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...

superfamily uses the catalytic triad or dyad in a different protein fold and so represent convergent evolution of the catalytic mechanism. The majority...

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...

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...

utilized for dihydrogen production. These processes could be replicated by a triad assembly, which could oxidize water at one catalyst, reduce protons at another...

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...

broken to regenerate the enzyme. This mechanism is utilised by the catalytic triad of enzymes such as proteases like chymotrypsin and trypsin, where an...

animals, fungi, eubacteria, archaea and viruses. The common use of the catalytic triad for hydrolysis by multiple clans of proteases, including the PA clan...

and a basic residue in a catalytic triad. The chemical and physical constraints on enzyme catalysis have caused identical triad arrangements to evolve independently...

example, proteases such as trypsin perform covalent catalysis using a catalytic triad, stabilize charge build-up on the transition states using an oxyanion...

residue is conserved through the superfamily, not even those in the catalytic triad. Conversely, the individual families that make up a superfamily are...

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...

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...

These proteases share a common catalytic mechanism that involves a nucleophilic cysteine thiol in a catalytic triad or dyad. Discovered by Gopal Chunder...

Protease serine- cysteine- aspartic- metallo- Enzyme Proteolysis Catalytic triad Convergent evolution The Proteolysis Map Protease inhibitor (pharmacology)...

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...

proteases. These enzymes contain a catalytic triad consisting of histidine-57, aspartate-102, and serine-195. This catalytic triad was formerly called a charge...

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...

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...

share common features in their active sites including a conserved catalytic triad or dyad, often including aspartate, glutamate, or serine residues....

metabolism). NAT enzymes are differentiated by the presence of a conserved catalytic triad that favors aromatic amine and hydrazine substrates. NATs catalyze...

activity is orchestrated by a catalytic triad containing the residues His296, Asp345, and Ser441. This noted catalytic triad is typically responsible for...

cysteine as its catalytic nucleophile (as do many other viral proteases). Covalent catalysis is performed with an Asp-His-Cys triad, split between the...

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...

the specific environmental conditions in the enzyme's active site (catalytic triad). Because PMSF bonds covalently to the enzyme, the complex can be viewed...

followed by aging also showed an unexpected conformational change in the catalytic triad suggestive of an "induced fit" between the VX molecule and acetylcholinesterase...

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...

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...

possess a unique, highly conserved Ser-Ser-Lys catalytic triad used for amide hydrolysis, although the catalytic mechanism for acyl-enzyme intermediate formation...

to the substrate. The three residues in particular that comprise a catalytic triad are histidine (His-195), aspartate (Asp-168), both of which work together...