tailieunhanh - Báo cáo khoa học: The crystal structure of coenzyme B12-dependent glycerol dehydratase in complex with cobalamin and propane-1,2-diol

Recombinant glycerol dehydratase ofKlebsiella pneumoniae was purified to homogeneity. The subunit composition of the enzyme was most probablya2b2c2 .When(R)- and (S)-propane-1,2-diolswere used independently as substrates, the rate with the (R)-enantiomer was times faster than that with the (S)-isomer. In contrast to diol dehydratase,an iso-functional enzyme,the affinity of the enzyme for the (S)-isomer was essentially the same or only slightly higher than that for the (R)-isomer (Km(R) /Km(S) ¼). . | Eur. J. Biochem. 269 ddsd dd M 22002 FEBS 2002 doi The crystal structure of coenzyme B12-dependent glycerol dehydratase in complex with cobalamin and propane-1 2-diol Mamoru Yamanishi1 Michio Yunoki1. Takamasa Tobimatsu1. Hideaki Sato1. Junko Matsui1. Avako Dokiva1. Yasuhiro iuchi1. Kazunori Oe1. Kvoko Suto2. Naoki Shibata2. Yukio Morimoto2 Noritake Yasuoka2 B fB f BB B B B B ff B BB BB B B B B B FF BB B B FF B B FF FB B B B F B B F F F BB B ff B B FF FF B BB F F B B B Ff fB B ff B BB B BB FF B B B FF B B B B B FF B FF B B FF B B B ff B B fF B ff FB BB ff B B ff and Tetsuo Torava1 1 Department of Bioscience and Biotechnology Faculty of Engineering Okayama University Okayama department of Life Science Himeji Institute of Technology Hyogo Japan Recombinant glycerol dehydratase of Klebsiella pneumoniae was purified to homogeneity. The subunit composition of the enzyme was most probably a2p2Y2. When R - and S -propane-1 2-diols were used independently as substrates the rate with the R -enantiomer was times faster than that with the S -isomer. In contrast to diol dehydratase an isofunctional enzyme the affinity of the nit yme oor the S -isomer was essentially the same or only slightly higher than that for the R -isomer Km R Km S . The crystal structure of glycerol dehydratase in complex with cyanocobalamin and propane-1 2-diol was determined at A resolution. The enzyme exists as a dimer of the abc heterotrimer. Cobalamin is bound at the interface between the a and b subunits in the so-called base-on mode with 5 6-dimethylbenzimidazole of the nucleotide moiety coordinating to the cobalt atom. The electron density of the cyano group was almost unobservable suggetfing that the cyanocobalamin was reduced to cob II alamin by X-ray irradiation. Theactivesiteisina b a 8 barrel that was formed by a central region of the a subunit. The substrate propane-1 2-diol and essential cofactor K are bound inside the b a 8 barrel above the .

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