Light-dependent and light-independent protochlorophyllide oxidoreductases share similar sequence motifs —in silico studies |
| |
Authors: | M Gabruk J Grzyb J Kruk B Mysliwa-Kurdziel |
| |
Institution: | 1. Department of Plant Physiology and Biochemistry, Faculty of Biochemistry, Biophysics and Biotechnology, Jagiellonian University, ul. Gronostajowa 7, 30-387, Kraków, Poland 2. Laboratory of Biological Physics, Institute of Physics PAS, al. Lotników 32/46, 02-668, Warsaw, Poland
|
| |
Abstract: | In the present studies, we have found a fragment of amino acid sequence, called TFT motif, both in light-dependent protochlorophyllide oxidoreductase (LPOR) and in the L subunit of dark-operative (light-independent) protochlorophyllide oxidoreductases (DPOR). Amino acid residues of this motif shared similar physicochemical properties in both types of the enzymes. In the present paper, physicochemical properties of amino acid residues of this common motif, its spatial arrangement and a possible physiological role are being discussed. This is the first report when similarity between LPOR and DPOR, phylogenetically unrelated, but functionally redundant enzymes, is described. |
| |
Keywords: | |
本文献已被 SpringerLink 等数据库收录! |
|