Different catalytic properties of two highly homologous triosephosphate isomerase monomers Article

Zárate-Pérez, F, Chánez-Cárdenas, ME, Arreola, R et al. (2009). Different catalytic properties of two highly homologous triosephosphate isomerase monomers . BIOCHEMICAL AND BIOPHYSICAL RESEARCH COMMUNICATIONS, 382(3), 626-630. 10.1016/j.bbrc.2009.03.085

cited authors

  • Zárate-Pérez, F; Chánez-Cárdenas, ME; Arreola, R; Torres-Larios, A; Vázquez-Contreras, E

authors

abstract

  • It is assumed that amino acid sequence differences in highly homologous enzymes would be found at the peripheral level, subtle changes that would not necessarily affect catalysis. Here, we demonstrate that, using the same set of mutations at the level of the interface loop 3, the activity of a triosephosphate isomerase monomeric enzyme is ten times higher than that of a homologous enzyme with 74% identity and 86% similarity, whereas the activity of the native, dimeric enzymes is essentially the same. This is an example of how the dimeric biological unit evolved to compensate for the intrinsic differences found at the monomeric species level. Biophysical techniques of size exclusion chromatography, dynamic light scattering, X-ray crystallography, fluorescence and circular dichroism, as well as denaturation/renaturation assays with guanidinium hydrochloride and ANS binding, allowed us to fully characterize the properties of the new monomer. © 2009 Elsevier Inc. All rights reserved.

publication date

  • May 8, 2009

published in

Digital Object Identifier (DOI)

start page

  • 626

end page

  • 630

volume

  • 382

issue

  • 3