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Centre for Extremophile Research

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Staff - Prof. Michael Danson, Dr David Hough, Dr Steve Bull.

Aldolases and chiral c-c synthesis. A novel thermostable aldolase, 2-keto-3-deoxygluconate aldolase (KDGA), has been isolated from the hyperthermophile S.solfataricus. Unlike many other isolated aldolases this type I aldolase has broad substrate specificity, high thermostability and can be expressed efficiently in E.coli. A thermostabile aldolase enzyme has potential for use in pharmaceutical and agrochemical industries, for example in stereoselective carbon-carbon bond forming reactions for assymetric synthesis of complex carbohydrates. Unusually the KDGA was found to exhibit no stereocontrol during reaction of its natural substrates, leading to the discovery of a 'promiscuous metabolic pathway' in S.solfataricus, but requiring engineering for industrial use. Biocatalysis is widely used because of the innate stereocontrol, but the lack of stereocontrol produces chiral molecules that then have to be seperated. Initially the lack of stereocontrol was solved by substrate engineering; a bulky group was added to the substrate forcing stereocontrol. Efforts are now concentrated on engineering the enzyme to exhibit stereocontrol, and this involves site-directed mutagenesis to alter the actiKDG aldolaseve site.

Biofuels from renewable resources. In collaboration with an industrial partner, TMO Biotec Ltd, the CER is isolating novel extremozymes for use in biofuel production. Current work is focussing on the isolation of enzymes for use in bio-diesel and bio-ethanol production.

 

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KDG aldolase