Molecular cloning and sequence analysis of the gene of the molybdenum‐containing aldehyde oxido‐reductase of Desulfovibrio gigas The deduced amino acid sequence shows similarity to xanthine dehydrogenase
Autor(a) principal: | |
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Data de Publicação: | 1994 |
Outros Autores: | , , , , , , , , |
Tipo de documento: | Artigo |
Idioma: | eng |
Título da fonte: | Repositório Científico de Acesso Aberto de Portugal (Repositórios Cientìficos) |
Texto Completo: | https://doi.org/10.1111/j.1432-1033.1994.tb18693.x |
Resumo: | In this report, we describe the isolation of a 4020‐bp genomic PstI fragment of Desulfovibrio gigas harboring the aldehyde oxido‐reductase gene. The aldehyde oxido‐reductase gene spans 2718 bp of genomic DNA and codes for a protein with 906 residues. The protein sequence shows an average 52% (± 1.5%) similarity to xanthine dehydrogenase from different organisms. The codon usage of the aldehyde oxidoreductase is almost identical to a calculated codon usage of the Desulfovibrio bacteria. |
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Molecular cloning and sequence analysis of the gene of the molybdenum‐containing aldehyde oxido‐reductase of Desulfovibrio gigas The deduced amino acid sequence shows similarity to xanthine dehydrogenaseBiochemistryIn this report, we describe the isolation of a 4020‐bp genomic PstI fragment of Desulfovibrio gigas harboring the aldehyde oxido‐reductase gene. The aldehyde oxido‐reductase gene spans 2718 bp of genomic DNA and codes for a protein with 906 residues. The protein sequence shows an average 52% (± 1.5%) similarity to xanthine dehydrogenase from different organisms. The codon usage of the aldehyde oxidoreductase is almost identical to a calculated codon usage of the Desulfovibrio bacteria.DQ - Departamento de QuímicaRUNThoenes, UlrichFlores, Orfeu L.Neves, AnaDevreese, Bartvan Beeumen, Jozef J.Huber, RobertRomão, Maria J.LeGall, JeanMoura, José J.G.Rodrigues‐Pousada, Claudina2019-03-19T23:24:27Z1994-01-011994-01-01T00:00:00Zinfo:eu-repo/semantics/publishedVersioninfo:eu-repo/semantics/article10application/pdfhttps://doi.org/10.1111/j.1432-1033.1994.tb18693.xeng0014-2956PURE: 12216368http://www.scopus.com/inward/record.url?scp=0028280650&partnerID=8YFLogxKhttps://doi.org/10.1111/j.1432-1033.1994.tb18693.xinfo:eu-repo/semantics/openAccessreponame:Repositório Científico de Acesso Aberto de Portugal (Repositórios Cientìficos)instname:Agência para a Sociedade do Conhecimento (UMIC) - FCT - Sociedade da Informaçãoinstacron:RCAAP2024-03-11T04:30:22Zoai:run.unl.pt:10362/63916Portal AgregadorONGhttps://www.rcaap.pt/oai/openaireopendoar:71602024-03-20T03:34:02.966896Repositório Científico de Acesso Aberto de Portugal (Repositórios Cientìficos) - Agência para a Sociedade do Conhecimento (UMIC) - FCT - Sociedade da Informaçãofalse |
dc.title.none.fl_str_mv |
Molecular cloning and sequence analysis of the gene of the molybdenum‐containing aldehyde oxido‐reductase of Desulfovibrio gigas The deduced amino acid sequence shows similarity to xanthine dehydrogenase |
title |
Molecular cloning and sequence analysis of the gene of the molybdenum‐containing aldehyde oxido‐reductase of Desulfovibrio gigas The deduced amino acid sequence shows similarity to xanthine dehydrogenase |
spellingShingle |
Molecular cloning and sequence analysis of the gene of the molybdenum‐containing aldehyde oxido‐reductase of Desulfovibrio gigas The deduced amino acid sequence shows similarity to xanthine dehydrogenase Thoenes, Ulrich Biochemistry |
title_short |
Molecular cloning and sequence analysis of the gene of the molybdenum‐containing aldehyde oxido‐reductase of Desulfovibrio gigas The deduced amino acid sequence shows similarity to xanthine dehydrogenase |
title_full |
Molecular cloning and sequence analysis of the gene of the molybdenum‐containing aldehyde oxido‐reductase of Desulfovibrio gigas The deduced amino acid sequence shows similarity to xanthine dehydrogenase |
title_fullStr |
Molecular cloning and sequence analysis of the gene of the molybdenum‐containing aldehyde oxido‐reductase of Desulfovibrio gigas The deduced amino acid sequence shows similarity to xanthine dehydrogenase |
title_full_unstemmed |
Molecular cloning and sequence analysis of the gene of the molybdenum‐containing aldehyde oxido‐reductase of Desulfovibrio gigas The deduced amino acid sequence shows similarity to xanthine dehydrogenase |
title_sort |
Molecular cloning and sequence analysis of the gene of the molybdenum‐containing aldehyde oxido‐reductase of Desulfovibrio gigas The deduced amino acid sequence shows similarity to xanthine dehydrogenase |
author |
Thoenes, Ulrich |
author_facet |
Thoenes, Ulrich Flores, Orfeu L. Neves, Ana Devreese, Bart van Beeumen, Jozef J. Huber, Robert Romão, Maria J. LeGall, Jean Moura, José J.G. Rodrigues‐Pousada, Claudina |
author_role |
author |
author2 |
Flores, Orfeu L. Neves, Ana Devreese, Bart van Beeumen, Jozef J. Huber, Robert Romão, Maria J. LeGall, Jean Moura, José J.G. Rodrigues‐Pousada, Claudina |
author2_role |
author author author author author author author author author |
dc.contributor.none.fl_str_mv |
DQ - Departamento de Química RUN |
dc.contributor.author.fl_str_mv |
Thoenes, Ulrich Flores, Orfeu L. Neves, Ana Devreese, Bart van Beeumen, Jozef J. Huber, Robert Romão, Maria J. LeGall, Jean Moura, José J.G. Rodrigues‐Pousada, Claudina |
dc.subject.por.fl_str_mv |
Biochemistry |
topic |
Biochemistry |
description |
In this report, we describe the isolation of a 4020‐bp genomic PstI fragment of Desulfovibrio gigas harboring the aldehyde oxido‐reductase gene. The aldehyde oxido‐reductase gene spans 2718 bp of genomic DNA and codes for a protein with 906 residues. The protein sequence shows an average 52% (± 1.5%) similarity to xanthine dehydrogenase from different organisms. The codon usage of the aldehyde oxidoreductase is almost identical to a calculated codon usage of the Desulfovibrio bacteria. |
publishDate |
1994 |
dc.date.none.fl_str_mv |
1994-01-01 1994-01-01T00:00:00Z 2019-03-19T23:24:27Z |
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 |
https://doi.org/10.1111/j.1432-1033.1994.tb18693.x |
url |
https://doi.org/10.1111/j.1432-1033.1994.tb18693.x |
dc.language.iso.fl_str_mv |
eng |
language |
eng |
dc.relation.none.fl_str_mv |
0014-2956 PURE: 12216368 http://www.scopus.com/inward/record.url?scp=0028280650&partnerID=8YFLogxK https://doi.org/10.1111/j.1432-1033.1994.tb18693.x |
dc.rights.driver.fl_str_mv |
info:eu-repo/semantics/openAccess |
eu_rights_str_mv |
openAccess |
dc.format.none.fl_str_mv |
10 application/pdf |
dc.source.none.fl_str_mv |
reponame:Repositório Científico de Acesso Aberto de Portugal (Repositórios Cientìficos) instname:Agência para a Sociedade do Conhecimento (UMIC) - FCT - Sociedade da Informação instacron:RCAAP |
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Agência para a Sociedade do Conhecimento (UMIC) - FCT - Sociedade da Informação |
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RCAAP |
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RCAAP |
reponame_str |
Repositório Científico de Acesso Aberto de Portugal (Repositórios Cientìficos) |
collection |
Repositório Científico de Acesso Aberto de Portugal (Repositórios Cientìficos) |
repository.name.fl_str_mv |
Repositório Científico de Acesso Aberto de Portugal (Repositórios Cientìficos) - Agência para a Sociedade do Conhecimento (UMIC) - FCT - Sociedade da Informação |
repository.mail.fl_str_mv |
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1799137962273800192 |