Next Article in Journal
Amelioration of Mitochondrial Dysfunction-Induced Insulin Resistance in Differentiated 3T3-L1 Adipocytes via Inhibition of NF-κB Pathways
Next Article in Special Issue
Binding Mode Analysis of Zerumbone to Key Signal Proteins in the Tumor Necrosis Factor Pathway
Previous Article in Journal
Over-Expression of Copper/Zinc Superoxide Dismutase in the Median Preoptic Nucleus Attenuates Chronic Angiotensin II-Induced Hypertension in the Rat
Previous Article in Special Issue
Analysis of Protein–Protein Interactions in MCF-7 and MDA-MB-231 Cell Lines Using Phthalic Acid Chemical
Article Menu
Issue 12 (December) cover image

Export Article

Open AccessArticle
Int. J. Mol. Sci. 2014, 15(12), 22214-22226; doi:10.3390/ijms151222214

The Importance of Polarity in the Evolution of the K+ Binding Site of Pyruvate Kinase

1
Departamento de Bioquímica, Facultad de Medicina, Universidad Nacional Autónoma de México, 04510 Distrito Federal, Mexico
2
Departamento de Bioquímica, Instituto de Fisiología Celular, Universidad Nacional Autónoma de México, 04510 Distrito Federal, Mexico
*
Author to whom correspondence should be addressed.
Received: 25 August 2014 / Revised: 25 October 2014 / Accepted: 18 November 2014 / Published: 2 December 2014
(This article belongs to the Collection Proteins and Protein-Ligand Interactions)
View Full-Text   |   Download PDF [1325 KB, uploaded 2 December 2014]   |  

Abstract

In a previous phylogenetic study of the family of pyruvate kinase, we found one cluster with Glu117 and another with Lys117. Those sequences with Glu117 have Thr113 and are K+-dependent, whereas those with Lys117 have Leu113 and are K+-independent. The carbonyl oxygen of Thr113 is one of the residues that coordinate K+ in the active site. Even though the side chain of Thr113 does not participate in binding K+, the strict co-evolution between position 117 and 113 suggests that T113 may be the result of the evolutionary pressure to maintain the selectivity of pyruvate kinase activity for K+. Thus, we explored if the replacement of Thr113 by Leu alters the characteristics of the K+ binding site. We found that the polarity of the residue 113 is central in the partition of K+ into its site and that the substitution of Thr for Leu changes the ion selectivity for the monovalent cation with minor changes in the binding of the substrates. Therefore, Thr113 is instrumental in the selectivity of pyruvate kinase for K+. View Full-Text
Keywords: pyruvate kinase; K+; ion selectivity; monovalent cation; hydrophobicity; site-directed mutagenesis pyruvate kinase; K+; ion selectivity; monovalent cation; hydrophobicity; site-directed mutagenesis
This is an open access article distributed under the Creative Commons Attribution License which permits unrestricted use, distribution, and reproduction in any medium, provided the original work is properly cited. (CC BY 4.0).

Supplementary material

Scifeed alert for new publications

Never miss any articles matching your research from any publisher
  • Get alerts for new papers matching your research
  • Find out the new papers from selected authors
  • Updated daily for 49'000+ journals and 6000+ publishers
  • Define your Scifeed now

SciFeed Share & Cite This Article

MDPI and ACS Style

Ramírez-Silva, L.; Guerrero-Mendiola, C.; Cabrera, N. The Importance of Polarity in the Evolution of the K+ Binding Site of Pyruvate Kinase. Int. J. Mol. Sci. 2014, 15, 22214-22226.

Show more citation formats Show less citations formats

Related Articles

Article Metrics

Article Access Statistics

1

Comments

[Return to top]
Int. J. Mol. Sci. EISSN 1422-0067 Published by MDPI AG, Basel, Switzerland RSS E-Mail Table of Contents Alert
Back to Top