Enzymatic toxins from snake venom: structural characterization and mechanism of catalysis

Detalhes bibliográficos
Autor(a) principal: Kang, Tse Siang
Data de Publicação: 2011
Outros Autores: Georgieva, Dessislava, Genov, Nikolay, Murakami, Mario T., Sinha, Mau, Kumar, Ramasamy P., Kaur, Punit, Kumar, Sanjit, Dey, Sharmistha, Sharma, Sujata, Vrielink, Alice, Betzel, Christian, Takeda, Soichi, Arni, Raghuvir K. [UNESP], Singh, Tej P., Kini, R. Manjunatha
Tipo de documento: Artigo
Idioma: eng
Título da fonte: Repositório Institucional da UNESP
Texto Completo: http://dx.doi.org/10.1111/j.1742-4658.2011.08115.x
http://hdl.handle.net/11449/22039
Resumo: Snake venoms are cocktails of enzymes and non-enzymatic proteins used for both the immobilization and digestion of prey. The most common snake venom enzymes include acetylcholinesterases, l-amino acid oxidases, serine proteinases, metalloproteinases and phospholipases A2. Higher catalytic efficiency, thermal stability and resistance to proteolysis make these enzymes attractive models for biochemists, enzymologists and structural biologists. Here, we review the structures of these enzymes and describe their structure-based mechanisms of catalysis and inhibition. Some of the enzymes exist as protein complexes in the venom. Thus we also discuss the functional role of non-enzymatic subunits and the pharmacological effects of such protein complexes. The structures of inhibitorenzyme complexes provide ideal platforms for the design of potent inhibitors which are useful in the development of prototypes and lead compounds with potential therapeutic applications.
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spelling Enzymatic toxins from snake venom: structural characterization and mechanism of catalysisAcetylcholinesterasel-amino acid oxidasemetalloproteinasephospholipase A2Serine proteinaseSnake venoms are cocktails of enzymes and non-enzymatic proteins used for both the immobilization and digestion of prey. The most common snake venom enzymes include acetylcholinesterases, l-amino acid oxidases, serine proteinases, metalloproteinases and phospholipases A2. Higher catalytic efficiency, thermal stability and resistance to proteolysis make these enzymes attractive models for biochemists, enzymologists and structural biologists. Here, we review the structures of these enzymes and describe their structure-based mechanisms of catalysis and inhibition. Some of the enzymes exist as protein complexes in the venom. Thus we also discuss the functional role of non-enzymatic subunits and the pharmacological effects of such protein complexes. The structures of inhibitorenzyme complexes provide ideal platforms for the design of potent inhibitors which are useful in the development of prototypes and lead compounds with potential therapeutic applications.Deutsche Forschungsgemeinschaft (DFG)Bulgarian National Foundation for Scientific ResearchDepartment of Science and Technology (Ministry of Science and Technology, New Delhi, India)Department of Biotechnology, Ministry of Science and Technology, New DelhiFundação de Amparo à Pesquisa do Estado de São Paulo (FAPESP)Conselho Nacional de Desenvolvimento Científico e Tecnológico (CNPq)Coordenação de Aperfeiçoamento de Pessoal de Nível Superior (CAPES)Natl Univ Singapore, Prot Sci Lab, Dept Biol Sci, Singapore 117543, SingaporeNatl Univ Singapore, Dept Pharm, Singapore 117543, SingaporeUniv Hamburg, Inst Biochem & Mol Biol, Lab Struct Biol Infect & Inflammat, Hamburg, GermanyBulgarian Acad Sci, Inst Organ Chem, Sofia, BulgariaNatl Ctr Res Energy & Mat, Natl Lab Biosci, Campinas, SP, BrazilAll India Inst Med Sci, Dept Biophys, New Delhi 110029, IndiaUniv Western Australia, Sch Biomed Biomol & Chem Sci, Crawley, WA, AustraliaNatl Cerebral & Cardiovasc Ctr, Res Inst, Suita, Osaka, JapanSão Paulo State Univ, Ctr Multiusuario Inovacao Biomol, Dept Phys, Sao Jose do Rio Preto, BrazilSão Paulo State Univ, Ctr Multiusuario Inovacao Biomol, Dept Phys, Sao Jose do Rio Preto, BrazilDFG: BE 1443/18-1DFG: BE 1443/23-1Bulgarian National Foundation for Scientific Research: TK-B 1610/06Wiley-BlackwellNatl Univ SingaporeUniv HamburgBulgarian Acad SciNatl Ctr Res Energy & MatAll India Inst Med SciUniv Western AustraliaNatl Cerebral & Cardiovasc CtrUniversidade Estadual Paulista (Unesp)Kang, Tse SiangGeorgieva, DessislavaGenov, NikolayMurakami, Mario T.Sinha, MauKumar, Ramasamy P.Kaur, PunitKumar, SanjitDey, SharmisthaSharma, SujataVrielink, AliceBetzel, ChristianTakeda, SoichiArni, Raghuvir K. [UNESP]Singh, Tej P.Kini, R. Manjunatha2014-05-20T14:02:31Z2014-05-20T14:02:31Z2011-12-01info:eu-repo/semantics/publishedVersioninfo:eu-repo/semantics/article4544-4576http://dx.doi.org/10.1111/j.1742-4658.2011.08115.xFebs Journal. Malden: Wiley-blackwell, v. 278, n. 23, p. 4544-4576, 2011.1742-464Xhttp://hdl.handle.net/11449/2203910.1111/j.1742-4658.2011.08115.xWOS:00029715590000991625089789458870000-0003-2460-1145Web of Sciencereponame:Repositório Institucional da UNESPinstname:Universidade Estadual Paulista (UNESP)instacron:UNESPengFEBS Journal4.530info:eu-repo/semantics/openAccess2021-10-22T18:21:05Zoai:repositorio.unesp.br:11449/22039Repositório InstitucionalPUBhttp://repositorio.unesp.br/oai/requestopendoar:29462024-08-05T17:03:51.051111Repositório Institucional da UNESP - Universidade Estadual Paulista (UNESP)false
dc.title.none.fl_str_mv Enzymatic toxins from snake venom: structural characterization and mechanism of catalysis
title Enzymatic toxins from snake venom: structural characterization and mechanism of catalysis
spellingShingle Enzymatic toxins from snake venom: structural characterization and mechanism of catalysis
Kang, Tse Siang
Acetylcholinesterase
l-amino acid oxidase
metalloproteinase
phospholipase A2
Serine proteinase
title_short Enzymatic toxins from snake venom: structural characterization and mechanism of catalysis
title_full Enzymatic toxins from snake venom: structural characterization and mechanism of catalysis
title_fullStr Enzymatic toxins from snake venom: structural characterization and mechanism of catalysis
title_full_unstemmed Enzymatic toxins from snake venom: structural characterization and mechanism of catalysis
title_sort Enzymatic toxins from snake venom: structural characterization and mechanism of catalysis
author Kang, Tse Siang
author_facet Kang, Tse Siang
Georgieva, Dessislava
Genov, Nikolay
Murakami, Mario T.
Sinha, Mau
Kumar, Ramasamy P.
Kaur, Punit
Kumar, Sanjit
Dey, Sharmistha
Sharma, Sujata
Vrielink, Alice
Betzel, Christian
Takeda, Soichi
Arni, Raghuvir K. [UNESP]
Singh, Tej P.
Kini, R. Manjunatha
author_role author
author2 Georgieva, Dessislava
Genov, Nikolay
Murakami, Mario T.
Sinha, Mau
Kumar, Ramasamy P.
Kaur, Punit
Kumar, Sanjit
Dey, Sharmistha
Sharma, Sujata
Vrielink, Alice
Betzel, Christian
Takeda, Soichi
Arni, Raghuvir K. [UNESP]
Singh, Tej P.
Kini, R. Manjunatha
author2_role author
author
author
author
author
author
author
author
author
author
author
author
author
author
author
dc.contributor.none.fl_str_mv Natl Univ Singapore
Univ Hamburg
Bulgarian Acad Sci
Natl Ctr Res Energy & Mat
All India Inst Med Sci
Univ Western Australia
Natl Cerebral & Cardiovasc Ctr
Universidade Estadual Paulista (Unesp)
dc.contributor.author.fl_str_mv Kang, Tse Siang
Georgieva, Dessislava
Genov, Nikolay
Murakami, Mario T.
Sinha, Mau
Kumar, Ramasamy P.
Kaur, Punit
Kumar, Sanjit
Dey, Sharmistha
Sharma, Sujata
Vrielink, Alice
Betzel, Christian
Takeda, Soichi
Arni, Raghuvir K. [UNESP]
Singh, Tej P.
Kini, R. Manjunatha
dc.subject.por.fl_str_mv Acetylcholinesterase
l-amino acid oxidase
metalloproteinase
phospholipase A2
Serine proteinase
topic Acetylcholinesterase
l-amino acid oxidase
metalloproteinase
phospholipase A2
Serine proteinase
description Snake venoms are cocktails of enzymes and non-enzymatic proteins used for both the immobilization and digestion of prey. The most common snake venom enzymes include acetylcholinesterases, l-amino acid oxidases, serine proteinases, metalloproteinases and phospholipases A2. Higher catalytic efficiency, thermal stability and resistance to proteolysis make these enzymes attractive models for biochemists, enzymologists and structural biologists. Here, we review the structures of these enzymes and describe their structure-based mechanisms of catalysis and inhibition. Some of the enzymes exist as protein complexes in the venom. Thus we also discuss the functional role of non-enzymatic subunits and the pharmacological effects of such protein complexes. The structures of inhibitorenzyme complexes provide ideal platforms for the design of potent inhibitors which are useful in the development of prototypes and lead compounds with potential therapeutic applications.
publishDate 2011
dc.date.none.fl_str_mv 2011-12-01
2014-05-20T14:02:31Z
2014-05-20T14:02:31Z
dc.type.status.fl_str_mv info:eu-repo/semantics/publishedVersion
dc.type.driver.fl_str_mv info:eu-repo/semantics/article
format article
status_str publishedVersion
dc.identifier.uri.fl_str_mv http://dx.doi.org/10.1111/j.1742-4658.2011.08115.x
Febs Journal. Malden: Wiley-blackwell, v. 278, n. 23, p. 4544-4576, 2011.
1742-464X
http://hdl.handle.net/11449/22039
10.1111/j.1742-4658.2011.08115.x
WOS:000297155900009
9162508978945887
0000-0003-2460-1145
url http://dx.doi.org/10.1111/j.1742-4658.2011.08115.x
http://hdl.handle.net/11449/22039
identifier_str_mv Febs Journal. Malden: Wiley-blackwell, v. 278, n. 23, p. 4544-4576, 2011.
1742-464X
10.1111/j.1742-4658.2011.08115.x
WOS:000297155900009
9162508978945887
0000-0003-2460-1145
dc.language.iso.fl_str_mv eng
language eng
dc.relation.none.fl_str_mv FEBS Journal
4.530
dc.rights.driver.fl_str_mv info:eu-repo/semantics/openAccess
eu_rights_str_mv openAccess
dc.format.none.fl_str_mv 4544-4576
dc.publisher.none.fl_str_mv Wiley-Blackwell
publisher.none.fl_str_mv Wiley-Blackwell
dc.source.none.fl_str_mv Web of Science
reponame:Repositório Institucional da UNESP
instname:Universidade Estadual Paulista (UNESP)
instacron:UNESP
instname_str Universidade Estadual Paulista (UNESP)
instacron_str UNESP
institution UNESP
reponame_str Repositório Institucional da UNESP
collection Repositório Institucional da UNESP
repository.name.fl_str_mv Repositório Institucional da UNESP - Universidade Estadual Paulista (UNESP)
repository.mail.fl_str_mv
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