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Literature summary for 2.1.1.11 extracted from

  • Richter, A.S.; Wang, P.; Grimm, B.
    Arabidopsis Mg-protoporphyrin IX methyltransferase activity and redox regulation depend on conserved cysteines (2016), Plant Cell Physiol., 57, 519-527 .
    View publication on PubMed

Activating Compound

Activating Compound Comment Organism Structure
dithiothreitol about 80% increase in activity in presence of dithiothreitol Arabidopsis thaliana

Cloned(Commentary)

Cloned (Comment) Organism
expression in Escherichia coli Arabidopsis thaliana

Protein Variants

Protein Variants Comment Organism
C111S 0.1% of wild-type activity Arabidopsis thaliana
C111S/C115S only residual in vitro activity under reducing conditions, almost complete loss of activity under non-reducing conditions Arabidopsis thaliana
C115S 20% of wild-type activity, strong stimulation by dithiothreitol Arabidopsis thaliana
C115S/C177S only residual in vitro activity under reducing conditions, almost complete loss of activity under non-reducing conditions Arabidopsis thaliana
C177S residue is responsible for redox-dependent enzyme activation. In absence of dithiothreitol, increased activity compared with wild-type. Only slight activation by dithiothreitol Arabidopsis thaliana

Molecular Weight [Da]

Molecular Weight [Da] Molecular Weight Maximum [Da] Comment Organism
70000
-
PAGE, part of protein Arabidopsis thaliana
120000
-
PAGE, part of protein Arabidopsis thaliana

Organism

Organism UniProt Comment Textmining
Arabidopsis thaliana Q9SW18
-
-

Synonyms

Synonyms Comment Organism
ChlM
-
Arabidopsis thaliana

General Information

General Information Comment Organism
physiological function Mg protoporphyrin IX methyltransferase is activated and stabilized by interaction with NADPH-dependent thioredoxin reductase NTRC Arabidopsis thaliana