解析II型乙二醛酶同工酶YcbL（GlxII-2）在大肠杆菌中的作用。
Deciphering the role of the type II glyoxalase isoenzyme YcbL (GlxII-2) in Escherichia coli.
作者信息
Reiger Matthias, Lassak Jürgen, Jung Kirsten
机构信息
Munich Center for integrated Protein Science (CiPSM) at the Department of Biology I, Microbiology, Ludwig-Maximilians-Universität München, Großhaderner Straße 2-4, D-82152 Martinsried, Germany Institute of Environmental Medicine, UNIKA-T, Neusässer Straße 47, 86156 Augsburg, Germany Faculty of Medicine, Technische Universität München, Ismaningerstr. 22, 81675 Munich, Germany.
Munich Center for integrated Protein Science (CiPSM) at the Department of Biology I, Microbiology, Ludwig-Maximilians-Universität München, Großhaderner Straße 2-4, D-82152 Martinsried, Germany.
出版信息
FEMS Microbiol Lett. 2015 Jan;362(2):1-7. doi: 10.1093/femsle/fnu014. Epub 2014 Dec 4.
In Escherichia coli, detoxification of methylglyoxal (MG) requires glyoxalases I and II. Glyoxalase I (gloA/GlxI) isomerizes the hemithioacetal, formed spontaneously from MG and glutathione (GSH) to S-lactoylglutathione (SLG), which is hydrolyzed by glyoxalase II (gloB/GlxII) to lactate and GSH. YcbL from Salmonella enterica serovar Typhimurium is an unusual type II glyoxalase whose role in MG detoxification has remained enigmatic. Here we show that YcbL (gloC/GlxII-2) acts as an accessory type II glyoxylase in E. coli. The two isoenzymes have additive effects and ensure maximal MG degradation.
在大肠杆菌中，甲基乙二醛（MG）的解毒需要乙二醛酶I和II。乙二醛酶I（gloA/GlxI）将由MG和谷胱甘肽（GSH）自发形成的半硫代乙缩醛异构化为S-乳酰谷胱甘肽（SLG），而乙二醛酶II（gloB/GlxII）则将其水解为乳酸和GSH。鼠伤寒沙门氏菌血清型鼠伤寒杆菌的YcbL是一种不同寻常的II型乙二醛酶，其在MG解毒中的作用一直不明。在此我们表明，YcbL（gloC/GlxII-2）在大肠杆菌中作为辅助性II型乙二醛酶发挥作用。这两种同工酶具有累加效应，并确保MG的最大程度降解。
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