The substrate tolerance of alcohol oxidases.
The substrate tolerance of alcohol oxidases.
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DOI：
10.1007/s00253-015-6699-6
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发表时间：
2015-08
影响因子：
5
通讯作者：
Faber K
中科院分区：
文献类型：
--
作者：
Pickl M;Fuchs M;Glueck SM;Faber K
醇是一种丰富的可再生化合物来源，但它们必须被激活，以便修改它们的碳主链。后者可以通过氧化生成相应的醛或酮来实现。作为（热力学不利的）烟酰胺依赖的醇脱氢酶的替代品，醇氧化酶利用分子氧，但其在合成生物转化中的应用代表性不足。本文从含铜和黄蛋白醇氧化酶接受电子激活或非激活醇的能力以及醛类过氧化生成羧酸的倾向等方面讨论了含铜和黄蛋白醇氧化酶的机理。为了便于为特定的生物催化应用选择最优的酶，对醇氧化酶的底物耐受性进行了汇编和讨论：底物被分类为不同的组（非活化的基醇和仲醇；活化的烯丙醇、肉桂醇和苯基醇；羟基酸；糖醇；核苷酸醇；甾醇）以及合适的醇氧化酶、它们的微生物来源、相对活性和（立体）选择性。本文的在线版本（doi:10.1007/s00253-015-6699-6）包含补充资料，仅供授权用户使用。
Alcohols are a rich source of compounds from renewable sources, but they have to be activated in order to allow the modification of their carbon backbone. The latter can be achieved via oxidation to the corresponding aldehydes or ketones. As an alternative to (thermodynamically disfavoured) nicotinamide-dependent alcohol dehydrogenases, alcohol oxidases make use of molecular oxygen but their application is under-represented in synthetic biotransformations. In this review, the mechanism of copper-containing and flavoprotein alcohol oxidases is discussed in view of their ability to accept electronically activated or non-activated alcohols and their propensity towards over-oxidation of aldehydes yielding carboxylic acids. In order to facilitate the selection of the optimal enzyme for a given biocatalytic application, the substrate tolerance of alcohol oxidases is compiled and discussed: Substrates are classified into groups (non-activated prim- and sec-alcohols; activated allylic, cinnamic and benzylic alcohols; hydroxy acids; sugar alcohols; nucleotide alcohols; sterols) together with suitable alcohol oxidases, their microbial source, relative activities and (stereo)selectivities. The online version of this article (doi:10.1007/s00253-015-6699-6) contains supplementary material, which is available to authorized users.