Actinonin (BioDeep_00000003875)

   

natural product Chemicals and Drugs


代谢物信息卡片


(2R)-N'-hydroxy-N-[(2S)-1-[(2S)-2-(hydroxymethyl)pyrrolidin-1-yl]-3-methyl-1-oxobutan-2-yl]-2-pentylbutanediamide

化学式: C19H35N3O5 (385.25765800000005)
中文名称: 肌动蛋白
谱图信息: 最多检出来源 Mentha canadensis(plant) 38.98%

Reviewed

Last reviewed on 2024-08-14.

Cite this Page

Actinonin. BioDeep Database v3. PANOMIX ltd, a top metabolomics service provider from China. https://query.biodeep.cn/s/actinonin (retrieved 2024-11-10) (BioDeep RN: BioDeep_00000003875). Licensed under the Attribution-Noncommercial 4.0 International License (CC BY-NC 4.0).

分子结构信息

SMILES: CCCCCC(CC(=O)NO)C(=O)NC(C(C)C)C(=O)N1CCCC1CO
InChI: InChI=1S/C19H35N3O5/c1-4-5-6-8-14(11-16(24)21-27)18(25)20-17(13(2)3)19(26)22-10-7-9-15(22)12-23/h13-15,17,23,27H,4-12H2,1-3H3,(H,20,25)(H,21,24)

描述信息

D000890 - Anti-Infective Agents > D000900 - Anti-Bacterial Agents
Actinonin ((-)-Actinonin) is a naturally occurring antibacterial agent produced by Actinomyces. Actinonin inhibits aminopeptidase M, aminopeptidase N and leucine aminopeptidase. Actinonin is a potent reversible peptide deformylase (PDF) inhibitor with a Ki of 0.28 nM. Actinonin also inhibits MMP-1, MMP-3, MMP-8, MMP-9, and hmeprin α with Ki values of 300 nM, 1,700 nM, 190 nM, 330 nM, and 20 nM, respectively. Actinonin is an apoptosis inducer. Actinonin has antiproliferative and antitumor activities[1][2][3][4][5].

同义名列表

4 个代谢物同义名

ACTINONIN; (2R)-N-hydroxy-N-[(2S)-1-[(2S)-2-(hydroxymethyl)pyrrolidin-1-yl]-3-methyl-1-oxobutan-2-yl]-2-pentylbutanediamide; 3-[[1-[(2-(Hydroxymethyl)-1-pyrrolidinyl)carbonyl]-2-methylpropyl]carbamoyl]octanohydroxamic acid; (-)-actinonin



数据库引用编号

33 个数据库交叉引用编号

分类词条

相关代谢途径

Reactome(0)

BioCyc(0)

PlantCyc(0)

代谢反应

0 个相关的代谢反应过程信息。

Reactome(0)

BioCyc(0)

WikiPathways(0)

Plant Reactome(0)

INOH(0)

PlantCyc(0)

COVID-19 Disease Map(0)

PathBank(0)

PharmGKB(0)

1 个相关的物种来源信息

在这里通过桑基图来展示出与当前的这个代谢物在我们的BioDeep知识库中具有相关联信息的其他代谢物。在这里进行关联的信息来源主要有：

  • PubMed: 来源于PubMed文献库中的文献信息，我们通过自然语言数据挖掘得到的在同一篇文献中被同时提及的相关代谢物列表，这个列表按照代谢物同时出现的文献数量降序排序，取前10个代谢物作为相关研究中关联性很高的代谢物集合展示在桑基图中。
  • NCBI Taxonomy: 通过文献数据挖掘，得到的代谢物物种来源信息关联。这个关联信息同样按照出现的次数降序排序，取前10个代谢物作为高关联度的代谢物集合展示在桑吉图上。
  • Chemical Taxonomy: 在物质分类上处于同一个分类集合中的其他代谢物
  • Chemical Reaction: 在化学反应过程中，存在为当前代谢物相关联的生化反应过程中的反应底物或者反应产物的关联代谢物信息。

点击图上的相关代谢物的名称，可以跳转到相关代谢物的信息页面。



文献列表

  • D A Chepurnova, E V Samoilova, А G Fesenko, А А Korotaeva. Reduced Expression of Extracellular Matrix Proteins in the Heart and Kidneys of Rats with Endotoxemia under the Effect of Actinonin. Bulletin of experimental biology and medicine. 2021 Apr; 170(6):744-747. doi: 10.1007/s10517-021-05146-y. [PMID: 33893962]
  • Katherine Amberg-Johnson, Sanjay B Hari, Suresh M Ganesan, Hernan A Lorenzi, Robert T Sauer, Jacquin C Niles, Ellen Yeh. Small molecule inhibition of apicomplexan FtsH1 disrupts plastid biogenesis in human pathogens. eLife. 2017 08; 6(?):. doi: 10.7554/elife.29865. [PMID: 28826494]
  • Daniel Ramsbeck, Antje Hamann, Dagmar Schlenzig, Stephan Schilling, Mirko Buchholz. First insight into structure-activity relationships of selective meprin β inhibitors. Bioorganic & medicinal chemistry letters. 2017 06; 27(11):2428-2431. doi: 10.1016/j.bmcl.2017.04.012. [PMID: 28408220]
  • Ho-Phuong-Thuy Ngo, Thien-Hoang Ho, Inho Lee, Huyen-Thi Tran, Bookyo Sur, Seunghwan Kim, Jeong-Gu Kim, Yeh-Jin Ahn, Sun-Shin Cha, Lin-Woo Kang. Crystal Structures of Peptide Deformylase from Rice Pathogen Xanthomonas oryzae pv. oryzae in Complex with Substrate Peptides, Actinonin, and Fragment Chemical Compounds. Journal of agricultural and food chemistry. 2016 Oct; 64(39):7307-7314. doi: 10.1021/acs.jafc.6b02976. [PMID: 27616570]
  • Nitin Kumar, Pablo Nakagawa, Branislava Janic, Cesar A Romero, Morel E Worou, Sumit R Monu, Edward L Peterson, Jiajiu Shaw, Frederick Valeriote, Elimelda M Ongeri, Jean-Marie V Niyitegeka, Nour-Eddine Rhaleb, Oscar A Carretero. The anti-inflammatory peptide Ac-SDKP is released from thymosin-β4 by renal meprin-α and prolyl oligopeptidase. American journal of physiology. Renal physiology. 2016 05; 310(10):F1026-34. doi: 10.1152/ajprenal.00562.2015. [PMID: 26962108]
  • Christian Herzog, Raju Marisiddaiah, Randy S Haun, Gur P Kaushal. Basement membrane protein nidogen-1 is a target of meprin β in cisplatin nephrotoxicity. Toxicology letters. 2015 Jul; 236(2):110-6. doi: 10.1016/j.toxlet.2015.05.005. [PMID: 25957482]
  • Sonia Fieulaine, Michel Desmadril, Thierry Meinnel, Carmela Giglione. Understanding the highly efficient catalysis of prokaryotic peptide deformylases by shedding light on the determinants specifying the low activity of the human counterpart. Acta crystallographica. Section D, Biological crystallography. 2014 Feb; 70(Pt 2):242-52. doi: 10.1107/s1399004713026461. [PMID: 24531459]
  • Petra Minder, Elke Bayha, Christoph Becker-Pauly, Erwin E Sterchi. Meprinα transactivates the epidermal growth factor receptor (EGFR) via ligand shedding, thereby enhancing colorectal cancer cell proliferation and migration. The Journal of biological chemistry. 2012 Oct; 287(42):35201-35211. doi: 10.1074/jbc.m112.368910. [PMID: 22923609]
  • Jonathan Pratt, René Roy, Borhane Annabi. Concanavalin-A-induced autophagy biomarkers requires membrane type-1 matrix metalloproteinase intracellular signaling in glioblastoma cells. Glycobiology. 2012 Sep; 22(9):1245-55. doi: 10.1093/glycob/cws093. [PMID: 22692046]
  • Melisande L Addison, James S Minnion, Joy C Shillito, Keisuke Suzuki, Tricia M Tan, Benjamin C T Field, Natacha Germain-Zito, Christoph Becker-Pauly, Mohammad A Ghatei, Stephen R Bloom, Kevin G Murphy. A role for metalloendopeptidases in the breakdown of the gut hormone, PYY 3-36. Endocrinology. 2011 Dec; 152(12):4630-40. doi: 10.1210/en.2011-1195. [PMID: 21952244]
  • Elimelda Moige Ongeri, Odinaka Anyanwu, W Brian Reeves, Judith S Bond. Villin and actin in the mouse kidney brush-border membrane bind to and are degraded by meprins, an interaction that contributes to injury in ischemia-reperfusion. American journal of physiology. Renal physiology. 2011 Oct; 301(4):F871-82. doi: 10.1152/ajprenal.00703.2010. [PMID: 21795642]
  • Zhen Wang, Christian Herzog, Gur P Kaushal, Neriman Gokden, Philip R Mayeux. Actinonin, a meprin A inhibitor, protects the renal microcirculation during sepsis. Shock (Augusta, Ga.). 2011 Feb; 35(2):141-7. doi: 10.1097/shk.0b013e3181ec39cc. [PMID: 20577148]
  • Agustin Garcia-Caballero, Susan S Ishmael, Yan Dang, Daniel Gillie, Judith S Bond, Sharon L Milgram, M Jackson Stutts. Activation of the epithelial sodium channel by the metalloprotease meprin β subunit. Channels (Austin, Tex.). 2011 Jan; 5(1):14-22. doi: 10.4161/chan.5.1.13759. [PMID: 20953144]
  • Pan Gao, Rui-wei Guo, Jian-fei Chen, Yang Chen, Hong Wang, Yang Yu, Lan Huang. A meprin inhibitor suppresses atherosclerotic plaque formation in ApoE-/- mice. Atherosclerosis. 2009 Nov; 207(1):84-92. doi: 10.1016/j.atherosclerosis.2009.04.036. [PMID: 19464686]
  • Christian Herzog, Randy S Haun, Varsha Kaushal, Philip R Mayeux, Sudhir V Shah, Gur P Kaushal. Meprin A and meprin alpha generate biologically functional IL-1beta from pro-IL-1beta. Biochemical and biophysical research communications. 2009 Feb; 379(4):904-8. doi: 10.1016/j.bbrc.2008.12.161. [PMID: 19135030]
  • Beatrice Oneda, Nadège Lods, Daniel Lottaz, Christoph Becker-Pauly, Walter Stöcker, Jeffrey Pippin, Maya Huguenin, Daniel Ambort, Hans-Peter Marti, Erwin E Sterchi. Metalloprotease meprin beta in rat kidney: glomerular localization and differential expression in glomerulonephritis. PloS one. 2008 May; 3(5):e2278. doi: 10.1371/journal.pone.0002278. [PMID: 18509531]
  • Maya Huguenin, Eliane J Müller, Sandra Trachsel-Rösmann, Beatrice Oneda, Daniel Ambort, Erwin E Sterchi, Daniel Lottaz. The metalloprotease meprinbeta processes E-cadherin and weakens intercellular adhesion. PloS one. 2008 May; 3(5):e2153. doi: 10.1371/journal.pone.0002153. [PMID: 18478055]
  • Hiromitsu Yoshimura, Masayoshi Ito, Yusuke Kuwahara, Aiko Ishii, Katsuki Tsuritani, Atsushi Nakamura, Yasushi Hirasawa, Tadashi Nagamatsu. Downregulated expression in high IgA (HIGA) mice and the renal protective role of meprinbeta. Life sciences. 2008 Apr; 82(15-16):899-908. doi: 10.1016/j.lfs.2008.02.006. [PMID: 18355876]
  • Junji Takayama, Masanori Takaoka, Shinya Yamamoto, Asami Nohara, Mamoru Ohkita, Yasuo Matsumura. Actinonin, a meprin inhibitor, protects ischemic acute kidney injury in male but not in female rats. European journal of pharmacology. 2008 Feb; 581(1-2):157-63. doi: 10.1016/j.ejphar.2007.11.044. [PMID: 18093581]
  • Kristin Pankow, Yong Wang, Florian Gembardt, Eberhard Krause, Xiaoou Sun, Gerd Krause, Heinz-Peter Schultheiss, Wolf-Eberhard Siems, Thomas Walther. Successive action of meprin A and neprilysin catabolizes B-type natriuretic peptide. Circulation research. 2007 Oct; 101(9):875-82. doi: 10.1161/circresaha.107.153585. [PMID: 17823376]
  • Junji Takayama, Masanori Takaoka, Yohko Sugino, Yuji Yamamoto, Mamoru Ohkita, Yasuo Matsumura. Sex difference in ischemic acute renal failure in rats: approach by proteomic analysis. Biological & pharmaceutical bulletin. 2007 Oct; 30(10):1905-12. doi: 10.1248/bpb.30.1905. [PMID: 17917260]
  • Anja Thielitz, Dirk Reinhold, Robert Vetter, Ute Bank, Martin Helmuth, Roland Hartig, Sabine Wrenger, Ingrid Wiswedel, Uwe Lendeckel, Thilo Kähne, Klaus Neubert, Jürgen Faust, Christos C Zouboulis, Siegfried Ansorge, Harald Gollnick. Inhibitors of dipeptidyl peptidase IV and aminopeptidase N target major pathogenetic steps in acne initiation. The Journal of investigative dermatology. 2007 May; 127(5):1042-51. doi: 10.1038/sj.jid.5700439. [PMID: 16778789]
  • C Herzog, R Seth, S V Shah, G P Kaushal. Role of meprin A in renal tubular epithelial cell injury. Kidney international. 2007 May; 71(10):1009-18. doi: 10.1038/sj.ki.5002189. [PMID: 17377510]
  • Cai-Xia Hou, Lynnette M A Dirk, Sitakanta Pattanaik, Narayan C Das, Indu B Maiti, Robert L Houtz, Mark A Williams. Plant peptide deformylase: a novel selectable marker and herbicide target based on essential cotranslational chloroplast protein processing. Plant biotechnology journal. 2007 Mar; 5(2):275-81. doi: 10.1111/j.1467-7652.2007.00238.x. [PMID: 17309682]
  • M K Holly, J W Dear, X Hu, A N Schechter, M T Gladwin, S M Hewitt, P S T Yuen, R A Star. Biomarker and drug-target discovery using proteomics in a new rat model of sepsis-induced acute renal failure. Kidney international. 2006 Aug; 70(3):496-506. doi: 10.1038/sj.ki.5001575. [PMID: 16760904]
  • Mona D Lee, Christophe Antczak, Yueming Li, Francis M Sirotnak, William G Bornmann, David A Scheinberg. A new human peptide deformylase inhibitable by actinonin. Biochemical and biophysical research communications. 2003 Dec; 312(2):309-15. doi: 10.1016/j.bbrc.2003.10.123. [PMID: 14637138]
  • Rory E Morty, Jennifer Morehead. Cloning and characterization of a leucyl aminopeptidase from three pathogenic Leishmania species. The Journal of biological chemistry. 2002 Jul; 277(29):26057-65. doi: 10.1074/jbc.m202779200. [PMID: 12006595]
  • Simone Carmago, Sudhir V Shah, Patrick D Walker. Meprin, a brush-border enzyme, plays an important role in hypoxic/ischemic acute renal tubular injury in rats. Kidney international. 2002 Mar; 61(3):959-66. doi: 10.1046/j.1523-1755.2002.00209.x. [PMID: 11849450]
  • A Serero, C Giglione, T Meinnel. Distinctive features of the two classes of eukaryotic peptide deformylases. Journal of molecular biology. 2001 Dec; 314(4):695-708. doi: 10.1006/jmbi.2001.5175. [PMID: 11733990]
  • L M Dirk, M A Williams, R L Houtz. Eukaryotic peptide deformylases. Nuclear-encoded and chloroplast-targeted enzymes in Arabidopsis. Plant physiology. 2001 Sep; 127(1):97-107. doi: 10.1104/pp.127.1.97. [PMID: 11553738]
  • Y Matsuda, M Katayama, I Hara, H Sato, H Tomomasa, T Iizumi, T Umeda, H Ishikawa. Inhibitors on an elastase-like enzyme activity catalyzing Suc-Ala-Ala-Pro-Leu-pNA amidolysis in human seminal plasma. Archives of andrology. 2000 Jan; 44(1):1-9. doi: 10.1080/014850100262353. [PMID: 10690759]
  • L Juillerat-Jeanneret, J D Aubert, P Leuenberger. Peptidases in human bronchoalveolar lining fluid, macrophages, and epithelial cells: dipeptidyl (amino)peptidase IV, aminopeptidase N, and dipeptidyl (carboxy)peptidase (angiotensin-converting enzyme). The Journal of laboratory and clinical medicine. 1997 Dec; 130(6):603-14. doi: 10.1016/s0022-2143(97)90110-4. [PMID: 9422334]
  • J M Bankus, J S Bond. Expression and distribution of meprin protease subunits in mouse intestine. Archives of biochemistry and biophysics. 1996 Jul; 331(1):87-94. doi: 10.1006/abbi.1996.0286. [PMID: 8660687]
  • M Shimamura, T Hazato, T Iwaguchi. Enkephalin-degrading aminopeptidase in the longitudinal muscle layer of guinea pig small intestine: its properties and action on neuropeptides. Journal of biochemistry. 1991 Mar; 109(3):492-7. doi: 10.1093/oxfordjournals.jbchem.a123409. [PMID: 1679058]
  • S Nakajima, K Kaya, T Hazato. Protection of endogenous enkephalin degradation from peptidases in human serum by actinonin. Neuropeptides. 1989 Apr; 13(3):201-6. doi: 10.1016/0143-4179(89)90093-0. [PMID: 2710293]