A catalytic triad is a set of three coordinated amino acids that can be found in the active site of some enzymes. Catalytic triads are most commonly found...
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Active site (redirect from Catalytic site)
enzyme, three amino acid residues work together to form a catalytic triad which makes up the catalytic site. In chymotrypsin, these residues are Ser-195, His-57...
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Serine protease (section Catalytic mechanism)
superfamily uses the catalytic triad or dyad in a different protein fold and so represent convergent evolution of the catalytic mechanism. The majority...
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Protease (section Based on catalytic residue)
the peptide carbonyl group. One way to make a nucleophile is by a catalytic triad, where a histidine residue is used to activate serine, cysteine, or...
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Lipase (section Structure and catalytic mechanism)
B. Huge-Jensen; L. Norskov; et al. (1990). "A serine protease triad forms the catalytic centre of a triacylglycerol lipase". Nature. 343 (6260): 767–70...
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Artificial photosynthesis (section Catalytic triad)
utilized for dihydrogen production. These processes could be replicated by a triad assembly, which could oxidize water at one catalyst, reduce protons at another...
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digestive enzymes called triacylglycerol lipases, EC 3.1.1.3, that use the catalytic triad of aspartate, histidine, and serine to hydrolyze medium and long-chain...
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Enzyme catalysis (redirect from Catalytic mechanism)
broken to regenerate the enzyme. This mechanism is utilised by the catalytic triad of enzymes such as proteases like chymotrypsin and trypsin, where an...
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Cysteine protease (section Catalytic mechanism)
These proteases share a common catalytic mechanism that involves a nucleophilic cysteine thiol in a catalytic triad or dyad. Discovered by Gopal Chunder...
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and a basic residue in a catalytic triad. The chemical and physical constraints on enzyme catalysis have caused identical triad arrangements to evolve independently...
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example, proteases such as trypsin perform covalent catalysis using a catalytic triad, stabilize charge build-up on the transition states using an oxyanion...
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Group II intron (redirect from Group II catalytic intron)
by a catalytic triad made up by CGC, while Group IIA and Group IIB are made up by AGC catalytic triad, which is more similar to the catalytic triad of the...
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residue is conserved through the superfamily, not even those in the catalytic triad. Conversely, the individual families that make up a superfamily are...
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active site, which contains a catalytic dyad that has been likened to the catalytic triad of chymotrypsin. The catalytic dyad is made up of the amino acids...
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Protease serine- cysteine- aspartic- metallo- Enzyme Proteolysis Catalytic triad Convergent evolution The Proteolysis Map Protease inhibitor (pharmacology)...
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proteases. These enzymes contain a catalytic triad consisting of histidine-57, aspartate-102, and serine-195. This catalytic triad was formerly called a charge...
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PA clan of proteases (section Catalytic activity)
animals, fungi, eubacteria, archaea and viruses. The common use of the catalytic triad for hydrolysis by multiple clans of proteases, including the PA clan...
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the central catalytic domain. The core domain belongs to the papain-like protease superfamily (CA clan) and uses a Cys-His-Asp catalytic triad. Protein 4...
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metabolism). NAT enzymes are differentiated by the presence of a conserved catalytic triad that favors aromatic amine and hydrazine substrates. NATs catalyze...
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Ranpirnase's active site encompasses a catalytic triad that commonly found in the RNase A superfamily. This catalytic triad consists of His10, Lys31, and His97...
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cysteine as its catalytic nucleophile (as do many other viral proteases). Covalent catalysis is performed with an Asp-His-Cys triad, split between the...
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activity is orchestrated by a catalytic triad containing the residues His296, Asp345, and Ser441. This noted catalytic triad is typically responsible for...
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the specific environmental conditions in the enzyme's active site (catalytic triad). Because PMSF bonds covalently to the enzyme, the complex can be viewed...
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sides. The active site of the Cre enzyme consists of the conserved catalytic triad residues Arg 173, His 289, Arg 292 as well as the conserved nucleophilic...
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filament consisting of 6-26 subunits. Nitrilase exploits the Lys-Cys-Glu catalytic triad which is essential for its active site function and enhancing its performance...
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histidine 57 and aspartic acid 102, this serine residue constitutes the catalytic triad of the active site. These findings rely on inhibition assays and the...
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followed by aging also showed an unexpected conformational change in the catalytic triad suggestive of an "induced fit" between the VX molecule and acetylcholinesterase...
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contains a catalytic triad of syrine, histine and arginine, which is conserved across all mutants and is proposed to initiate the reaction. The triad residues...
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subunits and has the characteristic Asp-Thr-Gly (Asp25, Thr26 and Gly27) catalytic triad sequence common to aspartic proteases. As HIV-1 PR can only function...
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Cerastocytin (section Catalytic triad)
distinguishing features: the hydrophobic pocket, the positive surface and the catalytic triad. Additionally, the tertiary structure of cerastocytin is maintained...
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