Photosynthetica 2012, 50(4):529-540 | DOI: 10.1007/s11099-012-0057-z

Light-dependent and light-independent protochlorophyllide oxidoreductases share similar sequence motifs -in silico studies

M. Gabruk1, J. Grzyb2, J. Kruk1, B. Mysliwa-Kurdziel1
1 Department of Plant Physiology and Biochemistry, Faculty of Biochemistry, Biophysics and Biotechnology, Jagiellonian University, Kraków, Poland
2 Laboratory of Biological Physics, Institute of Physics PAS, Warsaw, Poland

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.

Additional key words: chlorophyll biosynthesis; homology modeling; protochlorophyllide; protochlorophyllide oxidoreductase; sequence analysis

Received: January 20, 2012; Accepted: July 7, 2012; Published: December 1, 2012  Show citation

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Gabruk, M., Grzyb, J., Kruk, J., & Mysliwa-Kurdziel, B. (2012). Light-dependent and light-independent protochlorophyllide oxidoreductases share similar sequence motifs -in silico studies. Photosynthetica50(4), 529-540. doi: 10.1007/s11099-012-0057-z
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