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Change of product specificity of hexaprenyl diphosphate synthase from Sulfolobus solfataricus by introducing mimetic
Hisashi Hemmi1, Motoyoshi Noike, Toru Nakayama
1Department of Biochemistry and Engineering, Graduate School of Engineering, Tohoku University, Aoba-yama 07, Sendai-shi, 980-8579, Miyagi-ken, Japan.
Abstract:
The introduction of several sets of amino acid substitutions into the region around a substrate-binding site of a medium-chain (all-E) prenyl diphosphate synthase, hexaprenyl diphosphate synthase from a thermoacidophilic archaeon Sulfolobus solfataricus, to mimic the product determination mechanisms of various kinds of short-chain enzymes revealed that the structure around the region of the medium-chain enzyme resembles those of eukaryotic farnesyl diphosphate synthases but not those of the other short-chain enzymes, reflecting the evolutional relationships among these enzymes.