Show simple item record

dc.contributor.authorVerma, Rajni
dc.contributor.authorMitchell-Koch, Katie R.
dc.date.accessioned2015-03-13T21:05:30Z
dc.date.available2015-03-13T21:05:30Z
dc.date.issued2014-03-20
dc.identifier.citationVerma, Rajni; Mitchell-Koch, Katie R. 2014. Insight into the broad substrate promiscuity of E. coli alcohol dehydrogenase. Abstracts of Papers of the American Chemical Society, 247th National Spring Meeting of the American-Chemical-Society (ACS)en_US
dc.identifier.issn0065-7727
dc.identifier.otherWOS:000348455201070
dc.identifier.urihttp://hdl.handle.net/10057/11140
dc.descriptionPresented at the 247th National Spring Meeting of the American-Chemical-Society (ACS), Dallas, Texas on March 20, 2014.en_US
dc.description.abstractThe NADPH-dependent alcohol dehydrogenase (YqhD) from E. coli is a promiscuous enzyme with low substrate specificity. YqhD exhibits aldehyde reductase and alcohol dehydrogenase activity with a broad substrate range and produces biofuels and valuable chemicals. The industrial applicability of the enzyme makes it an ideal candidate for protein engineering studies with the available structure and kinetic information. Herein, we shed light on the substrate promiscuity of YqhD using molecular dynamics (MD) simulations. The MD simulations of YqhD were performed in pure water and at experimental concentrations of substrates, such as isobutaraldehyde and propanaldehyde. The study aims to enhance the knowledge about substrate dynamics in the active site and around the protein, and their relationship to protein structure, function and dynamics. The outcome of the study will enhance our basic understanding of this class of enzyme, with the possible application to guide the rational design of YqhD or related alcohol dehydrogenases to facilitate substrate transport to the active site for enhanced function.en_US
dc.language.isoen_USen_US
dc.publisherAmerican Chemical Societyen_US
dc.relation.ispartofseries247th National Spring Meeting of the American-Chemical-Society (ACS);
dc.titleInsight into the broad substrate promiscuity of E. coli alcohol dehydrogenaseen_US
dc.typeAbstracten_US
dc.rights.holderACS does not own copyrights to the individual abstracts. For permission, please contact the author(s) of the abstract.


Files in this item

FilesSizeFormatView

There are no files associated with this item.

This item appears in the following Collection(s)

Show simple item record