Nicotinoprotein (NADH-containing) alcohol dehydrogenase from Rhodococcus erythropolis DSM 1069: an efficient catalyst for coenzyme-independent oxidation of a broad spectrum of alcohols and the interconversion of alcohols and aldehydes.
Nicotinoprotein (NADH-containing) alcohol dehydrogenase from Rhodococcus erythropolis DSM 1069: an efficient catalyst for coenzyme-independent oxidation of a broad spectrum of alcohols and the interconversion of alcohols and aldehydes.
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来自红平红球菌 DSM 1069 的烟碱蛋白（含 NADH）醇脱氢酶：一种有效的催化剂，用于广泛醇的不依赖于辅酶的氧化以及醇和醛的相互转化。
DOI：
10.1099/00221287-146-4-775
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发表时间：
2000
期刊：
影响因子：
1.5
通讯作者：
J. Duine
中科院分区：
文献类型：
--
作者：
P. Schenkels;J. Duine
苄醇培养的红平红球菌DSM 1069的提取物显示出NAD（P）非依赖性、N，N-二甲基-4-亚硝基苯胺（NDMA）依赖性的醇脱氢酶活性。将表现出这种活性的酶纯化至均一并表征。它似乎是一种典型的烟碱蛋白，因为它含有紧密结合的NADH作为辅因子而不是辅酶。其他特征表明它与已知的来自Amycolatopsis methanolica的烟蛋白醇脱氢酶（np-ADH）高度相似：它是150 kDa的同源四聚体; N-末端氨基酸测序（22个残基）表明这两种酶中77%的氨基酸是相同的，它在pH7.0具有最佳活性，它缺乏NAD（P）H依赖性醛还原酶活性;它催化宽范围的（优选）伯醇和仲醇（脂肪族或芳香族）以及甲醛的氧化，伴随着人工电子受体NDMA的还原。NDMA可以被醛取代，但不能被甲醛取代，酶对醛的底物特异性反映了酶对相应醇的底物特异性。后者也适用于低醛歧化酶活性所显示的酶。结合诱导研究结果，我们认为np-ADH在R.并且在某些情况下还可以催化醇和醛的非辅酶依赖性相互转化。预计这种酶可能具有更广泛的意义，因为结构数据表明，np-ADH也存在于其他（诺卡氏菌）放线菌中。
Extracts from benzyl-alcohol-grown Rhodococcus erythropolis DSM 1069 showed NAD(P)-independent, N,N-dimethyl-4-nitrosoaniline (NDMA)-dependent alcohol dehydrogenase activity. The enzyme exhibiting this activity was purified to homogeneity and characterized. It appears to be a typical nicotinoprotein as it contains tightly bound NADH acting as cofactor instead of coenzyme. Other characteristics indicate that it is highly similar to the known nicotinoprotein alcohol dehydrogenase (np-ADH) from Amycolatopsis methanolica: it is a homotetramer of 150 kDa; N-terminal amino acid sequencing (22 residues) showed that 77% of these amino acids are identical in the two enzymes; it has optimal activity at pH 7.0; it lacks NAD(P)H-dependent aldehyde reductase activity; it catalyses the oxidation of a broad range of (preferably) primary and secondary alcohols, either aliphatic or aromatic, and formaldehyde, with the concomitant reduction of the artificial electron acceptor NDMA. NDMA could be replaced by an aldehyde, but not formaldehyde, the substrate specificity of the enzyme for the aldehydes reflecting that for the corresponding alcohols. The latter also applied to the low aldehyde dismutase activity displayed by the enzyme. From this, together with the results of the induction studies, it is concluded that np-ADH functions as the main alcohol-oxidizing enzyme in the dissimilation of many, but not all, alcohols by R. erythropolis and may also catalyse coenzyme-independent interconversion of alcohols and aldehydes under certain circumstances. It is anticipated that the enzyme may be of even wider significance since structural data indicate that np-ADH is also present in other (nocardioform) actinomycetes.
影响因子：
64.8
作者：
Cole, ST;Brosch, R;Barrell, BG
通讯作者：
Barrell, BG