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首页> 外文期刊>Acta crystallographica.Section D. Biological crystallography >Structures of the methyltransferase component of Desulfitobacterium hafniense DCB-2 O-demethylase shed light on methyltetrahydrofolate formation
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Structures of the methyltransferase component of Desulfitobacterium hafniense DCB-2 O-demethylase shed light on methyltetrahydrofolate formation

机译：甲基转移酶的组成部分的结构Desulfitobacterium hafniense DCB-2 O-demethylase阐明methyltetrahydrofolate形成

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摘要

O-Demethylation by acetogenic or organohalide-respiring bacteria leads to the formation of methyltetrahydrofolate from aromatic methyl ethers. O-Demethylases, which are cobalamin-dependent, three-component enzyme systems, catalyse methyl-group transfers from aromatic methyl ethers to tetrahydrofolate via methylcobalamin intermediates. In this study, crystal structures of the tetrahydrofolate-binding methyltransferase module from a Desulfitobacterium hafniense DCB-2 O-demethylase were determined both in complex with tetrahydrofolate and the product methyltetrahydrofolate. While these structures are similar to previously determined methyltransferase structures, the position of key active-site residues is subtly altered. A strictly conserved Asn is displaced to establish a putative proton-transfer network between the substrate N5 and solvent. It is proposed that this supports the efficient catalysis of methyltetrahydrofolate formation, which is necessary for efficient O-demethylation.
机译：O-Demethylation乙酸或organohalide-respiring细菌导致的形成methyltetrahydrofolate芳香甲基醚。cobalamin-dependent、三分量的酶系统,催化甲基转移芳甲基醚tetrahydrofolate通过methylcobalamin中间体。的晶体结构tetrahydrofolate-binding甲基转移酶模块从Desulfitobacterium hafniense DCB-2O-demethylase测定在复杂tetrahydrofolate和产品methyltetrahydrofolate。类似于之前确定吗甲基转移酶结构、关键的位置活性位点残基是巧妙地改变。严格守恒Asn流离失所的建立一个假定的质子转移之间的网络衬底它们和溶剂。这支持高效的催化methyltetrahydrofolate形成,高效O-demethylation所必需的。

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