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Literature summary for 1.8.1.9 extracted from

  • Richter, A.S.; Peter, E.; Rothbart, M.; Schlicke, H.; Toivola, J.; Rintamaeki, E.; Grimm, B.
    Posttranslational influence of NADPH-dependent thioredoxin reductase C on enzymes in tetrapyrrole synthesis (2013), Plant Physiol., 162, 63-73 .
    View publication on PubMedView publication on EuropePMC

Organism

Organism UniProt Comment Textmining
Arabidopsis thaliana O22229
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General Information

General Information Comment Organism
physiological function Arabidopsis thaliana NtrC knockout mutants show lower magnesium protoporphyrin IX and magnesium protoporphyrin IX monomethylester steady-state levels, the substrate and the product of protoporphyrin IX methyltransferase CHLM preceding MgPMME cyclase, while protoporphyrin IX strongly accumulates in mutant leaves after 5-aminolevulinic acid feeding. The mutant has a reduced capacity to synthesize 5-aminolevulinic acid and reduced CHLM activity compared with the wild-type. The contents of glutamyl-transfer RNA reductase1 and CHLM are reduced. NtrC physically interacts with glutamyl-transfer RNA reductase1 and CHLM. NtrC mutant plants contain partly oxidized CHLM, the wild-type has only reduced CHLM Arabidopsis thaliana