S-D-lactoylglutatione

• 分子结构分类: 有机化合物 - 有机酸及其衍生物 - 羧酸及其衍生物
• 英文名称: S-D-lactoylglutatione
• 英文别名: (4S)-4-amino-N-[(2R)-1-(carboxymethylamino)-3-[(2R)-2-hydroxypropanoyl]sulfanyl-1-oxopropan-2-yl]-5-hydroxy-5-oxopentanimidate
• 化学式: C₁₃H₂₀N₃O₈S
• 分子量: 378.383
• InChiKey: VDYDCVUWILIYQF-CSMHCCOUSA-M

计算性质

• 辛醇/水分配系数(LogP)：
  -3.3
• 重原子数：
  25
• 可旋转键数：
  10
• 环数：
  0.0
• sp3杂化的碳原子比例：
  0.62
• 拓扑面积：
  229
• 氢给体数：
  4
• 氢受体数：
  9

反应信息

• 作为反应物：
  描述：

  S-D-lactoylglutatione 生成 (R)-2-((S)-4-Amino-4-carboxy-butyrylamino)-2-(carboxymethyl-carbamoyl)-ethanethiol anion 、 丙酮醛
  参考文献：
  名称：

  RACKER E., J Biol Chem, 1951, 0021-9258, 685-96

  摘要：

  DOI：

文献信息

• Deciphering the role of the type II glyoxalase isoenzyme YcbL (GlxII-2) in Escherichia coli
  作者：Matthias Reiger、Jürgen Lassak、Kirsten Jung

  DOI：10.1093/femsle/fnu014

  日期：2015.1.1

  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）将半硫代缩醛（由MG和谷胱甘肽（GSH）自发形成）异构化为S-乳酰谷胱甘肽（SLG），后者由乙二醛酶II（gloB/GlxII）水解为乳酸和GSH。肠炎沙门氏菌（Salmonella enterica serovar Typhimurium）的YcbL是一种不寻常的II型乙二醛酶，其在MG解毒中的作用一直是个谜。在这里，我们展示了YcbL（gloC/GlxII-2）在大肠杆菌中作为辅助II型乙二醛酶的作用。这两种同工酶具有协同作用，可确保最大程度的MG降解。
• Ni2+-activated glyoxalase I from Escherichia coli: Substrate specificity, kinetic isotope effects and evolution within the βαβββ superfamily
  作者：Kadia Y. Mullings、Nicole Sukdeo、Uthaiwan Suttisansanee、Yanhong Ran、John F. Honek

  DOI：10.1016/j.jinorgbio.2011.11.008

  日期：2012.3

  The Escherichia coli glyoxalase system consists of the metalloenzymes glyoxalase I and glyoxalase II. Little is known regarding Ni2+-activated E. coli glyoxalase I substrate specificity, its thiol cofactor preference, the presence or absence of any substrate kinetic isotope effects on the enzyme mechanism, or whether glyoxalase I might catalyze additional reactions similar to those exhibited by related beta alpha beta beta beta structural superfamily members. The current investigation has shown that this two-enzyme system is capable of utilizing the thiol cofactors glutathionylspermidine and trypanothione, in addition to the known tripeptide glutathione, to convert substrate methylglyoxal to non-toxic D-lactate in the presence of Ni2+ ion. E. coli glyoxalase I, reconstituted with either Ni2+ or Cd2+, was observed to efficiently process deuterated and non-deuterated phenylglyoxal utilizing glutathione as cofactor. Interestingly, a substrate kinetic isotope effect for the Ni2+-substituted enzyme was not detected; however, the proton transfer step was observed to be partially rate limiting for the Cd2+-substituted enzyme. This is the first non-Zn2+-activated GlxI where a metal ion-dependent kinetic isotope effect using deuterium-labelled substrate has been observed. Attempts to detect a glutathione conjugation reaction with the antibiotic fosfomycin, similar to the reaction catalyzed by the related superfamily member FosA, were unsuccessful when utilizing the E. coli glyoxalase I E56A mutein. (c) 2011 Elsevier Inc. All rights reserved.
• RACKER E., J Biol Chem, 1951, 0021-9258, 685-96
  作者：RACKER E.

  DOI：——

  日期：——
• Preparation and assay of glutathione thiol esters. Survey of human liver glutathione thiol esterases
  作者：Lasse Uotila

  DOI：10.1021/bi00744a024

  日期：1973.9.1
• Escherichia coli glyoxalase II is a binuclear zinc-dependent metalloenzyme
  作者：Jason O’Young、Nicole Sukdeo、John F. Honek

  DOI：10.1016/j.abb.2006.11.024

  日期：2007.3

  Cytotoxic methylglyoxal is detoxified by the two-enzyme glyoxalase system. Glyoxalase I (GlxI) catalyzes conversion of non-enzymatically produced methylglyoxal-glutathione hemithioacetal into its corresponding thioester. Glyoxalase II (Glx II) hydrolyzes the thioester into D-lactate and free glutathione. Glyoxalase I and II are metalloenzymes, which possess mononuclear and binuclear active sites, respectively. There are two distinct classes of GlxI; the first class is Zn2+-dependent and is composed of GlxI from mainly eukaryotic organisms and the second class is composed of non-Zn2+-dependent (but Ni2+ or Co2+-dependent) GlxI enzymes (mainly prokaryotic and leishmanial species). GlxII is typically Zn2+-activated, containing Zn2+ and either Fe3+/Fe2+ or Mn2+ at the active site depending upon the biological source. To address whether two classes of GIxII might exist, glyoxalase II from Escherichia coli was cloned and overexpressed and characterized. Unlike E. coli GlxI, which is non-Zn2+-dependent, Zn2+ activates the E. coli GlxII enzyme, with no evidence for Ni2+ metal utilization. (c) 2006 Elsevier Inc. All rights reserved.