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 (385.2577)
中文名称: 肌动蛋白
谱图信息: 最多检出来源 Mentha canadensis(plant) 17.37%

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 2024-12-22) (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

5 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; Actinonin



数据库引用编号

34 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。

亚细胞结构定位 关联基因列表
Cytoplasm 10 ANPEP, BIRC2, CASP3, EGFR, ELANE, HSF1, MME, MMP14, NPEPPS, PINK1
Endosome membrane 1 EGFR
Endoplasmic reticulum membrane 2 EGFR, FOLR1
Nucleus 8 BIRC2, CASP3, EGFR, FOLR1, HSF1, MMP14, NPEPPS, PINK1
cytosol 8 BIRC2, CASP3, ELANE, HSF1, IQCB1, MMP14, NPEPPS, PINK1
dendrite 3 ADCY8, MME, OPRM1
phagocytic vesicle 1 ELANE
trans-Golgi network 1 MME
centrosome 2 HSF1, IQCB1
nucleoplasm 3 CASP3, HSF1, IQCB1
Cell membrane 8 ADCY8, ANPEP, DPP4, EGFR, FOLR1, MME, MMP14, OPRM1
lamellipodium 1 DPP4
ruffle membrane 1 EGFR
Cell projection, axon 2 ADCY8, OPRM1
Early endosome membrane 1 EGFR
Multi-pass membrane protein 2 ADCY8, OPRM1
Synapse 4 ADCY8, MME, OPRM1, TAC1
cell junction 2 DPP4, EGFR
cell surface 5 DPP4, EGFR, ELANE, FOLR1, MME
glutamatergic synapse 3 ADCY8, CASP3, EGFR
Golgi apparatus 1 OPRM1
Golgi membrane 2 EGFR, FOLR1
growth cone 1 PINK1
lysosomal membrane 2 ANPEP, DPP4
mitochondrial inner membrane 1 PINK1
neuronal cell body 3 CASP3, MME, TAC1
presynaptic membrane 1 ADCY8
synaptic vesicle 1 MME
Cytoplasm, cytosol 2 NPEPPS, PINK1
Presynapse 1 MME
endosome 3 EGFR, FOLR1, OPRM1
plasma membrane 10 ADCY8, ANPEP, DPP4, EGFR, FOLR1, MEP1A, MME, MMP14, OPRM1, RNPEP
presynaptic active zone 1 ADCY8
Membrane 10 ADCY8, DPP4, EGFR, FOLR1, MEP1A, MME, MMP14, NPEPPS, OPRM1, PINK1
apical plasma membrane 4 ADCY8, DPP4, EGFR, FOLR1
axon 5 ADCY8, MME, OPRM1, PINK1, TAC1
basolateral plasma membrane 3 ADCY8, EGFR, FOLR1
brush border 1 MME
caveola 1 ADCY8
extracellular exosome 10 ANPEP, DPP4, ELANE, FBLN5, FOLR1, IQCB1, MEP1A, MME, NPEPPS, RNPEP
endoplasmic reticulum 2 OPRM1, PINK1
extracellular space 10 ANPEP, CXCL8, EGFR, ELANE, FBLN5, MEP1A, MMP14, NPEPPS, RNPEP, TAC1
perinuclear region of cytoplasm 3 EGFR, HSF1, PINK1
Schaffer collateral - CA1 synapse 1 ADCY8
intercellular canaliculus 1 DPP4
mitochondrion 1 PINK1
protein-containing complex 1 EGFR
postsynaptic density 2 ADCY8, CASP3
Single-pass type I membrane protein 3 EGFR, MEP1A, MMP14
Secreted 5 CXCL8, DPP4, FBLN5, FOLR1, RNPEP
extracellular region 6 CXCL8, DPP4, ELANE, FBLN5, RNPEP, TAC1
cytoplasmic side of plasma membrane 1 BIRC2
Mitochondrion outer membrane 1 PINK1
Single-pass membrane protein 2 DPP4, PINK1
mitochondrial outer membrane 1 PINK1
excitatory synapse 1 ADCY8
hippocampal mossy fiber to CA3 synapse 1 ADCY8
neuronal cell body membrane 1 ADCY8
anchoring junction 1 DPP4
photoreceptor connecting cilium 1 IQCB1
photoreceptor outer segment 1 IQCB1
Cytoplasm, cytoskeleton, microtubule organizing center, centrosome 2 HSF1, IQCB1
nuclear membrane 1 EGFR
CD40 receptor complex 1 BIRC2
external side of plasma membrane 2 ANPEP, FOLR1
Secreted, extracellular space, extracellular matrix 1 FBLN5
perikaryon 1 OPRM1
cytoplasmic vesicle 3 FOLR1, MME, MMP14
microtubule cytoskeleton 1 IQCB1
Cytoplasmic vesicle, clathrin-coated vesicle membrane 1 ADCY8
clathrin-coated vesicle membrane 1 ADCY8
Early endosome 1 MME
clathrin-coated pit 1 ADCY8
Single-pass type II membrane protein 3 ANPEP, DPP4, MME
Apical cell membrane 3 ADCY8, DPP4, FOLR1
Cytoplasm, perinuclear region 1 HSF1
Mitochondrion inner membrane 1 PINK1
heterochromatin 1 HSF1
Membrane raft 4 ADCY8, DPP4, EGFR, MME
focal adhesion 4 DPP4, EGFR, MME, MMP14
extracellular matrix 2 FBLN5, MMP14
intracellular vesicle 1 EGFR
PML body 1 HSF1
mitochondrial intermembrane space 1 PINK1
collagen-containing extracellular matrix 2 ELANE, FBLN5
secretory granule 1 ELANE
receptor complex 1 EGFR
neuron projection 1 OPRM1
cilium 1 IQCB1
chromatin 2 HSF1, PINK1
mitotic spindle 1 IQCB1
cytoskeleton 1 PINK1
Cytoplasm, cytoskeleton, microtubule organizing center, centrosome, centriole 1 IQCB1
centriole 1 IQCB1
brush border membrane 1 FOLR1
Basolateral cell membrane 2 ADCY8, FOLR1
Lipid-anchor, GPI-anchor 1 FOLR1
Cytoplasm, cytoskeleton, spindle pole 1 HSF1
intercellular bridge 1 IQCB1
Endomembrane system 1 DPP4
Membrane, caveola 1 ADCY8
Chromosome, centromere, kinetochore 1 HSF1
Nucleus, nucleoplasm 1 HSF1
Cell projection, dendrite 2 ADCY8, OPRM1
Melanosome 1 MMP14
euchromatin 1 HSF1
Presynaptic cell membrane 1 ADCY8
cell body 1 PINK1
intermediate filament cytoskeleton 1 MMP14
basal plasma membrane 1 EGFR
clathrin-coated vesicle 1 FOLR1
synaptic membrane 1 EGFR
plasma membrane raft 1 ADCY8
secretory granule membrane 2 ANPEP, MME
Golgi lumen 1 MMP14
transcription repressor complex 1 ELANE
specific granule lumen 1 ELANE
kinetochore 1 HSF1
mitotic spindle pole 1 HSF1
Cytoplasmic vesicle, clathrin-coated vesicle 1 FOLR1
XY body 1 BIRC2
endocytic vesicle 1 DPP4
transport vesicle 1 FOLR1
azurophil granule lumen 1 ELANE
Endoplasmic reticulum-Golgi intermediate compartment membrane 1 FOLR1
ER to Golgi transport vesicle membrane 1 FOLR1
clathrin-coated endocytic vesicle membrane 1 EGFR
ribonucleoprotein complex 1 HSF1
endoplasmic reticulum-Golgi intermediate compartment 1 ANPEP
protein folding chaperone complex 1 HSF1
death-inducing signaling complex 1 CASP3
Lewy body 1 PINK1
Cytoplasmic vesicle, phagosome 1 ELANE
Membrane, coated pit 1 ADCY8
astrocyte projection 1 PINK1
lamellipodium membrane 1 DPP4
multivesicular body, internal vesicle lumen 1 EGFR
Shc-EGFR complex 1 EGFR
Cell projection, lamellipodium membrane 1 DPP4
Cell projection, invadopodium membrane 1 DPP4
neuron projection terminus 1 MME
Lipid-anchor, GPI-like-anchor 1 FOLR1
[Dipeptidyl peptidase 4 soluble form]: Secreted 1 DPP4
nuclear stress granule 1 HSF1
[Isoform 12]: Cytoplasm 1 OPRM1
macropinosome 1 MMP14
meprin A complex 1 MEP1A


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]
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  • 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]
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