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dc.contributor.author Asención Diez, Matías Damián
dc.contributor.author Miah, Farzana
dc.contributor.author Stevenson, Clare E. M.
dc.contributor.author Lawson, David M.
dc.contributor.author Iglesias, Alberto Alvaro
dc.contributor.author Bornemann, Stephen
dc.date.available 2018-05-18T20:57:54Z
dc.date.issued 2017-01
dc.identifier.citation Asención Diez, Matías Damián; Miah, Farzana; Stevenson, Clare E. M.; Lawson, David M.; Iglesias, Alberto Alvaro; et al.; The production and utilization of GDP-glucose in the biosynthesis of trehalose-6-phosphate by Streptomyces venezuelae; American Society for Biochemistry and Molecular Biology; Journal of Biological Chemistry (online); 292; 1-2017; 945-954
dc.identifier.issn 0021-9258
dc.identifier.uri http://hdl.handle.net/11336/45674
dc.description.abstract Trehalose-6-phosphate synthase OtsA from streptomycetes is unusual in that it uses GDP-glucose as the donor substrate rather than the more commonly used UDP-glucose. We now confirm that OtsA from Streptomyces venezuelae has such a preference for GDP-glucose and can utilize ADP-glucose to some extent too. A crystal structure of the enzyme shows that it shares twin Rossmann-like domains with the UDP-glucose-specific OtsA from Escherichia coli. However, it is structurally more similar to Streptomyces hygroscopicus VldE, a GDP-valienol-dependent pseudoglycosyltransferase enzyme. Comparison of the donor binding sites reveals that the amino acids associated with the binding of diphosphoribose are almost all identical in these three enzymes. By contrast, the amino acids associated with binding guanine in VldE (Asn, Thr, and Val) are similar in S. venezuelae OtsA (Asp, Ser, and Phe, respectively) but not conserved in E. coli OtsA (His, Leu, and Asp, respectively), providing a rationale for the purine base specificity of S. venezuelae OtsA. To establish which donor is used in vivo, we generated an otsA null mutant in S. venezuelae. The mutant had a cell density-dependent growth phenotype and accumulated galactose 1-phosphate, glucose 1-phosphate, and GDP-glucose when grown on galactose. To determine how the GDP-glucose is generated, we characterized three candidate GDP-glucose pyrophosphorylases. SVEN_3027 is a UDP-glucose pyrophosphorylase, SVEN_3972 is an unusual ITP-mannose pyrophosphorylase, and SVEN_2781 is a pyrophosphorylase that is capable of generating GDP-glucose as well as GDP-mannose. We have therefore established how S. venezuelae can make and utilize GDP-glucose in the biosynthesis of trehalose 6-phosphate.
dc.format application/pdf
dc.language.iso eng
dc.publisher American Society for Biochemistry and Molecular Biology
dc.rights info:eu-repo/semantics/openAccess
dc.rights.uri https://creativecommons.org/licenses/by-nc-sa/2.5/ar/
dc.subject TREHALOSE-6P
dc.subject ACTINOBACTERIA
dc.subject GLUCOSYLTRANSFERASE
dc.subject GDP-GLUCOSE
dc.subject.classification Otras Ciencias Biológicas
dc.subject.classification Ciencias Biológicas
dc.subject.classification CIENCIAS NATURALES Y EXACTAS
dc.title The production and utilization of GDP-glucose in the biosynthesis of trehalose-6-phosphate by Streptomyces venezuelae
dc.type info:eu-repo/semantics/article
dc.type info:ar-repo/semantics/artículo
dc.type info:eu-repo/semantics/publishedVersion
dc.date.updated 2018-05-11T21:16:58Z
dc.journal.volume 292
dc.journal.pagination 945-954
dc.journal.pais Estados Unidos
dc.description.fil Fil: Asención Diez, Matías Damián. Consejo Nacional de Investigaciones Científicas y Técnicas. Centro Científico Tecnológico Conicet - Santa Fe. Instituto de Agrobiotecnología del Litoral. Universidad Nacional del Litoral. Instituto de Agrobiotecnología del Litoral; Argentina
dc.description.fil Fil: Miah, Farzana. John Innes Institute; Reino Unido
dc.description.fil Fil: Stevenson, Clare E. M.. John Innes Institute; Reino Unido
dc.description.fil Fil: Lawson, David M.. John Innes Institute; Reino Unido
dc.description.fil Fil: Iglesias, Alberto Alvaro. Consejo Nacional de Investigaciones Científicas y Técnicas. Centro Científico Tecnológico Conicet - Santa Fe. Instituto de Agrobiotecnología del Litoral. Universidad Nacional del Litoral. Instituto de Agrobiotecnología del Litoral; Argentina
dc.description.fil Fil: Bornemann, Stephen. John Innes Institute; Reino Unido
dc.journal.title Journal of Biological Chemistry (online)
dc.relation.alternativeid info:eu-repo/semantics/altIdentifier/url/http://www.jbc.org/content/292/3/945
dc.relation.alternativeid info:eu-repo/semantics/altIdentifier/doi/http://dx.doi.org/10.1074/jbc.M116.758664
dc.conicet.fuente individual


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info:eu-repo/semantics/openAccess Excepto donde se diga explícitamente, este item se publica bajo la siguiente descripción: Creative Commons Attribution-NonCommercial-ShareAlike 2.5 Unported (CC BY-NC-SA 2.5)