Any feedback?
Please rate this page
(literature.php)
(0/150)

BRENDA support

Literature summary for 1.3.7.12 extracted from

  • Hoertensteiner, S.
    Chlorophyll breakdown in higher plants and algae (1999), Cell. Mol. Life Sci., 56, 330-347.
    View publication on PubMed

Inhibitors

Inhibitors Comment Organism Structure
O2 RCC reductase is sensitive towards oxygen, in vitro primary fluorescent chlorophyll catabolite formation from red chlorophyll catabolite occurs only under anoxic conditions Brassica napus
O2 RCC reductase is sensitive towards oxygen, in vitro primary fluorescent chlorophyll catabolite formation from red chlorophyll catabolite occurs only under anoxic conditions Capsicum annuum
O2 RCC reductase is sensitive towards oxygen, in vitro primary fluorescent chlorophyll catabolite formation from red chlorophyll catabolite occurs only under anoxic conditions Festuca pratensis
O2 RCC reductase is sensitive towards oxygen, in vitro primary fluorescent chlorophyll catabolite formation from red chlorophyll catabolite occurs only under anoxic conditions Hordeum vulgare
O2 RCC reductase is sensitive towards oxygen, in vitro primary fluorescent chlorophyll catabolite formation from red chlorophyll catabolite occurs only under anoxic conditions Phaseolus vulgaris

Localization

Localization Comment Organism GeneOntology No. Textmining
chloroplast stroma RCC reductase is a soluble protein of the stroma Brassica napus 9570
-
chloroplast stroma RCC reductase is a soluble protein of the stroma Festuca pratensis 9570
-
chloroplast stroma RCC reductase is a soluble protein of the stroma Hordeum vulgare 9570
-
gerontoplast RCC reductase is a soluble protein of the stroma Hordeum vulgare 34400
-
gerontoplast stroma RCC reductase is a soluble protein of the stroma Brassica napus 1905506
-
gerontoplast stroma RCC reductase is a soluble protein of the stroma Festuca pratensis 1905506
-

Metals/Ions

Metals/Ions Comment Organism Structure
Fe2+ in iron sulfur cluster Phaseolus vulgaris
Fe2+ in iron sulfur cluster Brassica napus
Fe2+ in iron sulfur cluster Capsicum annuum
Fe2+ in iron sulfur cluster Auxenochlorella protothecoides
Fe2+ in iron sulfur cluster Parachlorella kessleri
Fe2+ in iron sulfur cluster Festuca pratensis
Fe2+ in iron sulfur cluster Hordeum vulgare
iron sulfur cluster
-
Phaseolus vulgaris
iron sulfur cluster
-
Brassica napus
iron sulfur cluster
-
Capsicum annuum
iron sulfur cluster
-
Auxenochlorella protothecoides
iron sulfur cluster
-
Parachlorella kessleri
iron sulfur cluster
-
Festuca pratensis
iron sulfur cluster
-
Hordeum vulgare

Natural Substrates/ Products (Substrates)

Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
additional information Brassica napus in pFCC-1 of Brassica napus as well as in Chlorella protothecoides 18O is only found in the formyl group of pyrrole B, and hence the respective enzymes are monooxygenases. The lactam oxygen in pyrrole A is most probably derived from H2O ?
-
?
additional information Auxenochlorella protothecoides in pFCC-1 of Brassica napus as well as in Chlorella protothecoides 18O is only found in the formyl group of pyrrole B, and the respective enzymes are monooxygenases. The lactam oxygen in pyrrole A is most probably derived from H2O ?
-
?
red chlorophyll catabolite + 2 reduced ferredoxin [iron-sulfur] cluster + 2 H+ Phaseolus vulgaris
-
primary fluorescent chlorophyll catabolite + 2 oxidized ferredoxin [iron-sulfur] cluster
-
?
red chlorophyll catabolite + 2 reduced ferredoxin [iron-sulfur] cluster + 2 H+ Capsicum annuum
-
primary fluorescent chlorophyll catabolite + 2 oxidized ferredoxin [iron-sulfur] cluster
-
?
red chlorophyll catabolite + 2 reduced ferredoxin [iron-sulfur] cluster + 2 H+ Festuca pratensis
-
primary fluorescent chlorophyll catabolite + 2 oxidized ferredoxin [iron-sulfur] cluster
-
?
red chlorophyll catabolite + 2 reduced ferredoxin [iron-sulfur] cluster + 2 H+ Hordeum vulgare
-
primary fluorescent chlorophyll catabolite + 2 oxidized ferredoxin [iron-sulfur] cluster
-
?
red chlorophyll catabolite + 2 reduced ferredoxin [iron-sulfur] cluster + 2 H+ Auxenochlorella protothecoides in Chlorella, the release of red pigments is correlated with the loss of chlorophyll only if the cells are kept in the dark. These pigments are neither produced in light-grown cells nor in the dark if a source of nitrogen is provided primary fluorescent chlorophyll catabolite + 2 oxidized ferredoxin [iron-sulfur] cluster
-
?
red chlorophyll catabolite + 2 reduced ferredoxin [iron-sulfur] cluster + 2 H+ Parachlorella kessleri in Chlorella, the release of red pigments is correlated with the loss of chlorophyll only if the cells are kept in the dark. These pigments are neither produced in light-grown cells nor in the dark if a source of nitrogen is provided primary fluorescent chlorophyll catabolite + 2 oxidized ferredoxin [iron-sulfur] cluster
-
?
red chlorophyll catabolite + 2 reduced ferredoxin [iron-sulfur] cluster + 2 H+ Brassica napus two atoms of oxygen are introduced into RCC, pFCC-1 and the corresponding red catabolites of Chlorella protothecoides and production of pFCC-1 from Pheide a requires dioxygen primary fluorescent chlorophyll catabolite + 2 oxidized ferredoxin [iron-sulfur] cluster
-
?

Organism

Organism UniProt Comment Textmining
Auxenochlorella protothecoides
-
gene RCCR
-
Brassica napus
-
gene RCCR
-
Capsicum annuum
-
gene RCCR
-
Festuca pratensis
-
gene RCCR
-
Hordeum vulgare Q9MTQ6 gene RCCR
-
Parachlorella kessleri
-
gene RCCR
-
Phaseolus vulgaris
-
gene RCCR
-

Oxidation Stability

Oxidation Stability Organism
RCC reductase is sensitive towards oxygen, in vitro primary fluorescent chlorophyll catabolite formation from red chlorophyll catabolite occurs only under anoxic conditions Phaseolus vulgaris
RCC reductase is sensitive towards oxygen, in vitro primary fluorescent chlorophyll catabolite formation from red chlorophyll catabolite occurs only under anoxic conditions Brassica napus
RCC reductase is sensitive towards oxygen, in vitro primary fluorescent chlorophyll catabolite formation from red chlorophyll catabolite occurs only under anoxic conditions Capsicum annuum
RCC reductase is sensitive towards oxygen, in vitro primary fluorescent chlorophyll catabolite formation from red chlorophyll catabolite occurs only under anoxic conditions Festuca pratensis
RCC reductase is sensitive towards oxygen, in vitro primary fluorescent chlorophyll catabolite formation from red chlorophyll catabolite occurs only under anoxic conditions Hordeum vulgare

Purification (Commentary)

Purification (Comment) Organism
from senescent barley leaves to homogeneity Hordeum vulgare

Reaction

Reaction Comment Organism Reaction ID
primary fluorescent chlorophyll catabolite + 2 oxidized ferredoxin [iron-sulfur] cluster = red chlorophyll catabolite + 2 reduced ferredoxin [iron-sulfur] cluster + 2 H+ reaction pathway overview Phaseolus vulgaris
primary fluorescent chlorophyll catabolite + 2 oxidized ferredoxin [iron-sulfur] cluster = red chlorophyll catabolite + 2 reduced ferredoxin [iron-sulfur] cluster + 2 H+ reaction pathway overview Brassica napus
primary fluorescent chlorophyll catabolite + 2 oxidized ferredoxin [iron-sulfur] cluster = red chlorophyll catabolite + 2 reduced ferredoxin [iron-sulfur] cluster + 2 H+ reaction pathway overview Capsicum annuum
primary fluorescent chlorophyll catabolite + 2 oxidized ferredoxin [iron-sulfur] cluster = red chlorophyll catabolite + 2 reduced ferredoxin [iron-sulfur] cluster + 2 H+ reaction pathway overview Auxenochlorella protothecoides
primary fluorescent chlorophyll catabolite + 2 oxidized ferredoxin [iron-sulfur] cluster = red chlorophyll catabolite + 2 reduced ferredoxin [iron-sulfur] cluster + 2 H+ reaction pathway overview Parachlorella kessleri
primary fluorescent chlorophyll catabolite + 2 oxidized ferredoxin [iron-sulfur] cluster = red chlorophyll catabolite + 2 reduced ferredoxin [iron-sulfur] cluster + 2 H+ reaction pathway overview Festuca pratensis
primary fluorescent chlorophyll catabolite + 2 oxidized ferredoxin [iron-sulfur] cluster = red chlorophyll catabolite + 2 reduced ferredoxin [iron-sulfur] cluster + 2 H+ reaction pathway overview Hordeum vulgare

Source Tissue

Source Tissue Comment Organism Textmining
cell culture in Chlorella, the release of red pigments is correlated with the loss of chlorophyll only if the cells are kept in the dark. These pigments are neither produced in light-grown cells nor in the dark if a source of nitrogen is provided Parachlorella kessleri
-
cotyledon senescent cotyledons Brassica napus
-
leaf senescent Festuca pratensis
-
leaf senescent Hordeum vulgare
-
additional information in Chlorella, the release of red pigments is correlated with the loss of chlorophyll only if the cells are kept in the dark. These pigments are neither produced in light-grown cells nor in the dark if a source of nitrogen is provided Auxenochlorella protothecoides
-

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
additional information in pFCC-1 of Brassica napus as well as in Chlorella protothecoides 18O is only found in the formyl group of pyrrole B, and hence the respective enzymes are monooxygenases. The lactam oxygen in pyrrole A is most probably derived from H2O Brassica napus ?
-
?
additional information in pFCC-1 of Brassica napus as well as in Chlorella protothecoides 18O is only found in the formyl group of pyrrole B, and the respective enzymes are monooxygenases. The lactam oxygen in pyrrole A is most probably derived from H2O Auxenochlorella protothecoides ?
-
?
red chlorophyll catabolite + 2 reduced ferredoxin [iron-sulfur] cluster + 2 H+
-
Phaseolus vulgaris primary fluorescent chlorophyll catabolite + 2 oxidized ferredoxin [iron-sulfur] cluster
-
?
red chlorophyll catabolite + 2 reduced ferredoxin [iron-sulfur] cluster + 2 H+
-
Capsicum annuum primary fluorescent chlorophyll catabolite + 2 oxidized ferredoxin [iron-sulfur] cluster
-
?
red chlorophyll catabolite + 2 reduced ferredoxin [iron-sulfur] cluster + 2 H+
-
Parachlorella kessleri primary fluorescent chlorophyll catabolite + 2 oxidized ferredoxin [iron-sulfur] cluster
-
?
red chlorophyll catabolite + 2 reduced ferredoxin [iron-sulfur] cluster + 2 H+
-
Festuca pratensis primary fluorescent chlorophyll catabolite + 2 oxidized ferredoxin [iron-sulfur] cluster
-
?
red chlorophyll catabolite + 2 reduced ferredoxin [iron-sulfur] cluster + 2 H+
-
Hordeum vulgare primary fluorescent chlorophyll catabolite + 2 oxidized ferredoxin [iron-sulfur] cluster
-
?
red chlorophyll catabolite + 2 reduced ferredoxin [iron-sulfur] cluster + 2 H+ in Chlorella, the release of red pigments is correlated with the loss of chlorophyll only if the cells are kept in the dark. These pigments are neither produced in light-grown cells nor in the dark if a source of nitrogen is provided Auxenochlorella protothecoides primary fluorescent chlorophyll catabolite + 2 oxidized ferredoxin [iron-sulfur] cluster
-
?
red chlorophyll catabolite + 2 reduced ferredoxin [iron-sulfur] cluster + 2 H+ in Chlorella, the release of red pigments is correlated with the loss of chlorophyll only if the cells are kept in the dark. These pigments are neither produced in light-grown cells nor in the dark if a source of nitrogen is provided Parachlorella kessleri primary fluorescent chlorophyll catabolite + 2 oxidized ferredoxin [iron-sulfur] cluster
-
?
red chlorophyll catabolite + 2 reduced ferredoxin [iron-sulfur] cluster + 2 H+ two atoms of oxygen are introduced into RCC, pFCC-1 and the corresponding red catabolites of Chlorella protothecoides and production of pFCC-1 from Pheide a requires dioxygen Brassica napus primary fluorescent chlorophyll catabolite + 2 oxidized ferredoxin [iron-sulfur] cluster
-
?
red chlorophyll catabolite + 2 reduced ferredoxin [iron-sulfur] cluster + 2 H+ two atoms of oxygen are introduced into RCC, pFCC-1 and the corresponding red catabolites of Chlorella protothecoides and production of pFCC-1 from Pheide a requires dioxygen Auxenochlorella protothecoides primary fluorescent chlorophyll catabolite + 2 oxidized ferredoxin [iron-sulfur] cluster
-
?
red chlorophyll catabolite + 2 reduced ferredoxin [iron-sulfur] cluster + 2 H+ stereospecificity towards reduction of C1 Phaseolus vulgaris primary fluorescent chlorophyll catabolite + 2 oxidized ferredoxin [iron-sulfur] cluster
-
?
red chlorophyll catabolite + 2 reduced ferredoxin [iron-sulfur] cluster + 2 H+ stereospecificity towards reduction of C1 Festuca pratensis primary fluorescent chlorophyll catabolite + 2 oxidized ferredoxin [iron-sulfur] cluster
-
?
red chlorophyll catabolite + 2 reduced ferredoxin [iron-sulfur] cluster + 2 H+ stereospecificity towards reduction of C1 Hordeum vulgare primary fluorescent chlorophyll catabolite + 2 oxidized ferredoxin [iron-sulfur] cluster three products identified as pFCC-1 and pFCC-2, that have identical constitutions but differ in the absolute configuration at C1, and pFCC-3 with undetermined structure ?
red chlorophyll catabolite + 2 reduced ferredoxin [iron-sulfur] cluster + 2 H+ stereospecificity towards reduction of C1 Capsicum annuum primary fluorescent chlorophyll catabolite + 2 oxidized ferredoxin [iron-sulfur] cluster two products identified as pFCC-1 and pFCC-2, that have identical constitutions but differ in the absolute configuration at C1 ?
red chlorophyll catabolite + 2 reduced ferredoxin [iron-sulfur] cluster + 2 H+ two atoms of oxygen are introduced into RCC, pFCC-1 and the corresponding red catabolites of Chlorella protothecoides and production of pFCC-1 from Pheide a requires dioxygen, stereospecificity towards reduction of C1 Brassica napus primary fluorescent chlorophyll catabolite + 2 oxidized ferredoxin [iron-sulfur] cluster
-
?

Synonyms

Synonyms Comment Organism
RCC reductase
-
Phaseolus vulgaris
RCC reductase
-
Brassica napus
RCC reductase
-
Capsicum annuum
RCC reductase
-
Auxenochlorella protothecoides
RCC reductase
-
Parachlorella kessleri
RCC reductase
-
Festuca pratensis
RCC reductase
-
Hordeum vulgare

Cofactor

Cofactor Comment Organism Structure
Ferredoxin
-
Phaseolus vulgaris
Ferredoxin
-
Brassica napus
Ferredoxin
-
Capsicum annuum
Ferredoxin
-
Auxenochlorella protothecoides
Ferredoxin
-
Parachlorella kessleri
Ferredoxin
-
Festuca pratensis
Ferredoxin
-
Hordeum vulgare

General Information

General Information Comment Organism
evolution RCC reductase activity can be demonstrated in mono- as well as in dicotyledons, and is also found in pteridophytes and gymnosperms. Within a plant family RCC reductases from different genera and species have the same stereospecificity Phaseolus vulgaris
evolution RCC reductase activity can be demonstrated in mono- as well as in dicotyledons, and is also found in pteridophytes and gymnosperms. Within a plant family RCC reductases from different genera and species have the same stereospecificity Brassica napus
evolution RCC reductase activity can be demonstrated in mono- as well as in dicotyledons, and is also found in pteridophytes and gymnosperms. Within a plant family RCC reductases from different genera and species have the same stereospecificity Capsicum annuum
evolution RCC reductase activity can be demonstrated in mono- as well as in dicotyledons, and is also found in pteridophytes and gymnosperms. Within a plant family RCC reductases from different genera and species have the same stereospecificity Festuca pratensis
evolution RCC reductase activity can be demonstrated in mono- as well as in dicotyledons, and is also found in pteridophytes and gymnosperms. Within a plant family RCC reductases from different genera and species have the same stereospecificity Hordeum vulgare
metabolism leaf senescence is accompanied by the metabolism of chlorophyll (Chl) to nonfluorescent catabolites (NCCs). The pathway of Chl degradation comprises several reactions and includes the occurrence of intermediary catabolites. After removal of phytol and the central Mg atom from Chl by chlorophyllase and Mg dechelatase, respectively, the porphyrin macrocycle of pheophorbide (Pheide) a is cleaved. This two-step reaction is catalyzed by Pheide a oxygenase and RCC reductase and yields a primary fluorescent catabolite (pFCC). After hydroxylation and additional species-specific modifications, FCCs are tautomerized nonenzymically to NCCs inside the vacuole Festuca pratensis
metabolism leaf senescence is accompanied by the metabolism of chlorophyll (Chl) to nonfluorescent catabolites (NCCs). The pathway of Chl degradation comprises several reactions and includes the occurrence of intermediary catabolites. After removal of phytol and the central Mg atom from Chl by chlorophyllase and Mg dechelatase, respectively, the porphyrin macrocycle of pheophorbide (Pheide) a is cleaved. This two-step reaction is catalyzed by Pheide a oxygenase and RCC reductase and yields a primary fluorescent catabolite (pFCC). After hydroxylation and additional species-specific modifications, in Chlorella, the final degradation products of chlorophyll are excreted into the surrounding medium, whereas in higher plants they are deposited in the vacuoles of mesophyll cells. Occurrence of catabolites of both Chl a and b in Chlorella. In Chlorella porphyrin cleavage does not require the joint action of a monooxygenase and a reductase as is the case in higher plants Parachlorella kessleri
metabolism leaf senescence is accompanied by the metabolism of chlorophyll (Chl) to nonfluorescent catabolites (NCCs). The pathway of Chl degradation comprises several reactions and includes the occurrence of intermediary catabolites. After removal of phytol and the central Mg atom from Chl by chlorophyllase and Mg dechelatase, respectively, the porphyrin macrocycle of pheophorbide (Pheide) a is cleaved. This two-step reaction is catalyzed by Pheide a oxygenase and RCC reductase and yields a primary fluorescent catabolite (pFCC). Two atoms of oxygen are introduced into RCC, pFCC-1 and the corresponding red catabolites of Chlorella protothecoides and production of pFCC-1 from Pheide a requires dioxygen. After hydroxylation and additional species-specific modifications, FCCs are tautomerized nonenzymically to NCCs inside the vacuole Brassica napus
metabolism leaf senescence is accompanied by the metabolism of chlorophyll to nonfluorescent catabolites (NCCs). The pathway of chlorophyll degradation comprises several reactions and includes the occurrence of intermediary catabolites. After removal of phytol and the central Mg atom from chlorophyll by chlorophyllase and Mg dechelatase, respectively, the porphyrin macrocycle of pheophorbide (Pheide) a is cleaved. This two-step reaction is catalyzed by Pheide a oxygenase and RCC reductase and yields a primary fluorescent catabolite (pFCC). After hydroxylation and additional species-specific modifications, FCCs are tautomerized nonenzymically to NCCs inside the vacuole Phaseolus vulgaris
metabolism leaf senescence is accompanied by the metabolism of chlorophyll to nonfluorescent catabolites (NCCs). The pathway of chlorophyll degradation comprises several reactions and includes the occurrence of intermediary catabolites. After removal of phytol and the central Mg atom from chlorophyll by chlorophyllase and Mg dechelatase, respectively, the porphyrin macrocycle of pheophorbide (Pheide) a is cleaved. This two-step reaction is catalyzed by Pheide a oxygenase and RCC reductase and yields a primary fluorescent catabolite (pFCC). After hydroxylation and additional species-specific modifications, FCCs are tautomerized nonenzymically to NCCs inside the vacuole Capsicum annuum
metabolism leaf senescence is accompanied by the metabolism of chlorophyll to nonfluorescent catabolites (NCCs). The pathway of chlorophyll degradation comprises several reactions and includes the occurrence of intermediary catabolites. After removal of phytol and the central Mg atom from chlorophyll by chlorophyllase and Mg dechelatase, respectively, the porphyrin macrocycle of pheophorbide (Pheide) a is cleaved. This two-step reaction is catalyzed by Pheide a oxygenase and RCC reductase and yields a primary fluorescent catabolite (pFCC). After hydroxylation and additional species-specific modifications, FCCs are tautomerized nonenzymically to NCCs inside the vacuole Hordeum vulgare
metabolism the oxygenase catalyzing porphyrin cleavage is a monooxygenase. In Chlorella, a mechanism with intermediary formation of a C4:C5 epoxide and subsequent hydrolytic cleavage and prototropic rearrangements has been proposed. Thereby, the second rearrangement at C10 has been demonstrated to be highly stereoselective. Two atoms of oxygen are introduced into RCC, pFCC-1 and the corresponding red catabolites of Chlorella protothecoides and production of pFCC-1 from Pheide a requires dioxygen. After hydroxylation and additional species-specific modifications, in Chlorella, the final degradation products of chlorophyll are excreted into the surrounding medium, whereas in higher plants they are deposited in the vacuoles of mesophyll cells. Occurrence of catabolites of both Chl a and b in Chlorella. In Chlorella porphyrin cleavage does not require the joint action of a monooxygenase and a reductase as is the case in higher plants Auxenochlorella protothecoides
additional information in contrast to the enzyme's O2 sensitivity, the coupled in vitro assay (formation of pFCC from Pheide a) requires oxygen for incorporation into the substrate. In the metabolic channelling of the two partial reactions, PaO creates an oxygen-depleted microenvironment which allows the action of RCC reductase Phaseolus vulgaris
additional information in contrast to the enzyme's O2 sensitivity, the coupled in vitro assay (formation of pFCC from Pheide a) requires oxygen for incorporation into the substrate. In the metabolic channelling of the two partial reactions, PaO creates an oxygen-depleted microenvironment which allows the action of RCC reductase Brassica napus
additional information in contrast to the enzyme's O2 sensitivity, the coupled in vitro assay (formation of pFCC from Pheide a) requires oxygen for incorporation into the substrate. In the metabolic channelling of the two partial reactions, PaO creates an oxygen-depleted microenvironment which allows the action of RCC reductase Capsicum annuum
additional information in contrast to the enzyme's O2 sensitivity, the coupled in vitro assay (formation of pFCC from Pheide a) requires oxygen for incorporation into the substrate. In the metabolic channelling of the two partial reactions, PaO creates an oxygen-depleted microenvironment which allows the action of RCC reductase Festuca pratensis
additional information in contrast to the enzyme's O2 sensitivity, the coupled in vitro assay (formation of pFCC from Pheide a) requires oxygen for incorporation into the substrate. In the metabolic channelling of the two partial reactions, PaO creates an oxygen-depleted microenvironment which allows the action of RCC reductase Hordeum vulgare