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dc.contributor.author
Tanner, John J.
dc.contributor.author
Boechi, Leonardo
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McCammon, J. Andrew
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Sobrado, Pablo
dc.date.available
2018-01-11T21:14:46Z
dc.date.issued
2014-10
dc.identifier.citation
Sobrado, Pablo; McCammon, J. Andrew; Boechi, Leonardo; Tanner, John J.; Structure, mechanism, and dynamics of UDP-galactopyranose mutase; Elsevier Inc; Archives of Biochemistry and Biophysics; 544; 10-2014; 128-141
dc.identifier.issn
0003-9861
dc.identifier.uri
http://hdl.handle.net/11336/33030
dc.description.abstract
The flavoenzyme UDP-galactopyranose mutase (UGM) is a key enzyme in galactofuranose biosynthesis. The enzyme catalyzes the 6-to-5 ring contraction of UDP-galactopyranose to UDP-galactofuranose. Galactofuranose is absent in humans yet is an essential component of bacterial and fungal cell walls and a cell surface virulence factor in protozoan parasites. Thus, inhibition of galactofuranose biosynthesis is a valid strategy for developing new antimicrobials. UGM is an excellent target in this effort because the product of the UGM reaction represents the first appearance of galactofuranose in the biosynthetic pathway. The UGM reaction is redox neutral, which is atypical for flavoenzymes, motivating intense examination of the chemical mechanism and structural features that tune the flavin for its unique role in catalysis. These studies show that the flavin functions as nucleophile, forming a flavin–sugar adduct that facilitates galactose-ring opening and contraction. The 3-dimensional fold is novel and conserved among all UGMs, however the larger eukaryotic enzymes have additional secondary structure elements that lead to significant differences in quaternary structure, substrate conformation, and conformational flexibility. Here we present a comprehensive review of UGM three-dimensional structure, provide an update on recent developments in understanding the mechanism of the enzyme, and summarize computational studies of active site flexibility.
dc.format
application/pdf
dc.language.iso
eng
dc.publisher
Elsevier Inc
dc.rights
info:eu-repo/semantics/openAccess
dc.rights.uri
https://creativecommons.org/licenses/by-nc-nd/2.5/ar/
dc.subject
Chagas
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Ugm
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Molecular Dynamics
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Conformational Changes
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Otras Ciencias Biológicas
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Ciencias Biológicas
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CIENCIAS NATURALES Y EXACTAS
dc.title
Structure, mechanism, and dynamics of UDP-galactopyranose mutase
dc.type
info:eu-repo/semantics/article
dc.type
info:ar-repo/semantics/artículo
dc.type
info:eu-repo/semantics/publishedVersion
dc.date.updated
2018-01-11T19:35:42Z
dc.journal.volume
544
dc.journal.pagination
128-141
dc.journal.pais
Estados Unidos
dc.description.fil
Fil: Tanner, John J.. University of Missouri; Estados Unidos
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Fil: Boechi, Leonardo. University of California at San Diego; Estados Unidos. Consejo Nacional de Investigaciones Científicas y Técnicas; Argentina
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Fil: McCammon, J. Andrew. University of California at San Diego; Estados Unidos
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Fil: Sobrado, Pablo. Virginia Tech University; Estados Unidos
dc.journal.title
Archives of Biochemistry and Biophysics
dc.relation.alternativeid
info:eu-repo/semantics/altIdentifier/doi/http://dx.doi.org/10.1016/j.abb.2013.09.017
dc.relation.alternativeid
info:eu-repo/semantics/altIdentifier/url/http://www.sciencedirect.com/science/article/pii/S0003986113003007
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