Institute for Ecopreneurship, School of Life Sciences, University of Applied Sciences Northwestern Switzerland, Muttenz, Switzerland.
Appl Microbiol Biotechnol. 2012 Feb;93(3):1315-24. doi: 10.1007/s00253-011-3451-8. Epub 2011 Jul 14.
In silico analysis of nucleotide sequences flanking the recently found hydroquinone dioxygenase in Sphingomonas sp. strain TTNP3 revealed a gene cluster that encodes a hydroquinone catabolic pathway. In addition to the two open-reading frames encoding the recently characterized hydroquinone dioxygenase, the cluster consisted of six open-reading frames. We were able to express the three open-reading frames, hqdC, hqdD, and hqdE, and demonstrated that the three gene products, HqdC, HqdD, and HqdE had 4-hydroxymuconic semialdehyde dehydrogenase, maleylacetate reductase, and intradiol dioxygenase activity, respectively. Surprisingly, the gene cluster showed similarities to functionally related clusters found in members of the β- and γ-proteobacteria rather than to those found in other members of the genus Sphingomonas sensu latu.
在 Sphingomonas sp. strain TTNP3 中最近发现的对苯二酚双加氧酶周围核苷酸序列的计算机分析揭示了一个基因簇,该基因簇编码对苯二酚的降解途径。除了两个编码最近鉴定的对苯二酚双加氧酶的开放阅读框外,该簇还包含六个开放阅读框。我们能够表达三个开放阅读框 hqdC、hqdD 和 hqdE,并证明这三个基因产物 HqdC、HqdD 和 HqdE 分别具有 4-羟基粘康酸半醛脱氢酶、马来酸乙酰酯还原酶和间二醇双加氧酶活性。令人惊讶的是,该基因簇与β-和γ-变形菌中发现的功能相关簇具有相似性,而不是与其他属 Sphingomonas 中的那些相似。