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Literature summary for 1.3.7.12 extracted from

  • Hoertensteiner, S.
    Chlorophyll degradation during senescence (2006), Annu. Plant Biol., 57, 55-77.
    View publication on PubMed

Cloned(Commentary)

Cloned (Comment) Organism
recombinant expression of chimeric enzyme mutants in Escherichia coli Arabidopsis thaliana

Protein Variants

Protein Variants Comment Organism
additional information construction of chimeric enzymes composed of portions of the Arabidopsis and the tomato proteins and expression in Escherichia coli, functional complementation of Arabidopsis acd2-2 mutant Arabidopsis thaliana

Localization

Localization Comment Organism GeneOntology No. Textmining
chloroplast soluble protein Arabidopsis thaliana 9507
-
additional information in young Arabidopsis seedlings, the enzyme is also associated with mitochondria Arabidopsis thaliana
-
-

Molecular Weight [Da]

Molecular Weight [Da] Molecular Weight Maximum [Da] Comment Organism
31000
-
x * 35000, precursor enzyme, SDS-PAGE, x * 31000, mature enzyme, SDS-PAGE Arabidopsis thaliana
35000
-
x * 35000, precursor enzyme, SDS-PAGE, x * 31000, mature enzyme, SDS-PAGE Arabidopsis thaliana

Natural Substrates/ Products (Substrates)

Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
red chlorophyll catabolite + 2 reduced ferredoxin [iron-sulfur] cluster + 2 H+ Arabidopsis thaliana
-
primary fluorescent chlorophyll catabolite + 2 oxidized ferredoxin [iron-sulfur] cluster
-
?

Organism

Organism UniProt Comment Textmining
Arabidopsis thaliana Q8LDU4 gene RCCR or ACD2
-

Source Tissue

Source Tissue Comment Organism Textmining
leaf
-
Arabidopsis thaliana
-
seedling
-
Arabidopsis thaliana
-

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
red chlorophyll catabolite + 2 reduced ferredoxin [iron-sulfur] cluster + 2 H+
-
Arabidopsis thaliana primary fluorescent chlorophyll catabolite + 2 oxidized ferredoxin [iron-sulfur] cluster
-
?
red chlorophyll catabolite + 2 reduced ferredoxin [iron-sulfur] cluster + 2 H+ reduction of the C20/C1 double bond of red chlorophyll catabolite is catalyzed by RCCR in a stereospecific manner forming the C1 isomer pFCC-1 Arabidopsis thaliana primary fluorescent chlorophyll catabolite + 2 oxidized ferredoxin [iron-sulfur] cluster
-
?

Subunits

Subunits Comment Organism
? x * 35000, precursor enzyme, SDS-PAGE, x * 31000, mature enzyme, SDS-PAGE Arabidopsis thaliana

Synonyms

Synonyms Comment Organism
AtRCCR
-
Arabidopsis thaliana
RCC reductase
-
Arabidopsis thaliana
RCCR
-
Arabidopsis thaliana
red Chl catabolite reductase
-
Arabidopsis thaliana

Cofactor

Cofactor Comment Organism Structure
Ferredoxin ferredoxin dependent, but appears to lack a metal or flavin cofactor, indicating that electrons are directly transferred from ferredoxin to red chlorophyll catabolite, RCC Arabidopsis thaliana

General Information

General Information Comment Organism
evolution RCCR is distantly related to a family of bilin reductases Arabidopsis thaliana
malfunction mutants defective in pheophorbide a oxygenase or red chlorophyll catabolite reductase, e.g. acd2 mutants that exhibit a light-dependent cell death phenotype with spontaneous spreading lesions, the mutants develop a lesion mimic phenotype, due to accumulation of breakdown intermediates Arabidopsis thaliana
metabolism the three chl catabolic enzymes, chlorophyllase, pheophorbide a oxygenase (PAO), and red chlorophyll catabolite reductase (RCCR) catalyze chlorophyll breakdown, which is very important for plant development and survival. Chlorophyll breakdown is a prerequisite to detoxify the potentially phototoxic pigment within the vacuoles in order to permit the remobilization of nitrogen from chlorophyll-binding proteins to proceed during senescence. Enzyme RCCR might be required to mediate an efficient interaction between red chlorophyll catabolite (still bound to PAO) and ferredoxin, thereby enabling a fast, regio-, and stereoselective reduction to primary fluorescent chlorophyll catabolite Arabidopsis thaliana