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Structurally informed site-directed mutagenesis of a stereochemically promiscuous aldolase to afford stereochemically complementary biocatalysts


Reference:

Royer, S. F., Haslett, L., Crennell, S. J., Hough, D. W., Danson, M. J. and Bull, S. D., 2010. Structurally informed site-directed mutagenesis of a stereochemically promiscuous aldolase to afford stereochemically complementary biocatalysts. Journal of the American Chemical Society, 132 (33), pp. 11753-11758.

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Official URL:

http://dx.doi.org/10.1021/ja104412a

Abstract

2-Keto-3-deoxygluconate aldolase from the hyperthermophile Sulfolobus solfataricus is a highly thermostable type I aldolase that can catalyze carbon-carbon bond formation using nonphosphorylated substrates. However, it exhibits poor diastereocontrol in many of its aldol reactions, including the reaction of its natural substrates, pyruvate and D-glyceraldehyde, which afford a 55:45 mixture of D-2-keto-3-deoxygluconate (D-KDGlu) and D-2-keto-3-deoxy-galactonate (D-KDGal). We have employed detailed X-ray crystallographic structural information of this aldolase bound to these diastereoisomeric aldol products to selectively target specific amino acids for mutation for the rapid creation of stereochemically complementary mutants that catalyze either (Re)- or (Si)-facial selective aldol reactions to afford either D-KDGlu or D-KDGal with good levels of diastereocontrol.

Details

Item Type Articles
CreatorsRoyer, S. F., Haslett, L., Crennell, S. J., Hough, D. W., Danson, M. J. and Bull, S. D.
DOI10.1021/ja104412a
DepartmentsFaculty of Science > Biology & Biochemistry
Faculty of Science > Chemistry
Research CentresCentre for Extremophile Research (CER)
RefereedYes
StatusPublished
ID Code20593

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