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dc.contributor.author
Bhayani, Jaina A.
dc.contributor.author
Hill, Benjamin L.
dc.contributor.author
Sharma, Anisha
dc.contributor.author
Iglesias, Alberto Alvaro
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dc.contributor.author
Olsen, Kenneth W.
dc.contributor.author
Ballicora, Miguel A.
dc.date.available
2020-11-23T15:17:14Z
dc.date.issued
2019-09
dc.identifier.citation
Bhayani, Jaina A.; Hill, Benjamin L.; Sharma, Anisha; Iglesias, Alberto Alvaro; Olsen, Kenneth W.; et al.; Mapping of a Regulatory Site of the Escherichia coli ADP-Glucose Pyrophosphorylase; Frontiers Media S.A.; Frontiers in Molecular Biosciences; 6; 9-2019; 1-13
dc.identifier.issn
2296-889X
dc.identifier.uri
http://hdl.handle.net/11336/118791
dc.description.abstract
The enzyme ADP-glucose pyrophosphorylase (ADP-Glc PPase) controls the biosynthesis of glycogen in bacteria and starch in plants. It is regulated by various activators in different organisms according to their metabolic characteristics. In Escherichia coli, the major allosteric activator is fructose 1,6-bisphosphate (FBP). Other potent activator analogs include 1,6-hexanediol bisphosphate (HBP) and pyridoxal 5′-phosphate (PLP). Recently, a crystal structure with FBP bound was reported (PDB ID: 5L6S). However, it is possible that the FBP site found is not directly responsible for the activation of the enzyme. We hypothesized FBP activates by binding one of its phosphate groups to another site (“P1”) in which a sulfate molecule was observed. In the E. coli enzyme, Arg40, Arg52, and Arg386 are part of this “P1” pocket and tightly complex this sulfate, which is also present in the crystal structures of ADP-Glc PPases from Agrobacterium tumefaciens and Solanum tuberosum. To test this hypothesis, we modeled alternative binding conformations of FBP, HBP, and PLP into “P1.” In addition, we performed a scanning mutagenesis of Arg residues near potential phosphate binding sites (“P1,” “P2,” “P3”). We found that Arg40 and Arg52 are essential for FBP and PLP binding and activation. In addition, mutation of Arg386 to Ala decreased the apparent affinity for the activators more than 35-fold. We propose that the activator binds at this “P1” pocket, as well as “P2.” Arg40 and Arg52 are highly conserved residues and they may be a common feature to complex the phosphate moiety of different sugar phosphate activators in the ADP-Glc PPase family.
dc.format
application/pdf
dc.language.iso
eng
dc.publisher
Frontiers Media S.A.
dc.rights
info:eu-repo/semantics/openAccess
dc.rights.uri
https://creativecommons.org/licenses/by-nc-sa/2.5/ar/
dc.subject
ALLOSTERIC REGULATION
dc.subject
ARGININE SCANNING MUTAGENESIS
dc.subject
POLYSACCHARIDE BIOSYNTHESIS
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PYRIDOXAL 5′-PHOSPHATE ACTIVATION
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SUGAR PHOSPHATE REGULATION
dc.subject.classification
Bioquímica y Biología Molecular
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dc.subject.classification
Ciencias Biológicas
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dc.subject.classification
CIENCIAS NATURALES Y EXACTAS
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dc.title
Mapping of a Regulatory Site of the Escherichia coli ADP-Glucose Pyrophosphorylase
dc.type
info:eu-repo/semantics/article
dc.type
info:ar-repo/semantics/artículo
dc.type
info:eu-repo/semantics/publishedVersion
dc.date.updated
2020-11-20T19:54:39Z
dc.journal.volume
6
dc.journal.pagination
1-13
dc.journal.pais
Suiza
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dc.journal.ciudad
Lussane
dc.description.fil
Fil: Bhayani, Jaina A.. Loyola University Of Chicago; Estados Unidos
dc.description.fil
Fil: Hill, Benjamin L.. Loyola University Of Chicago; Estados Unidos
dc.description.fil
Fil: Sharma, Anisha. Loyola University Of Chicago; Estados Unidos
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: Olsen, Kenneth W.. Loyola University Of Chicago; Estados Unidos
dc.description.fil
Fil: Ballicora, Miguel A.. Loyola University Of Chicago; Estados Unidos
dc.journal.title
Frontiers in Molecular Biosciences
dc.relation.alternativeid
info:eu-repo/semantics/altIdentifier/doi/http://dx.doi.org/10.3389/fmolb.2019.00089
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