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Literature summary for 1.3.1.33 extracted from

  • Gabruk, M.; Mysliwa-Kurdziel, B.
    The origin, evolution and diversification of multiple isoforms of light-dependent protochlorophyllide oxidoreductase (LPOR) focus on angiosperms (2020), Biochem. J., 477, 2221-2236 .
    View publication on PubMed
Search for more literature for 1.3.1.33

Activating Compound

Activating Compound Comment Organism Structure
phosphatidylglycerol active complexes of PORB preferentially bind to the lipid membranes due to the interaction with phosphatidylglycerol Arabidopsis thaliana
phosphatidylglycerol isoform PORC can bind chlorophyllide without the lipids under low NADPH concentrations. When the lipid concentration is high, PORC can oligomerize on the lipid membrane, which increases its activity Arabidopsis thaliana
phosphatidylglycerol the interaction with PG increases the affinity of the PORA towards NADPH, so active PORA complexes preferentially bind to the lipid membranes Arabidopsis thaliana

Localization

Localization Comment Organism GeneOntology No. Textmining
chloroplast
-
 Arabidopsis thaliana 9507
-

Organism

Organism UniProt Comment Textmining
Arabidopsis thaliana O48741
-
-
Arabidopsis thaliana P21218
-
-
Arabidopsis thaliana Q42536
-
-

Synonyms

Synonyms Comment Organism
PORA
-
 Arabidopsis thaliana
PORB
-
 Arabidopsis thaliana
PORC
-
 Arabidopsis thaliana

General Information

General Information Comment Organism
evolution all modern sequences of light-dependent protochlorophyllide oxidoreductase POR diverged from a single sequence about 1.36 billlion years ago. The LPOR gene was then duplicated at least 10 times in angiosperms, leading to the formation of two or even more LPOR isoforms in multiple species. In the case of Arabidopsis thaliana, isoforms PORA and PORB originated in one duplication event, in contrary to the isoform PORC, which diverged first Arabidopsis thaliana