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

Title:

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

Creator:

Gabruk, M., Grzyb, J., Kruk, J., and Mysliwa-Kurdziel, B.

Identifier:

https://cdk.lib.cas.cz/client/handle/uuid:f2dbee37-a4cf-494f-ba76-d88684d8cfe5
uuid:f2dbee37-a4cf-494f-ba76-d88684d8cfe5
issn:0300-3604
doi:10.1007/s11099-012-0057-z

Subject:

botanika, botany, chlorophyll biosynthesis, homology modeling, protochlorophyllide, protochlorophyllide oxidoreductase, sequence analysis, 2, and 58

Type:

model:article and TEXT

Format:

bez média and svazek

Description:

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., M. Gabruk ... [et al.]., and Obsahuje bibliografii

Language:

Multiple languages

Rights:

http://creativecommons.org/licenses/by-nc-sa/4.0/
policy:public

Coverage:

529-540

Source:

Photosynthetica | 2012 Volume:50 | Number:4

Harvested from:

CDK

Metadata only:

false