{"id":3581,"date":"2019-05-29T17:45:23","date_gmt":"2019-05-29T08:45:23","guid":{"rendered":"http:\/\/163.180.4.222\/lab\/?p=3581"},"modified":"2019-05-29T17:45:23","modified_gmt":"2019-05-29T08:45:23","slug":"catalytic-machinery-of-enzymes-expanded","status":"publish","type":"post","link":"https:\/\/biochemistry.khu.ac.kr\/lab\/?p=3581","title":{"rendered":"Catalytic machinery of enzymes expanded"},"content":{"rendered":"

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Only a few types of natural amino-acid residue are used directly by enzymes to catalyse reactions. The incorporation of an unnatural residue into an enzyme shows how the catalytic repertoire of enzymes can be enlarged.<\/h5>\n

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Enzymes are exceptionally powerful catalysts that recognize molecular substrates and process them in active sites. They are generally built from just 20 types of amino acid, and their catalytic machinery is typically assembled from chemical groups in the amino-acid side chains, often with extra bound metal ions or cofactors. This raises the question of whether the catalytic repertoire of enzymes could be expanded by using an extended \u2018alphabet\u2019 of amino acids that offers a wider range of side chains for catalysis. <\/span>Writing in\u00a0Nature<\/i><\/a>, Burke\u00a0<\/span>et al.<\/i>1<\/a><\/sup>\u00a0report the construction of an enzyme that uses an unnatural catalytic chemical group, and show that the enzyme\u2019s catalytic properties can be greatly improved using an approach called directed evolution.<\/span><\/span> <\/p>\n<\/div>\n<\/div>\n
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