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dc.contributor.author
Laino, Aldana
dc.contributor.author
Lopez Zavala, Alonso A.
dc.contributor.author
Garcia, Carlos Fernando
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Carrasco Miranda, Jesus S.
dc.contributor.author
Santana, Marianela
dc.contributor.author
Stojanoff, Vivian
dc.contributor.author
Sotelo Mundo, Rogerio Rafael
dc.contributor.author
Garcia, Carlos Fernando
dc.date.available
2018-07-10T21:11:19Z
dc.date.issued
2017-12
dc.identifier.citation
Laino, Aldana; Lopez Zavala, Alonso A.; Garcia, Carlos Fernando; Carrasco Miranda, Jesus S.; Santana, Marianela; et al.; Biochemical and structural characterization of a novel arginine kinase from the spider Polybetes pythagoricus; PeerJ Inc.; PeerJ; 2017; 9; 12-2017; 1-19
dc.identifier.issn
2167-8359
dc.identifier.uri
http://hdl.handle.net/11336/51679
dc.description.abstract
Energy buffering systems are key for homeostasis during variations in energy supply. Spiders are the most important predators for insects and therefore key in terrestrial ecosystems. From biomedical interest, spiders are important for their venoms and as a source of potent allergens, such as arginine kinase (AK, EC 2.7.3.3). AK is an enzyme crucial for energy metabolism, keeping the pool of phosphagens in invertebrates, and also an allergen for humans. In this work, we studied AK from the Argentininan spider Polybetes pythagoricus (PpAK), from its complementary DNA to the crystal structure. The PpAK cDNA from muscle was cloned, and it is comprised of 1068 nucleotides that encode a 384-amino acids protein, similar to other invertebrate AKs. The apparent Michaelis-Menten kinetic constant (Km) was 1.7 mM with a kcat of 75 s-1. Two crystal structures are presented, the apoPvAK and PpAK bound to arginine, both in the open conformation with the active site lid (residues 310-320) completely disordered. The guanidino group binding site in the apo structure appears to be organized to accept the arginine substrate. Finally, these results contribute to knowledge of mechanistic details of the function of arginine kinase.
dc.format
application/pdf
dc.language.iso
eng
dc.publisher
PeerJ Inc.
dc.rights
info:eu-repo/semantics/openAccess
dc.rights.uri
https://creativecommons.org/licenses/by-nc-sa/2.5/ar/
dc.subject
Allergen
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Arachnida
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Arginine Kinase
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Arthropoda
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Cdna Cloning
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Crystal Structure
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Open Conformation
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Phosphagen
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Polybetes Pytagoricus
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Spider
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Otras Ciencias Biológicas
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Ciencias Biológicas
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CIENCIAS NATURALES Y EXACTAS
dc.title
Biochemical and structural characterization of a novel arginine kinase from the spider Polybetes pythagoricus
dc.type
info:eu-repo/semantics/article
dc.type
info:ar-repo/semantics/artículo
dc.type
info:eu-repo/semantics/publishedVersion
dc.date.updated
2018-06-15T18:35:45Z
dc.journal.volume
2017
dc.journal.number
9
dc.journal.pagination
1-19
dc.journal.pais
Estados Unidos
dc.description.fil
Fil: Laino, Aldana. Consejo Nacional de Investigaciones Científicas y Técnicas. Centro Científico Tecnológico Conicet - La Plata. Instituto de Investigaciones Bioquímicas de La Plata ; Argentina
dc.description.fil
Fil: Lopez Zavala, Alonso A.. Universidad de Sonora; México
dc.description.fil
Fil: Garcia, Carlos Fernando. Centro de Investigación en Alimentación y Desarrollo; México
dc.description.fil
Fil: Carrasco Miranda, Jesus S.. Centro de Investigación en Alimentación y Desarrollo; México
dc.description.fil
Fil: Santana, Marianela. Consejo Nacional de Investigaciones Científicas y Técnicas. Centro Científico Tecnológico Conicet - La Plata. Instituto de Investigaciones Bioquímicas de La Plata ; Argentina
dc.description.fil
Fil: Stojanoff, Vivian. Consejo Nacional de Investigaciones Científicas y Técnicas. Centro Científico Tecnológico Conicet - La Plata. Instituto de Investigaciones Bioquímicas de La Plata ; Argentina
dc.description.fil
Fil: Sotelo Mundo, Rogerio Rafael. Centro de Investigación en Alimentación y Desarrollo; México. Consejo Nacional de Investigaciones Científicas y Técnicas; Argentina
dc.description.fil
Fil: Garcia, Carlos Fernando. Consejo Nacional de Investigaciones Científicas y Técnicas. Centro Científico Tecnológico Conicet - La Plata. Instituto de Investigaciones Bioquímicas de La Plata ; Argentina
dc.journal.title
PeerJ
dc.relation.alternativeid
info:eu-repo/semantics/altIdentifier/doi/https://dx.doi.org/10.7717/peerj.3787
dc.relation.alternativeid
info:eu-repo/semantics/altIdentifier/url/https://peerj.com/articles/3787/
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