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Literature summary 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

Activating Compound

EC Number Activating Compound Comment Organism Structure
1.3.1.33 phosphatidylglycerol active complexes of PORB preferentially bind to the lipid membranes due to the interaction with phosphatidylglycerol Arabidopsis thaliana
1.3.1.33 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
1.3.1.33 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

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

Organism

EC Number Organism UniProt Comment Textmining
1.3.1.33 Arabidopsis thaliana O48741
-
-
1.3.1.33 Arabidopsis thaliana P21218
-
-
1.3.1.33 Arabidopsis thaliana Q42536
-
-

Synonyms

EC Number Synonyms Comment Organism
1.3.1.33 PORA
-
 Arabidopsis thaliana
1.3.1.33 PORB
-
 Arabidopsis thaliana
1.3.1.33 PORC
-
 Arabidopsis thaliana

General Information

EC Number General Information Comment Organism
1.3.1.33 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