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Literature summary for 1.2.1.70 extracted from

  • Czarnecki, O.; Hedtke, B.; Melzer, M.; Rothbart, M.; Richter, A.; Schroeter, Y.; Pfannschmidt, T.; Grimm, B.
    An Arabidopsis GluTR binding protein mediates spatial separation of 5-aminolevulinic acid synthesis in chloroplasts (2011), Plant Cell, 23, 4476-4491.
    View publication on PubMedView publication on EuropePMC

Organism

Organism UniProt Comment Textmining
Arabidopsis thaliana
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Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
additional information identification of a GluTR binding protein, GluTRBP, that is localized in chloroplasts and is part of a 300000 Da protein complex in the thylakoid membrane, protein does not modulate activity of ALA synthesis, but the knockout of GluTRBP is lethal in Arabidopsis thaliana, whereas mutants expressing reduced levels of GluTRBP contain less heme Arabidopsis thaliana ?
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Synonyms

Synonyms Comment Organism
GluTR
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Arabidopsis thaliana

Expression

Organism Comment Expression
Arabidopsis thaliana expression profiles in the first hours of deetiolation of Arabidopsis seedlings show an abundance of GluTR that gradually increased with chlorophyll biosynthesis up

General Information

General Information Comment Organism
metabolism GluTR is proposed to be the key regulatory enzyme of tetrapyrrole biosynthetic pathway that is tightly controlled at transcriptional and posttranslational levels Arabidopsis thaliana