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Title (Primary) Active site alanine preceding catalytic cysteine determines unique substrate specificity in bacterial CoA‐acylating prenal dehydrogenase
Author Becher, E.; Heese, A.; Claußen, L.; Eisen, S.; Jehmlich, N.; Rohwerder, T.; Purswani, J.;
Journal FEBS Letters
Year 2018
Department UMB; MOLSYB;
Volume 592
Issue 7
Language englisch;
POF III (all) T41;
Supplements https://febs.onlinelibrary.wiley.com/action/downloadSupplement?doi=10.1002%2F1873-3468.13019&attachmentId=2206041928
Keywords active site architecture; acylating aldehyde dehydrogenase; acyl‐CoA‐forming dehydrogenase; biofuel production; fuel oxygenates; hemiterpenes; substrate specificity
Abstract In detoxification and fermentation processes, acylating dehydrogenases catalyze the reversible oxidation of aldehydes to their corresponding acyl‐CoA esters. Here, we characterize an enzyme from Aquincola tertiaricarbonis L108 responsible for prenal (3‐methyl‐2‐butenal) to 3‐methylcrotonyl‐CoA oxidation. Enzyme kinetics demonstrate a preference for C5 substrates not yet observed in aldehyde dehydrogenases. Compared to acetaldehyde and acetyl‐CoA, conversion of valeraldehyde and valeryl‐CoA is > 100‐ and 8‐fold more efficient, respectively. Enzyme variants with A254I, A254P, and A254G mutations indicate that active site Ala preceding the catalytic C255 is crucial for this unique specificity. These results shed new light on evolutionary adaptation of aldehyde dehydrogenases toward xenobiotics and structure‐guided design of highly specific enzymes for production of biofuels, such as linear or iso‐branched butanols and pentanols.
ID 20250
Persistent UFZ Identifier http://www.ufz.de/index.php?en=20939&ufzPublicationIdentifier=20250
Becher, E., Heese, A., Claußen, L., Eisen, S., Jehmlich, N., Rohwerder, T., Purswani, J. (2018):
Active site alanine preceding catalytic cysteine determines unique substrate specificity in bacterial CoA‐acylating prenal dehydrogenase
FEBS Lett. 592 (7), 1150 - 1160