35 シス型プレニル鎖延長酵素の構造と機能 : Micrococcus luteus B-P26のウンデカプレニル二リン酸合成酵素の構造解析(口頭発表の部)

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Multiple alignments of primary structures of many kinds of prenyltransferases which participate in the most fundamental prenyl-chain backbone synthesizing process in isoprenoid biosynthesis have revealed the presence ofseven conservedregions in the primary structures of (E)-prenyl diphosphate synthases. However, no information has been available about the structures of (Z)-prenyl diphosphate synthases until our recent isolation of the gene for the undecaprenyl diphosphate synthase of Micrococcus luteus B-P 26 by use of the method "colony autoradiography" The amino acid sequence of the (Z)-prenyl diphosphate synthase istotally different from those of (E)-prenyl chain elongating enzymes. Protein data base searches for the sequences similar to that of the undecaprenyl diphosphate synthase yielded many unknown proteins which have not yet been characterized. Two of the proteins have recently been identified as the undecaprenyl diphosphate synthase of Escherichia coli and the dehydrodolichyl diphosphate synthase of Saccharomyces cerevisiae, indicating the presence of five highly conserved regions typical of (Z)-prenyl chain elongating enzymes. The crystal structure of M. luteus B-P 26 UPP synthase was determined at 2.2 A resolution as the first three dimensional structure among cis-prenyl chain elongating enzymes (Fig. 5). This enzyme shows a novel protein fold, which iscompletely different from the structures for the enzymes relating to isoprenoid biosynthesis, which is believed to have a common structure, the so-called "isoprenoid synthase fold". The UPP synthase has a large cleft composed of highly conserved residues among cis-prenyl chain elongating enzymes. A P-loop motif, which is composed of several conserved residues was found in the UPP synthase, suggesting a binding site for the diphosphate moiety of the allylic substrate FPP.
天然有機化合物討論会の論文
2000-10-01

35 シス型プレニル鎖延長酵素の構造と機能 : Micrococcus luteus B-P26のウンデカプレニル二リン酸合成酵素の構造解析(口頭発表の部)

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