis–Menten equation labelled in accordance with IUBMB recommendations. In biochemistry, Michaelis–Menten kinetics, named after Leonor Michaelis and Maud Menten, is the simplest case of enzyme kinetics, applied to enzyme-catalysed reactions of one substrate and one product.
Adenosine deaminase (also known as adenosine aminohydrolase, or ADA) is an enzyme (EC 3.5.4.4) involved in purine metabolism. It is needed for the breakdown of adenosine from food and for the turnover of nucleic acids in tissues. Its primary function in humans is the development and maintenance of the immune system. [5]
Cytochrome P450. Cytochromes P450 (P450s or CYPs) are a superfamily of enzymes containing heme as a cofactor that mostly, but not exclusively, function as monooxygenases. [1] However, they are not omnipresent; for example, they have not been found in Escherichia coli. [2] In mammals, these enzymes oxidize steroids, fatty acids, xenobiotics, and ...
Citrate synthase (E.C. 2.3.3.1 (previously 4.1.3.7)) is an enzyme that exists in nearly all living cells. It functions as a pace-making enzyme in the first step of the citric acid cycle (or Krebs cycle). [5] Citrate synthase is located within eukaryotic cells in the mitochondrial matrix, but is encoded by nuclear DNA rather than mitochondrial.
Ammonium, rather than ammonia, binds to GS because the binding site is polar and exposed to solvent. [7] In the second step, deprotonation of ammonium allows ammonia to attack the intermediate from its nearby site to form glutamine. [12] Phosphate leaves through the top of the active site, while glutamine leaves through the bottom (between two ...
Acetylcholinesterase (HGNC symbol ACHE; EC 3.1.1.7; systematic name acetylcholine acetylhydrolase), also known as AChE, AChase or acetylhydrolase, is the primary cholinesterase in the body. It is an enzyme that catalyzes the breakdown of acetylcholine and some other choline esters that function as neurotransmitters: