Anaerobic Activation of p-Cymene in Denitrifying Betaproteobacteria: Methyl Group Hydroxylation versus Addition to Fumarate
Anaerobic Activation of p-Cymene in Denitrifying Betaproteobacteria: Methyl Group Hydroxylation versus Addition to Fumarate
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反硝化 Betaproteobacteria 中对伞花烃的厌氧活化：甲基羟基化与添加到富马酸盐
DOI：
10.1128/aem.02385-14
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发表时间：
2014
影响因子：
4.4
通讯作者：
Rabus R
中科院分区：
文献类型：
--
作者：
Strijkstra A;Trautwein K;Jarling R;Wöhlbrand L;Dörries M;Reinhardt R;Drozdowska M;Golding BT;Wilkes H;Rabus R
betaproteobacteria“Aromatoleum aromaticum”pCyN1和“Thauera”sp. strain pCyN2在硝酸盐还原条件下厌氧降解植物源芳烃-花枝烃（4-异丙基甲苯）。对伞花适应的“A”的代谢物分析。aromaticum “ pCyN1细胞特异生成4-异丙基苄基醇和4-异丙基苯甲醛，而” Thauera " sp. pCyN2细胞特异生成4-异丙基苄基琥珀酸酯和初步鉴定的（4-异丙基苯基）itaconate。两株菌株均检测到4-异丙基苯甲酸酯。对这两种菌株的对伞花素和琥珀酸适应细胞的蛋白质基因组学研究显示，不同的蛋白质谱与伞花素形成的不同代谢物相一致。”一个。aromaticum pCyN1特异性地产生(i)一种推定的对伞花烯脱氢酶（CmdABC），预计将对伞花烯的苯基甲基羟基化，（ii）两种推定氧化4-异丙基苯甲醇（Iod）和4-异丙基苯甲醛（Iad）的脱氢酶，以及（iii）推定的4-异丙基苯甲酸辅酶a （CoA）连接酶（Ibl）。另一方面，“Thauera”sp. pCyN2的对花青素特异性蛋白谱包含了与甲苯活化苄基琥珀酸合成酶（称为[4-异丙基苄基]琥珀酸合成酶IbsABCDEF；已鉴定亚基IbsAE）和苄基琥珀酸β-氧化（Bbs）途径的蛋白同源物（称为BisABCDEFGH；除BisEF外均已鉴定）。本研究表明，两种相关的反硝化细菌对同一种底物对伞花烃采用完全不同的外周降解途径，两种途径在4-异丙基苯甲酰辅酶a水平上明显收敛。
The betaproteobacteria “Aromatoleum aromaticum” pCyN1 and “Thauera” sp. strain pCyN2 anaerobically degrade the plant-derived aromatic hydrocarbonp-cymene (4-isopropyltoluene) under nitrate-reducing conditions. Metabolite analysis ofp-cymene-adapted “A. aromaticum” pCyN1 cells demonstrated the specific formation of 4-isopropylbenzyl alcohol and 4-isopropylbenzaldehyde, whereas with “Thauera” sp. pCyN2, exclusively 4-isopropylbenzylsuccinate and tentatively identified (4-isopropylphenyl)itaconate were observed. 4-Isopropylbenzoate in contrast was detected with both strains. Proteogenomic investigation ofp-cymene- versus succinate-adapted cells of the two strains revealed distinct protein profiles agreeing with the different metabolites formed fromp-cymene. “A. aromaticum” pCyN1 specifically produced (i) a putativep-cymene dehydrogenase (CmdABC) expected to hydroxylate the benzylic methyl group ofp-cymene, (ii) two dehydrogenases putatively oxidizing 4-isopropylbenzyl alcohol (Iod) and 4-isopropylbenzaldehyde (Iad), and (iii) the putative 4-isopropylbenzoate-coenzyme A (CoA) ligase (Ibl). Thep-cymene-specific protein profile of “Thauera” sp. pCyN2, on the other hand, encompassed proteins homologous to subunits of toluene-activating benzylsuccinate synthase (termed [4-isopropylbenzyl]succinate synthase IbsABCDEF; identified subunits, IbsAE) and protein homologs of the benzylsuccinate β-oxidation (Bbs) pathway (termed BisABCDEFGH; all identified except for BisEF). This study reveals that two related denitrifying bacteria employ fundamentally different peripheral degradation routes for one and the same substrate,p-cymene, with the two pathways apparently converging at the level of 4-isopropylbenzoyl-CoA.
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