玫瑰栖粪杆菌中1,2-丙二醇脱水反应：底物和对映体选择性的结构基础
1,2-Propanediol Dehydration in Roseburia inulinivorans: STRUCTURAL BASIS FOR SUBSTRATE AND ENANTIOMER SELECTIVITY.
作者信息
LaMattina Joseph W, Keul Nicholas D, Reitzer Pierre, Kapoor Suraj, Galzerani Felipe, Koch Daniel J, Gouvea Iuri E, Lanzilotta William N
机构信息
From the Department of Biochemistry and Molecular Biology, University of Georgia, Athens, Georgia 30602 and.
BRASKEM S.A., Rua Lemos Moonteiro, 120 Edifício Odebrecht São Paulo, Butantã 05501-050-São Paulo, SP Brasil.
出版信息
J Biol Chem. 2016 Jul 22;291(30):15515-26. doi: 10.1074/jbc.M116.721142. Epub 2016 Jun 1.
Glycyl radical enzymes (GREs) represent a diverse superfamily of enzymes that utilize a radical mechanism to catalyze difficult, but often essential, chemical reactions. In this work we present the first biochemical and structural data for a GRE-type diol dehydratase from the organism Roseburia inulinivorans (RiDD). Despite high sequence (48% identity) and structural similarity to the GRE-type glycerol dehydratase from Clostridium butyricum, we demonstrate that the RiDD is in fact a diol dehydratase. In addition, the RiDD will utilize both (S)-1,2-propanediol and (R)-1,2-propanediol as a substrate, with an observed preference for the S enantiomer. Based on the new structural information we developed and successfully tested a hypothesis that explains the functional differences we observe.
甘氨酰自由基酶（GREs）是一类多样的酶超家族，它们利用自由基机制催化困难但往往至关重要的化学反应。在这项工作中，我们展示了来自食菊罗氏菌（RiDD）的GRE型二醇脱水酶的首个生化和结构数据。尽管与丁酸梭菌的GRE型甘油脱水酶具有高度的序列同一性（48%）和结构相似性，但我们证明RiDD实际上是一种二醇脱水酶。此外，RiDD将同时利用（S）-1,2-丙二醇和（R）-1,2-丙二醇作为底物，观察到其对S型对映体有偏好。基于新的结构信息，我们提出并成功验证了一个假设，该假设解释了我们观察到的功能差异。
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