2''-O-succinyl-ADP-D-ribose(3-)

• 分子结构分类: 有机化合物 - 核苷、核苷酸和类似物 - 嘌呤核苷酸
• 英文名称: 2''-O-succinyl-ADP-D-ribose(3-)
• 英文别名: 4-[(3R,4R,5R)-5-[[[[(2R,3S,4R,5R)-5-(6-aminopurin-9-yl)-3,4-dihydroxyoxolan-2-yl]methoxy-oxidophosphoryl]oxy-oxidophosphoryl]oxymethyl]-2,4-dihydroxyoxolan-3-yl]oxy-4-oxobutanoate
• 化学式: C19H24N5O17P2-3
• 分子量: 656.4
• InChiKey: AKEYIRFGFICPER-DBTCLECXSA-K

计算性质

• 辛醇/水分配系数(LogP)：
  -5.7
• 重原子数：
  43
• 可旋转键数：
  13
• 环数：
  4.0
• sp3杂化的碳原子比例：
  0.63
• 拓扑面积：
  343
• 氢给体数：
  5
• 氢受体数：
  21

反应信息

• 作为产物：
  描述：

  水 、 N⁶-succinyl-L-lysine residue 、 nicotinamide adenine dinucleotide 生成 2''-O-succinyl-ADP-D-ribose(3-) 、 L-lysine residue 、 烟酰胺
  参考文献：
  名称：

  Cloning and characterization of NAD-dependent protein deacetylase (Rv1151c) from Mycobacterium tuberculosis

  摘要：

  Sir2家族蛋白高度保守，催化一种特征明确的NAD依赖性蛋白脱乙酰化反应，该反应可调节多种细胞过程，包括衰老、基因沉默、细胞分化和代谢途径。关于细菌中的Sir2家族蛋白知之甚少。结核分枝杆菌的Sir2同源物Rv1151c在大肠杆菌中被克隆并过量表达，然后通过Ni2+亲和色谱法纯化至纯度。纯化的重组蛋白显示出典型的NAD依赖性蛋白脱乙酰化酶活性，该活性可被烟酰胺和其他已知的Sir2抑制剂抑制。Rv1151c的最佳活性和pH值分别为25°C和pH 9 ± 1。Rv1151c能够对结核分枝杆菌的乙酰辅酶A合成酶进行脱乙酰化。然而，与从其他细菌中鉴定的Sir2家族蛋白不同，Rv1151c表现出一种与底物无关的NAD糖水解酶活性，这与它的自ADP核糖基化活性一致。

  DOI：

  10.1134/s0006297909070062

文献信息

• Sirt5 Is a NAD-Dependent Protein Lysine Demalonylase and Desuccinylase
  作者：Jintang Du、Yeyun Zhou、Xiaoyang Su、Jiu Jiu Yu、Saba Khan、Hong Jiang、Jungwoo Kim、Jimin Woo、Jun Huyn Kim、Brian Hyun Choi、Bin He、Wei Chen、Sheng Zhang、Richard A. Cerione、Johan Auwerx、Quan Hao、Hening Lin

  DOI：10.1126/science.1207861

  日期：2011.11.11

  Biological functions of sirtuins may involve lysine desuccinylase and demalonylase activities.

  Sirtuins的生物功能可能涉及到赖氨酸去琥珀酰基酶和去马来酰基酶的活性。
• The First Identification of Lysine Malonylation Substrates and Its Regulatory Enzyme
  作者：Chao Peng、Zhike Lu、Zhongyu Xie、Zhongyi Cheng、Yue Chen、Minjia Tan、Hao Luo、Yi Zhang、Wendy He、Ke Yang、Bernadette M.M. Zwaans、Daniel Tishkoff、Linh Ho、David Lombard、Tong-Chuan He、Junbiao Dai、Eric Verdin、Yang Ye、Yingming Zhao

  DOI：10.1074/mcp.m111.012658

  日期：2011.12

  Protein post-translational modifications (PTMs) at the lysine residue, such as lysine methylation, acetylation, and ubiquitination, are diverse, abundant, and dynamic. They play a key role in the regulation of diverse cellular physiology. Here we report discovery of a new type of lysine PTM, lysine malonylation (Kmal). Kmal was initially detected by mass spectrometry and protein sequence-database searching. The modification was comprehensively validated by Western blot, tandem MS, and high-performance liquid chromatography of synthetic peptides, isotopic labeling, and identification of multiple Kmal substrate proteins. Kmal is a dynamic and evolutionarily conserved PTM observed in mammalian cells and bacterial cells. In addition, we demonstrate that Sirt5, a member of the class III lysine deacetylases, can catalyze lysine demalonylation and lysine desuccinylation reactions both in vitro and in vivo. This result suggests the possibility of nondeacetylation activity of other class III lysine deacetylases, especially those without obvious acetylation protein substrates. Our results therefore reveal a new type of PTM pathway and identify the first enzyme that can regulate lysine malonylation and lysine succinylation status. Molecular & Cellular Proteomics 10: 10.1074/mcp.M111.012658, 1-12, 2011.