Identification of coenzyme M biosynthetic phosphosulfolactate synthase - A new family of sulfonate-biosynthesizing enzymes
Identification of coenzyme M biosynthetic phosphosulfolactate synthase - A new family of sulfonate-biosynthesizing enzymes
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DOI：
10.1074/jbc.m201011200
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发表时间：
2002-04-19
影响因子：
4.8
通讯作者：
White, RH
中科院分区：
文献类型：
--
作者：
Graham, DE;Xu, HM;White, RH
超嗜热宽古菌詹氏甲烷球菌使用辅酶M（2-巯基乙磺酸）作为甲烷生成的末端甲基载体。我们描述了一种来自该生物体的酶，（2 R）-磷酸-3-磺基乳酸合酶（ComA），它催化辅酶M生物合成的第一步。ComA催化亚硫酸盐在宽范围的温度和pH条件下与磷酸烯醇式丙酮酸的立体专一性Michael加成。底物和产物类似物中度抑制活性。这种酶没有显着的序列相似性，以前表征的酶，但是，它的Mg 2+依赖的酶反应机制可能是类似的烯醇化酶提出的。一组不同的微生物和植物具有ComA的同源物，这些同源物可能被招募用于硫代乳酸或硫代脂质的生物合成。
The hyperthermophilic euryarchaeon Methanococcus jannaschii uses coenzyme M (2-mereaptoethanesulfonic acid) as the terminal methyl carrier in methanogenesis. We describe an enzyme from that organism, (2R)-phospho-3-sulfolactate synthase (ComA), that catalyzes the first step in coenzyme M biosynthesis. ComA catalyzed the stercospecific Michael addition of sulfite to phosphoenolpyruvate over a broad range of temperature and pH conditions. Substrate and product analogs moderately inhibited activity. This enzyme has no significant sequence similarity to previously characterized enzymes; however, its Mg2+-dependent enzyme reaction mechanism may be analogous to one proposed for enolase. A diverse group of microbes and plants have homologs of ComA that could have been recruited for sulfolactate or sulfolipid biosyntheses.