N-Succinyl-ala-ala-pro-phe-p-nitroanilide (BioDeep_00000175142)

   

human metabolite blood metabolite


代谢物信息卡片


3-{[1-({1-[2-({1-[(4-nitrophenyl)carbamoyl]-2-phenylethyl}carbamoyl)pyrrolidin-1-yl]-1-oxopropan-2-yl}carbamoyl)ethyl]carbamoyl}propanoic acid

化学式: C30H36N6O9 (624.2543646)
中文名称:
谱图信息: 最多检出来源 () 0%

分子结构信息

SMILES: CC(C(=O)NC(C)C(=O)N1CCCC1C(=O)NC(CC2=CC=CC=C2)C(=O)NC3=CC=C(C=C3)[N+](=O)[O-])NC(=O)CCC(=O)O
InChI: InChI=1S/C30H36N6O9/c1-18(31-25(37)14-15-26(38)39)27(40)32-19(2)30(43)35-16-6-9-24(35)29(42)34-23(17-20-7-4-3-5-8-20)28(41)33-21-10-12-22(13-11-21)36(44)45/h3-5,7-8,10-13,18-19,23-24H,6,9,14-17H2,1-2H3,(H,31,37)(H,32,40)(H,33,41)(H,34,42)(H,38,39)

描述信息

同义名列表

8 个代谢物同义名

3-{[1-({1-[2-({1-[(4-nitrophenyl)carbamoyl]-2-phenylethyl}carbamoyl)pyrrolidin-1-yl]-1-oxopropan-2-yl}carbamoyl)ethyl]carbamoyl}propanoic acid; Succinyl-alanyl-alanyl-prolyl-phenylalanine-4-nitroanilide; Succinyl-alanyl-alanyl-prolyl-phenylalanine-p-nitroanilide; N-Succinyl-ala-ala-pro-phe-p-nitroanilide; Suc-ala-ala-pro-phe-4-na; Suc-aapf-pna; Cathepsin G; SAAPPNA



数据库引用编号

4 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

  • Satoru Yui. [Unintended Observations Leading to Macrophage Growth and Neutrophil Factor Research]. Yakugaku zasshi : Journal of the Pharmaceutical Society of Japan. 2022; 142(3):229-239. doi: 10.1248/yakushi.21-00191. [PMID: 35228378]
  • Shiyuan Zhang, Nannan Li, Weili Chen, Qiang Fu, Yi Liu. Time Series Gene Expression Profiles Analysis Identified Several Potential Biomarkers for Sepsis. DNA and cell biology. 2020 Oct; 39(10):1862-1871. doi: 10.1089/dna.2020.5383. [PMID: 32845709]
  • Andreas Koeberle, Arne Henkel, Moritz Verhoff, Lars Tausch, Stefanie König, Dagmar Fischer, Nicole Kather, Stefanie Seitz, Michael Paul, Johann Jauch, Oliver Werz. Triterpene Acids from Frankincense and Semi-Synthetic Derivatives That Inhibit 5-Lipoxygenase and Cathepsin G. Molecules (Basel, Switzerland). 2018 Feb; 23(2):. doi: 10.3390/molecules23020506. [PMID: 29495286]
  • Takuma Matsuoka, Takuji Kawashima, Tadashi Nakamura, Tomio Yabe. Characterization and comparison of recombinant honeybee chymotrypsin-like protease (HCLPase) expressed in Escherichia coli and insect cells. Bioscience, biotechnology, and biochemistry. 2017 Jul; 81(7):1401-1404. doi: 10.1080/09168451.2017.1318698. [PMID: 28463596]
  • Natsuko Nakayama, Saki Yamaguchi, Yuta Sasaki, Toshiyuki Chikuma. Hydrogen Peroxide-Induced Oxidative Stress Activates Proteasomal Trypsin-Like Activity in Human U373 Glioma Cells. Journal of molecular neuroscience : MN. 2016 Feb; 58(2):297-305. doi: 10.1007/s12031-015-0680-9. [PMID: 26563451]
  • Ilana Cruz-Silva, Viviane Abreu Nunes, Andrezza Justino Gozzo, Priscila Praxedes-Garcia, Aparecida Sadae Tanaka, Kazuaki Shimamoto, Mariana Silva Araujo. Protease Inhibitors Extracted from Caesalpinia echinata Lam. Affect Kinin Release during Lung Inflammation. Pulmonary medicine. 2016; 2016(?):9425807. doi: 10.1155/2016/9425807. [PMID: 28044105]
  • Hsiang-Ruei Liao, Ching-Ru Chien, Jih-Jung Chen, Tzung-Yan Lee, Shinn-Zhi Lin, Ching-Ping Tseng. The anti-inflammatory effect of 2-(4-hydroxy-3-prop-2-enyl-phenyl)-4-prop-2-enyl-phenol by targeting Lyn kinase in human neutrophils. Chemico-biological interactions. 2015 Jul; 236(?):90-101. doi: 10.1016/j.cbi.2015.05.004. [PMID: 25980585]
  • Naimeh Rafatian, Ross W Milne, Frans H H Leenen, Stewart C Whitman. Role of renin-angiotensin system in activation of macrophages by modified lipoproteins. American journal of physiology. Heart and circulatory physiology. 2013 Nov; 305(9):H1309-20. doi: 10.1152/ajpheart.00826.2012. [PMID: 23997101]
  • Martin Lappann, Sophia Danhof, Frank Guenther, Silvana Olivares-Florez, Ines Louise Mordhorst, Ulrich Vogel. In vitro resistance mechanisms of Neisseria meningitidis against neutrophil extracellular traps. Molecular microbiology. 2013 Aug; 89(3):433-49. doi: 10.1111/mmi.12288. [PMID: 23750848]
  • Carsten Skarke, Karina Kuczka, Lars Tausch, Oliver Werz, Tanja Rossmanith, Jeffrey S Barrett, Sebastian Harder, Wolfgang Holtmeier, Joachim A Schwarz. Increased bioavailability of 11-keto-β-boswellic acid following single oral dose frankincense extract administration after a standardized meal in healthy male volunteers: modeling and simulation considerations for evaluating drug exposures. Journal of clinical pharmacology. 2012 Oct; 52(10):1592-600. doi: 10.1177/0091270011422811. [PMID: 22167571]
  • A Augustyniak, A Bylińska, E Skrzydlewska. Age-dependent changes in the proteolytic-antiproteolytic balance after alcohol and black tea consumption. Toxicology mechanisms and methods. 2011 Mar; 21(3):209-15. doi: 10.3109/15376516.2010.543189. [PMID: 21329467]
  • David F Houston, David J Timson. Interaction of prothrombin with a phospholipid surface: evidence for a membrane-induced conformational change. Molecular and cellular biochemistry. 2011 Feb; 348(1-2):109-15. doi: 10.1007/s11010-010-0644-x. [PMID: 21080035]
  • Yukihiro Tsuchiya, Go Okada, Shigeki Kobayashi, Toshiyuki Chikuma, Hiroshi Hojo. 4-hydroxy-2-nonenal-modified glyceraldehyde-3-phosphate dehydrogenase is degraded by cathepsin G in rat neutrophils. Oxidative medicine and cellular longevity. 2011; 2011(?):213686. doi: 10.1155/2011/213686. [PMID: 21904640]
  • C Oliveira, R A Navarro-Xavier, E A Anjos-Vallota, J O Martins, V L F Silveira, L R C Gonçalves, M S Araújo, G Motta, P Sannomiya, M L V Oliva. Effect of plant neutrophil elastase inhibitor on leucocyte migration, adhesion and cytokine release in inflammatory conditions. British journal of pharmacology. 2010 Oct; 161(4):899-910. doi: 10.1111/j.1476-5381.2010.00924.x. [PMID: 20860667]
  • Lars Tausch, Arne Henkel, Ulf Siemoneit, Daniel Poeckel, Nicole Kather, Lutz Franke, Bettina Hofmann, Gisbert Schneider, Carlo Angioni, Gerd Geisslinger, Carsten Skarke, Wolfgang Holtmeier, Tobias Beckhaus, Michael Karas, Johann Jauch, Oliver Werz. Identification of human cathepsin G as a functional target of boswellic acids from the anti-inflammatory remedy frankincense. Journal of immunology (Baltimore, Md. : 1950). 2009 Sep; 183(5):3433-42. doi: 10.4049/jimmunol.0803574. [PMID: 19648270]
  • Claude Rispe, Mayako Kutsukake, Vincent Doublet, Sylvie Hudaverdian, Fabrice Legeai, Jean-Christophe Simon, Denis Tagu, Takema Fukatsu. Large gene family expansion and variable selective pressures for cathepsin B in aphids. Molecular biology and evolution. 2008 Jan; 25(1):5-17. doi: 10.1093/molbev/msm222. [PMID: 17934209]
  • Yukihiro Tsuchiya, Yasutaka Okuno, Kayoko Hishinuma, Asami Ezaki, Go Okada, Mitsune Yamaguchi, Toshiyuki Chikuma, Hiroshi Hojo. 4-Hydroxy-2-nonenal-modified glyceraldehyde-3-phosphate dehydrogenase is degraded by cathepsin G. Free radical biology & medicine. 2007 Dec; 43(12):1604-15. doi: 10.1016/j.freeradbiomed.2007.08.024. [PMID: 18037126]
  • Kenji Mitsudo, Arumugam Jayakumar, Ying Henderson, Mitchell J Frederick, Ya'an Kang, Mary Wang, Adel K El-Naggar, Gary L Clayman. Inhibition of serine proteinases plasmin, trypsin, subtilisin A, cathepsin G, and elastase by LEKTI: a kinetic analysis. Biochemistry. 2003 Apr; 42(13):3874-81. doi: 10.1021/bi027029v. [PMID: 12667078]
  • E Skrzydewska, A Stankiewicz, K Michalak, M Sulkowska, B Zalewski, Z Piotrowski. Antioxidant status and proteolytic-antiproteolytic balance in colorectal cancer. Folia histochemica et cytobiologica. 2001; 39 Suppl 2(?):98-9. doi: NULL. [PMID: 11820646]
  • T Cierpicki, J Bania, J Otlewski. NMR solution structure of Apis mellifera chymotrypsin/cathepsin G inhibitor-1 (AMCI-1): structural similarity with Ascaris protease inhibitors. Protein science : a publication of the Protein Society. 2000 May; 9(5):976-84. doi: 10.1110/ps.9.5.976. [PMID: 10850807]
  • J Polanowska, I Krokoszynska, H Czapinska, W Watorek, M Dadlez, J Otlewski. Specificity of human cathepsin G. Biochimica et biophysica acta. 1998 Jul; 1386(1):189-98. doi: 10.1016/s0167-4838(98)00085-5. [PMID: 9675278]
  • M Sulkowska, S Sulkowski. Endogenous lipid pneumonia- and alveolar proteinosis-type changes in the vicinity of non-small cell lung cancer: histiopathologic, immunohistochemical, and ultrastructural evaluation. Ultrastructural pathology. 1998 Mar; 22(2):109-19. doi: 10.3109/01913129809032265. [PMID: 9615379]
  • S W Dahl, S K Rasmussen, J Hejgaard. Heterologous expression of three plant serpins with distinct inhibitory specificities. The Journal of biological chemistry. 1996 Oct; 271(41):25083-8. doi: 10.1074/jbc.271.41.25083. [PMID: 8810262]
  • D J Kusner, J N Aucott, D Franceschi, M M Sarasua, P J Spagnuolo, C H King. Protease priming of neutrophil superoxide production. Effects on membrane lipid order and lateral mobility. The Journal of biological chemistry. 1991 Sep; 266(25):16465-71. doi: 10.1016/s0021-9258(18)55323-0. [PMID: 1653237]
  • P Kaspar, G Möller, A Wahlefeld. New photometric assay for chymotrypsin in stool. Clinical chemistry. 1984 Nov; 30(11):1753-7. doi: NULL. [PMID: 6548423]
  • G D Virca, G Metz, H P Schnebli. Similarities between human and rat leukocyte elastase and cathepsin G. European journal of biochemistry. 1984 Oct; 144(1):1-9. doi: 10.1111/j.1432-1033.1984.tb08423.x. [PMID: 6566611]
  • Y Hojima, J J Pisano, C G Cochrane. Survey of plant inhibitors of polymorphonuclear leukocyte elastase, pancreatic elastase, cathepsin G, cathepsin B, Hageman factor fragments, and other serine proteinases. Biochemical pharmacology. 1983 Mar; 32(6):985-90. doi: 10.1016/0006-2952(83)90615-9. [PMID: 6340694]