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Literature summary extracted from

  • Sugishima, M.; Kitamori, Y.; Noguchi, M.; Kohchi, T.; Fukuyama, K.
    Crystal structure of red chlorophyll catabolite reductase: enlargement of the ferredoxin-dependent bilin reductase family (2009), J. Mol. Biol., 389, 376-387.
    View publication on PubMed

Activating Compound

EC Number Activating Compound Comment Organism Structure
1.3.7.12 additional information the catalytic activity of RCCR in vitro dramatically increases by coupling with pheophorbide alpha oxygenase, which also results in a stereospecific product Arabidopsis thaliana
1.3.7.12 additional information the catalytic activity of RCCR in vitro dramatically increases by coupling with PaO, possibly due to cooperative action, although PaO has been localized to the plastid envelope and RCCR is a soluble stroma enzyme Arabidopsis thaliana

Cloned(Commentary)

EC Number Cloned (Comment) Organism
1.3.7.12 cloning and expression in Escherichia coli Arabidopsis thaliana

Crystallization (Commentary)

EC Number Crystallization (Comment) Organism
1.3.7.12 at 2.4 A resolution, determination of the crystal structure of, where chloroplast transit peptide is truncated and a Gly-Pro-Leu-Gly-Ser peptide is added to the N terminus, 2 peptide chains A and B are located in an asymmetric unit of the selenomethionine-RCCR crystal, these 2 chains form a homodimer, AtRCCR folds into an alpha/beta/alpha sandwich: 5 N-terminal alpha-helices, an anti-parallel beta-sheet consisting of 8 strands, and 4 C-terminal alpha-helices Arabidopsis thaliana
1.3.7.12 purified substrate-free enzyme, with the chloroplast transit peptide truncated and a Gly-Pro-Leu-Gly-Ser peptide added to the N-terminus, X-ray diffraction structure determination and analysis at 2.5-2.7 A resolution, structure modelling Arabidopsis thaliana

Localization

EC Number Localization Comment Organism GeneOntology No. Textmining
1.3.7.12 chloroplast mainly Arabidopsis thaliana 9507
-
1.3.7.12 chloroplast stroma, constitutive enzyme, the N-terminal 39-amino-acid stretch of RCCR is predicted to be the chloroplast transit peptide Arabidopsis thaliana 9507
-
1.3.7.12 mitochondrion in young seedlings and in response to stress, RCCR is somewhat localized to mitochondria Arabidopsis thaliana 5739
-
1.3.7.12 additional information RCCR is constitutively expressed in chloroplasts, whereas in young seedlings and in response to stress, it is also localized to mitochondria Arabidopsis thaliana
-
-

Molecular Weight [Da]

EC Number Molecular Weight [Da] Molecular Weight Maximum [Da] Comment Organism
1.3.7.12 32000
-
 2 * 32000, predicted by amino acid sequence, each subunit folds in an alpha/beta/alpha sandwich Arabidopsis thaliana
1.3.7.12 32000
-
 2 * 32000, about, sequence calculation Arabidopsis thaliana
1.3.7.12 60000
-
 about, gel filtration Arabidopsis thaliana
1.3.7.12 60000
-
 dimer, determined by gel filtration Arabidopsis thaliana

Natural Substrates/ Products (Substrates)

EC Number Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
1.3.7.12 red chlorophyll catabolite + 2 reduced ferredoxin [iron-sulfur] cluster + 2 H+ Arabidopsis thaliana
-
 primary fluorescent chlorophyll catabolite + 2 oxidized ferredoxin [iron-sulfur] cluster
-
 ?
1.3.7.12 red chlorophyll catabolite + reduced acceptor Arabidopsis thaliana the key steps in the degradation pathway of chlorophylls are the ring-opening reaction catalyzed by pheophorbide a oxygenase and sequential reduction by RCCR, RCCR catalyzes the ferredoxin-dependent reduction of the C20/C1 double bond of red chlorophyll catabolite primary fluorescent chlorophyll catabolite + oxidized acceptor in the acidic environment of vacuoles, primary fluorescent chlorophyll catabolite is spontaneously converted into nonfluorescent chlorophyll catabolites ?

Organism

EC Number Organism UniProt Comment Textmining
1.3.7.12 Arabidopsis thaliana Q8LDU4
-
-

Purification (Commentary)

EC Number Purification (Comment) Organism
1.3.7.12 anion exchange chromatography Arabidopsis thaliana

Source Tissue

EC Number Source Tissue Comment Organism Textmining
1.3.7.12 leaf
-
 Arabidopsis thaliana
-

Substrates and Products (Substrate)

EC Number Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
1.3.7.12 red chlorophyll catabolite + 2 reduced ferredoxin [iron-sulfur] cluster + 2 H+
-
 Arabidopsis thaliana primary fluorescent chlorophyll catabolite + 2 oxidized ferredoxin [iron-sulfur] cluster
-
 ?
1.3.7.12 red chlorophyll catabolite + 2 reduced ferredoxin [iron-sulfur] cluster + 2 H+
-
 Arabidopsis thaliana primary fluorescent chlorophyll catabolite + 2 oxidized ferredoxin [iron-sulfur] cluster formation of a stereospecific product, overview ?
1.3.7.12 red chlorophyll catabolite + reduced acceptor the key steps in the degradation pathway of chlorophylls are the ring-opening reaction catalyzed by pheophorbide a oxygenase and sequential reduction by RCCR, RCCR catalyzes the ferredoxin-dependent reduction of the C20/C1 double bond of red chlorophyll catabolite Arabidopsis thaliana primary fluorescent chlorophyll catabolite + oxidized acceptor in the acidic environment of vacuoles, primary fluorescent chlorophyll catabolite is spontaneously converted into nonfluorescent chlorophyll catabolites ?

Subunits

EC Number Subunits Comment Organism
1.3.7.12 homodimer 2 * 32000, predicted by amino acid sequence, each subunit folds in an alpha/beta/alpha sandwich Arabidopsis thaliana
1.3.7.12 homodimer 2 * 32000, about, sequence calculation Arabidopsis thaliana
1.3.7.12 More enzyme RCCR forms a homodimer, in which each subunit folds in an alphabetaalpha sandwich, five N-terminal alpha-helices (H1/H2/H3/H5/H7), an anti-parallel beta-sheet consisting of eight strands (S1-S8), and four C-terminal alpha-helices (H4/H6/H8/H9). The two subunits are related by noncrystallographic 2fold symmetry in which the alpha-helices near the edge of the beta-sheet unique in RCCR participate in intersubunit interaction. The putative RCC-binding site forms an open pocket surrounded by conserved residues among RCCRs. Residues Glu154 and Asp291 stand opposite each other in the substrate binding pocket and are likely involved in substrate binding and/or catalysis. Primary structure comparisons, overview Arabidopsis thaliana

Synonyms

EC Number Synonyms Comment Organism
1.3.7.12 RCCR
-
 Arabidopsis thaliana
1.3.7.12 red chlorophyll catabolite reductase
-
 Arabidopsis thaliana

Cofactor

EC Number Cofactor Comment Organism Structure
1.3.7.12 Ferredoxin
-
 Arabidopsis thaliana
1.3.7.12 Ferredoxin dependent on Arabidopsis thaliana

General Information

EC Number General Information Comment Organism
1.3.7.12 evolution the enzyme belongs to the ferredoxin-dependent bilin reductase (FDBR) family, which synthesizes a variety of phytobilin pigments, on the basis of sequence similarity, ferredoxin dependency, and the common tetrapyrrole skeleton of their substrates. The tertiary structure of RCCR is similar to those of FDBRs, strongly supporting that these enzymes evolved from a common ancestor Arabidopsis thaliana
1.3.7.12 additional information Residues Glu154 and Asp291 stand opposite each other in the substrate binding pocket and are likely involved in substrate binding and/or catalysis Arabidopsis thaliana
1.3.7.12 physiological function the key steps in the degradation pathway of chlorophylls are the ring opening reaction catalyzed by pheophorbide a oxygenase and sequential reduction by red chlorophyll catabolite reductase (RCCR). During these steps, chlorophyll catabolites lose their color and phototoxicity. Enzyme RCCR catalyzes the ferredoxin-dependent reduction of the C20/C1 double bond of red chlorophyll catabolite Arabidopsis thaliana