Masai E, Katayama Y, Nishikawa S, Fukuda M
Department of Bioengineering, Nagaoka University of Technology, Nagaoka, Niigata 940-2188, Japan.
J Ind Microbiol Biotechnol. 1999 Oct;23(4-5):364-373. doi: 10.1038/sj.jim.2900747.
Sphingomonas paucimobilis SYK-6 is able to grow on a wide variety of dimeric lignin compounds. These compounds are degraded via vanillate and syringate by a unique enzymatic system, composed of etherases, O demethylases, ring cleavage oxygenases and side chain cleaving enzymes. These unique and specific lignin modification enzymes are thought to be powerful tools for utilization of the most abundant aromatic biomass, lignin. Here, we focus on the genes and enzymes involved in beta-aryl ether cleavage and biphenyl degradation. Two unique etherases are involved in the reductive cleavage of beta-aryl ether. These two etherases have amino acid sequence similarity with the glutathione S-transferases, and use glutathione as a hydrogen donor. It was found that 5,5'-dehydrodivanillate, which is a typical lignin-related biphenyl structure, was transformed into 5-carboxyvanillate by the reaction sequence of O-demethylation, meta-ring cleavage, and hydrolysis, and the genes involved in the latter two reactions have been characterized. Vanillate and syringate are the most common intermediate metabolites in lignin catabolism. These compounds are initially O-demethylated and the resulting diol compounds, protocatechuate (PCA) and 3-O-methylgallate, respectively, are subjected to ring cleavage catalyzed by PCA 4,5-dioxygenase. The ring cleavage products generated are further degraded through the PCA 4,5-cleavage pathway. We have isolated and characterized genes for enzymes involved in this pathway. Disruption of a gene for 2-pyrone-4,6-dicarboxylate hydrolase (ligI) in this pathway suggested that an alternative route for 3-O-methylgallate degradation, in which ligI is not involved, would play a role in syringate catabolism. In this article, we describe the genetic and biochemical features of the S. paucimobilis SYK-6 genes involved in degradation of lignin-related compounds. A possible application of the SYK-6 lignin degradation system to produce a valuable chemical material is also described.
少动鞘氨醇单胞菌SYK-6能够在多种二聚体木质素化合物上生长。这些化合物通过香草酸和丁香酸,由一种独特的酶系统降解,该酶系统由醚酶、O-脱甲基酶、环裂解加氧酶和侧链裂解酶组成。这些独特且特异的木质素修饰酶被认为是利用最丰富的芳香生物质——木质素的有力工具。在此,我们聚焦于参与β-芳基醚裂解和联苯降解的基因与酶。两种独特的醚酶参与β-芳基醚的还原裂解。这两种醚酶与谷胱甘肽S-转移酶具有氨基酸序列相似性,并以谷胱甘肽作为氢供体。研究发现,一种典型的与木质素相关的联苯结构5,5'-脱氢二香草酸,通过O-脱甲基、间位环裂解和水解的反应序列转化为5-羧基香草酸,并且参与后两个反应的基因已得到表征。香草酸和丁香酸是木质素分解代谢中最常见的中间代谢产物。这些化合物首先进行O-脱甲基,然后分别生成的二醇化合物原儿茶酸(PCA)和3-O-甲基没食子酸,由PCA 4,5-双加氧酶催化进行环裂解。生成的环裂解产物通过PCA 4,5-裂解途径进一步降解。我们已分离并表征了参与该途径的酶的基因。该途径中2-吡喃-4,6-二羧酸水解酶(ligI)基因的破坏表明,在丁香酸分解代谢中,一条不涉及ligI的3-O-甲基没食子酸降解替代途径将发挥作用。在本文中,我们描述了少动鞘氨醇单胞菌SYK-6中参与木质素相关化合物降解的基因的遗传和生化特征。还描述了SYK-6木质素降解系统在生产有价值化学材料方面的可能应用。