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Raymond, Elizabeth A.; Mack, Korrie L.; Yoon, Jennifer H.; Moroz, Olesia V.; Moroz, Yurii S.; Korendovych, Ivan V.
Protein science, April 2015, Letnik: 24, Številka: 4Journal Article
We employed a minimalist approach for design of an allosterically controlled retroaldolase. Introduction of a single lysine residue into the nonenzymatic protein calmodulin led to a 15,000‐fold increase in the second order rate constant for retroaldol reaction with methodol as a substrate. The resulting catalyst AlleyCatR is active enough for subsequent directed evolution in crude cell bacterial lysates. AlleyCatR's activity is allosterically regulated by Ca2+ ions. No catalysis is observed in the absence of the metal ion. The increase in catalytic activity originates from the hydrophobic interaction of the substrate (∼2000‐fold) and the change in the apparent pKa of the active lysine residue.
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JCR | SNIP | JCR | SNIP | JCR | SNIP | JCR | SNIP |
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in: SICRIS
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