BENZOYLARGININE NITROANILIDE (BioDeep_00000005476)
Secondary id: BioDeep_00001871002
代谢物信息卡片
N-Benzoyl-D-arginine-4-nitroanilide
化学式: C19H22N6O4 (398.1702452)
中文名称:
谱图信息:
最多检出来源 Viridiplantae(plant) 7.34%
分子结构信息
SMILES: C1=CC=C(C=C1)C(=O)NC(CCCN=C(N)N)C(=O)NC2=CC=C(C=C2)[N+](=O)[O-]
InChI: InChI=1S/C19H22N6O4/c20-19(21)22-12-4-7-16(24-17(26)13-5-2-1-3-6-13)18(27)23-14-8-10-15(11-9-14)25(28)29/h1-3,5-6,8-11,16H,4,7,12H2,(H,23,27)(H,24,26)(H4,20,21,22)
描述信息
D019995 - Laboratory Chemicals > D007202 - Indicators and Reagents > D002863 - Chromogenic Compounds
D004396 - Coloring Agents
同义名列表
数据库引用编号
12 个数据库交叉引用编号
- ChEBI: CHEBI:15766
- KEGG: C04303
- PubChem: 440290
- PubChem: 13494
- Metlin: METLIN66158
- ChEMBL: CHEMBL1907476
- MeSH: Benzoylarginine Nitroanilide
- CAS: 26056-64-4
- CAS: 911-76-2
- PMhub: MS000018292
- PubChem: 6962
- NIKKAJI: J417.701K
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)
0 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
- Barbora Legerská, Daniela Chmelová, Miroslav Ondrejovič. TLC-Bioautography as a fast and cheap screening method for the detection of α-chymotrypsin inhibitors in crude plant extracts.
Journal of biotechnology.
2020 Apr; 313(?):11-17. doi:
10.1016/j.jbiotec.2020.02.016. [PMID: 32126268] - Chandrashekhar D Patil, Hemant P Borase, Rahul K Suryawanshi, Satish V Patil. Trypsin inactivation by latex fabricated gold nanoparticles: A new strategy towards insect control.
Enzyme and microbial technology.
2016 Oct; 92(?):18-25. doi:
10.1016/j.enzmictec.2016.06.005. [PMID: 27542740] - Wen-Hsiao Chuang, Kuo-Kau Lee, Ping-Chung Liu. Characterization of alpha-2-macroglobulin from groupers.
Fish & shellfish immunology.
2013 Aug; 35(2):389-98. doi:
10.1016/j.fsi.2013.04.050. [PMID: 23711467] - Fatemeh Saadati, Ali R Bandani. Effects of serine protease inhibitors on growth and development and digestive serine proteinases of the Sunn pest, Eurygaster integriceps.
Journal of insect science (Online).
2011; 11(?):72. doi:
10.1673/031.011.7201. [PMID: 21867440] - Marco Túlio Ribeiro Gomes, Raphael Dias Teixeira, Henrique de Assis Lopes Ribeiro, Andréia Pereira Turchetti, Caroline Furtado Junqueira, Míriam Tereza Paz Lopes, Carlos Edmundo Salas, Ronaldo Alves Pinto Nagem. Purification, crystallization and preliminary X-ray analysis of CMS1MS2: a cysteine proteinase from Carica candamarcensis latex.
Acta crystallographica. Section F, Structural biology and crystallization communications.
2008 Jun; 64(Pt 6):492-4. doi:
10.1107/s174430910801172x. [PMID: 18540057] - Ritu Tomar, Reetesh Kumar, M V Jagannadham. A stable serine protease, wrightin, from the latex of the plant Wrightia tinctoria (Roxb.) R. Br.: purification and biochemical properties.
Journal of agricultural and food chemistry.
2008 Feb; 56(4):1479-87. doi:
10.1021/jf0726536. [PMID: 18220346] - Marta Dabek, Paweł Podgurniak, Jose L Valverde Piedra, Sylwia Szymańczyk, Rafał Filip, Anna Wojtasz-Pajak, Eliza Werpachowska, Malgorzata Podgurniak, Stefan G Pierzynowski. Effect of the electrical currents generated by the intestinal smooth muscle layers on pancreatic enzyme activity: an in vitro study.
Bioelectromagnetics.
2007 May; 28(4):275-80. doi:
10.1002/bem.20263. [PMID: 17212355] - Diogo Ribeiro Demartini, Alexander Wlodawer, Célia Regina Carlini. A comparative study of the expression of serine proteinases in quiescent seeds and in developing Canavalia ensiformis plants.
Journal of experimental botany.
2007; 58(3):521-32. doi:
10.1093/jxb/erl223. [PMID: 17158110] - Barbara Lisowska-Myjak, Jan Pachecka. Trypsin and antitrypsin activities and protein concentration in serial meconium and feces of healthy newborns.
The journal of maternal-fetal & neonatal medicine : the official journal of the European Association of Perinatal Medicine, the Federation of Asia and Oceania Perinatal Societies, the International Society of Perinatal Obstetricians.
2006 Aug; 19(8):477-82. doi:
10.1080/14767050600746720. [PMID: 16966112] - A Josephrajkumar, R Chakrabarty, G Thomas. Midgut proteases of the cardamom shoot and capsule borer Conogethes punctiferalis (Lepidoptera: Pyralidae) and their interaction with aprotinin.
Bulletin of entomological research.
2006 Feb; 96(1):91-8. doi:
10.1079/ber2005403. [PMID: 16441909] - Manish Kumar Agrawal, Divya Bagchi, Suvendra Nath Bagchi. Cysteine and serine protease-mediated proteolysis in body homogenate of a zooplankter, Moina macrocopa, is inhibited by the toxic cyanobacterium, Microcystis aeruginosa PCC7806.
Comparative biochemistry and physiology. Part B, Biochemistry & molecular biology.
2005 May; 141(1):33-41. doi:
10.1016/j.cbpc.2005.01.002. [PMID: 15820132] - Bara Hieng, Kristina Ugrinović, Jelka Sustar-Vozlic, Marjetka Kidric. Different classes of proteases are involved in the response to drought of Phaseolus vulgaris L. cultivars differing in sensitivity.
Journal of plant physiology.
2004 May; 161(5):519-30. doi:
10.1078/0176-1617-00956. [PMID: 15202708] - Yu Cheng Zhu, Fanrong Zeng, Brenda Oppert. Molecular cloning of trypsin-like cDNAs and comparison of proteinase activities in the salivary glands and gut of the tarnished plant bug Lygus lineolaris (Heteroptera: Miridae).
Insect biochemistry and molecular biology.
2003 Sep; 33(9):889-99. doi:
10.1016/s0965-1748(03)00094-8. [PMID: 12915180] - G Tabouret, L Bret-Bennis, Ph Dorchies, Ph Jacquiet. Serine protease activity in excretory-secretory products of Oestrus ovis (Diptera: Oestridae) larvae.
Veterinary parasitology.
2003 Jun; 114(4):305-14. doi:
10.1016/s0304-4017(03)00157-2. [PMID: 12809756] - D R Holsberger, C D Rice, R J Thurston. Localization of a proteolytic enzyme within the efferent and deferent duct epithelial cells of the turkey (Meleagris gallopavo) using immunohistochemistry.
Biology of reproduction.
2002 Jul; 67(1):276-81. doi:
10.1095/biolreprod67.1.276. [PMID: 12080028] - Senia Johansson, Ulf Göransson, Teus Luijendijk, Anders Backlund, Per Claeson, Lars Bohlin. A neutrophil multitarget functional bioassay to detect anti-inflammatory natural products.
Journal of natural products.
2002 Jan; 65(1):32-41. doi:
10.1021/np010323o. [PMID: 11809061] - A Schlereth, D Standhardt, H P Mock, K Müntz. Stored cysteine proteinases start globulin mobilization in protein bodies of embryonic axes and cotyledons during vetch (Vicia sativa L.) seed germination.
Planta.
2001 Apr; 212(5-6):718-27. doi:
10.1007/s004250000436. [PMID: 11346945] - B Doljak, M Stegnar, U Urleb, S Kreft, A Umek, M Ciglaric, B Strukelj, T Popovic. Screening for selective thrombin inhibitors in mushrooms.
Blood coagulation & fibrinolysis : an international journal in haemostasis and thrombosis.
2001 Mar; 12(2):123-8. doi:
10.1097/00001721-200103000-00006. [PMID: 11302474] - M R Konorev. [Antibody enzymes in Helicobacter pylori-associated infection].
Zhurnal mikrobiologii, epidemiologii i immunobiologii.
2000 Jan; ?(1):75-9. doi:
NULL. [PMID: 10876902] - V R Devaraj, N H Manjunatha. Purification and characterization of a proteinase inhibitor from field bean, Dolichos lablab perpureus L.
Journal of protein chemistry.
1999 Jan; 18(1):47-54. doi:
10.1023/a:1020695315964. [PMID: 10071928] - R Das Gupta, P K Ghosh, B Bano. Characterisaton of human plasma thiol proteinase inhibitors.
Indian journal of biochemistry & biophysics.
1998 Dec; 35(6):377-81. doi:
NULL. [PMID: 10412233] - K F Dobinson, N Lecomte, G Lazarovits. Production of an extracellular trypsin-like protease by the fungal plant pathogen Verticillium dahliae.
Canadian journal of microbiology.
1997 Mar; 43(3):227-33. doi:
10.1139/m97-031. [PMID: 9090111] - A Ciereszko, K Dabrowski, S I Ochkur. Characterization of acrosin-like activity of lake sturgeon (Acipenser fulvescens) spermatozoa.
Molecular reproduction and development.
1996 Sep; 45(1):72-7. doi:
10.1002/(sici)1098-2795(199609)45:1<72::aid-mrd10>3.0.co;2-z. [PMID: 8873072] - I G Sumner, A Vaughan, R Eisenthal, R W Pickersgill, A J Owen, P W Goodenough. Kinetic analysis of papaya proteinase omega.
Biochimica et biophysica acta.
1993 Aug; 1164(3):243-51. doi:
10.1016/0167-4838(93)90255-p. [PMID: 8393709] - B B Wolf, J Vasudevan, S L Gonias. Reaction of nerve growth factor gamma and 7S nerve growth factor complex with human and murine alpha 2-macroglobulin.
Biochemistry.
1993 Feb; 32(7):1875-82. doi:
10.1021/bi00058a022. [PMID: 7679924] - R J Thurston, N Korn, D P Froman, A B Bodine. Proteolytic enzymes in seminal plasma of domestic turkey (Meleagris gallopavo).
Biology of reproduction.
1993 Feb; 48(2):393-402. doi:
10.1095/biolreprod48.2.393. [PMID: 7679933] - A S Brecher, J L Pavlock. Acetaldehyde decreases the antitryptic activity of alpha 1-proteinase inhibitor.
Alcohol (Fayetteville, N.Y.).
1992 May; 9(3):181-4. doi:
10.1016/0741-8329(92)90049-g. [PMID: 1318722] - A V Babiĭ, I Iu Sakharov, S N Pokrovskiĭ. [Effect of anticoagulants on the activity of trypsin-like proteinases in human blood plasma].
Biulleten' eksperimental'noi biologii i meditsiny.
1989 Feb; 107(2):177-9. doi:
NULL. [PMID: 2538168] - F W Sosulski, L A Minja, D A Christensen. Trypsin inhibitors and nutritive value in cereals.
Plant foods for human nutrition (Dordrecht, Netherlands).
1988; 38(1):23-34. doi:
10.1007/bf01092307. [PMID: 2852804] - K Ohta, K K Makinen, W J Loesche. Purification and characterization of an enzyme produced by Treponema denticola capable of hydrolyzing synthetic trypsin substrates.
Infection and immunity.
1986 Jul; 53(1):213-20. doi:
10.1128/iai.53.1.213-220.1986. [PMID: 3013780] - P B Armstrong, J P Quigley. Proteinase inhibitory activity released from the horseshoe crab blood cell during exocytosis.
Biochimica et biophysica acta.
1985 Mar; 827(3):453-9. doi:
10.1016/0167-4838(85)90232-8. [PMID: 2982412] - S A Steiner, F J Castellino. Kinetic mechanism for stimulation by monovalent cations of the amidase activity of the plasma protease bovine activated protein C.
Biochemistry.
1985 Jan; 24(3):609-17. doi:
10.1021/bi00324a011. [PMID: 2986681] - N R Rao, P G Bhat, T N Pattabiraman. Estimation of serum alpha 2-macroglobulin based on the esterolytic activity of bound alpha-chymotrypsin.
Biochemical medicine.
1984 Dec; 32(3):357-63. doi:
10.1016/0006-2944(84)90042-5. [PMID: 6083782] - F Yoshimura, M Nishikata, T Suzuki, C I Hoover, E Newbrun. Characterization of a trypsin-like protease from the bacterium Bacteroides gingivalis isolated from human dental plaque.
Archives of oral biology.
1984; 29(7):559-64. doi:
10.1016/0003-9969(84)90078-5. [PMID: 6089721] - J H Eckfeldt, R T Light, C Leiendecker-Foster. Automated assay for alpha 1-antitrypsin with N-alpha-benzoyl-DL-arginine-p-nitroanilide as trypsin substrate and standardized with p-nitrophenyl-p'-guanidinobenzoate as titrant for trypsin active sites.
Clinical chemistry.
1982 May; 28(5):1108-12. doi:
10.1093/clinchem/28.5.1108. [PMID: 6280895] - K J Johnson, J Varani. Substrate hydrolysis by immune complex-activated neutrophils: effect of physical presentation of complexes and protease inhibitors.
Journal of immunology (Baltimore, Md. : 1950).
1981 Nov; 127(5):1875-9. doi:
NULL. [PMID: 6170676] - A Ito, K Kitamura, S Hirakawa, Y Mori. An alkaline metallo-proteinase in the human uterine cervix an changes in its activity by cervical ripening.
Biochimica et biophysica acta.
1981 Oct; 661(2):267-73. doi:
10.1016/0005-2744(81)90014-0. [PMID: 6271220] - H Steinhart, R Wieninger-Rustemeyer, M Kirchgessner. [Effect of Cu++ ions on the activity of trypsin on natural substance].
Archiv fur Tierernahrung.
1981 Feb; 31(2):119-25. doi:
10.1080/17450398109434327. [PMID: 6263218] - D Vercaigne, C Morcamp, J P Martin, J P Joly, B Hillemand, J P Raoult. 'Tryptic-like' activity in sera of patients with pancreatitis.
Clinica chimica acta; international journal of clinical chemistry.
1980 Oct; 106(3):269-77. doi:
10.1016/0009-8981(80)90310-1. [PMID: 6251987] - Ia E Dunaevskiĭ, M A Belozerskiĭ. [Changes in activity of proteolytic enzymes (BAPAases) in germinating buckwheat and rye seeds].
Biokhimiia (Moscow, Russia).
1980 May; 45(5):908-11. doi:
". [PMID: 6155154] - A Kaga. [Influence of food browning on nutrition. IV. Effect on trypsin action on a synthetic substrate (author's transl)].
[Hokkaido igaku zasshi] The Hokkaido journal of medical science.
1980 Jan; 55(1):41-5. doi:
". [PMID: 6250958] - D A Grant, J Hermon-Taylor. Hydrolysis of artificial substrates by enterokinase and trypsin and the development of a sensitive specific assay for enterokinase in serum.
Biochimica et biophysica acta.
1979 Mar; 567(1):207-15. doi:
10.1016/0005-2744(79)90187-6. [PMID: 454624] - B Urbanek-Karłowska, M Fonberg-Broczek. [Determination of soybean trypsin inhibitors in textured soybean proteins].
Roczniki Panstwowego Zakladu Higieny.
1979; 30(4):377-81. doi:
". [PMID: 574661] - V A Protsenko, V Z Kharchenko, V F Veselov, I F Spitsyn, I V Bogadel'nikov. [Effect of proteolysis inhibitors on serum proteinase activity and its antitryptic activity in postischemic toxemia].
Farmakologiia i toksikologiia.
1978 Nov; 41(6):693-6. doi:
NULL. [PMID: 720581] - C S Sundaresh, A R Aroor, T N Pattabiraman. Comparative study of the amidolytic and caseinolytic methods for the determination of urinary trypsin inhibitor.
The Indian journal of medical research.
1978 Aug; 68(?):341-7. doi:
NULL. [PMID: 721207] - C Kluft. Determination of prekallikrein in human plasma: optimal conditions for activating prekallikrein.
The Journal of laboratory and clinical medicine.
1978 Jan; 91(1):83-95. doi:
NULL. [PMID: 618993] - J R Crossley, C C Berryman, R B Elliott. Cystic-fibrosis screening in the newborn.
Lancet (London, England).
1977 Nov; 2(8048):1093-5. doi:
10.1016/s0140-6736(77)90543-8. [PMID: 73007] - C H Konings. Measurement of antitryptic activity of serum with a centrifugal analyzer.
Clinical chemistry.
1977 Sep; 23(9):1760-3. doi:
10.1093/clinchem/23.9.1760. [PMID: 302161] - I B Emtseva, M A Belozerskiĭ. [Benzoyl-DL-arginine-p-nitroanilidase from buckwheat seeds. Properties and substrate specificity].
Biokhimiia (Moscow, Russia).
1977 Apr; 42(4):726-34. doi:
. [PMID: 870091] - O D Ratnoff, H Saito. Evidence that Fitzgerald factor counteracts inhibition by kaolin or ellagic acid of the amidolytic properties of a plasma kallikrein.
Blood.
1976 Feb; 47(2):243-51. doi:
. [PMID: 1244922] - J E Fräki, V K Hopsu-Havu. Human skin proteases: separation and characterization of two alkaline proteases, one splitting trypsin and the other chymotrypsin substrates.
Archives for dermatological research = Archiv fur dermatologische Forschung.
1975 Oct; 253(3):261-76. doi:
10.1007/bf00561152. [PMID: 1200704] - O R Odegård, U Abildgaard. Proceedings: Coagulation inhibitors in plasma and serum.
Thrombosis et diathesis haemorrhagica.
1975 Sep; 34(1):346. doi:
NULL. [PMID: 1188790] - U Miyatani, J Takahata, I Fukui. [Studies on the determination of human serum trypsin protein esterase activity (author's transl)].
Rinsho byori. The Japanese journal of clinical pathology.
1975 Jun; 23(6):423-6. doi:
NULL. [PMID: 1237002] - D C Egberg, R H Potter, G R Honold. The semiautomated determination of trypsin inhibitors in textured soy protein.
Journal of agricultural and food chemistry.
1975 May; 23(3):603-5. doi:
10.1021/jf60199a042. [PMID: 1171133]