EC Number   |
General Information |
Reference |
|---|
   1.3.7.12 | evolution |
evolutionary tree of vascular plants based on analysis of several molecular data sets for enzymes RCCR, overview. RCCR-1 appears to have evolved independently in some unrelated lineages. It has a restricted phylogenetic distribution and most likely represents recent derivations from RCC-2. Two forms of primary fluorescent chlorophyll catabolite, pFCC, are found in plants, the slightly more polar pFCC-1 or the less polar pFCC-2. A third form, pFCC-3 is found only in basal pteridophytes and in some gymnosperms, it seems to be produced by an ancestral type of RCCR. RCCR-1 appears to have evolved independently in some unrelated lineages. It has a restricted phylogenetic distribution and most likely represents recent derivations from RCCR-2. The situation within monocots appears to be quite clear cut. All the grasses and Carex tested are characterized by type 1 of RCCR, all other monocots produce pFCC-2 |
676395 |
| 1.3.7.12 | evolution |
evolutionary tree of vascular plants based on analysis of several molecular data sets for enzymes RCCR, overview. Two forms of primary fluorescent chlorophyll catabolite, pFCC, are found in plants, the slightly more polar pFCC-1 or the less polar pFCC-2. A third form, pFCC-3 is found only in basal pteridophytes and in some gymnosperms, it seems to be produced by an ancestral type of RCCR. RCCR-1 appears to have evolved independently in some unrelated lineages. It has a restricted phylogenetic distribution and most likely represents recent derivations from RCCR-2. The situation within monocots appears to be quite clear cut. All the grasses and Carex tested are characterized by type 1 of RCCR, all other monocots produce pFCC-2 |
676395 |
| 1.3.7.12 | evolution |
in chlorophyll breakdown, the basic mechanism of macrocycle cleavage appears to be the same in green algae and in angiosperms |
676395 |
| 1.3.7.12 | 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 |
735913 |
| 1.3.7.12 | evolution |
RCCR is distantly related to a family of bilin reductases |
735438 |
| 1.3.7.12 | evolution |
red chlorophyll catabolite reductases appear to represent a phylogenetically early addition to the chlorophyll catabolic pathway. Two types of red chlorophyll-catabolite reductases (RCCR), named RCCR-type 1 and RCCR-type 2, appear to have evolved in higher plants. Chlorophyll catabolism in higher plants differs remarkably from that in the green alga by the formation of FCCs and NCCs |
736215 |
| 1.3.7.12 | evolution |
red chlorophyll catabolite reductases appear to represent a phylogenetically early addition to the chlorophyll catabolic pathway. Two types of red chlorophyll-catabolite reductases (RCCR), named RCCR-type 1 and RCCR-type 2, appear to have evolved in higher plants. Chlorophyll catabolism in higher plants differs remarkably from that in the green algae by the formation of FCCs and NCCs |
736215 |
| 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 |
699585 |
| 1.3.7.12 | evolution |
the enzyme belongs to the ferredoxin-dependent bilin reductase (FDBR) family. RCC is bound to the pocket between the beta-sheet and the C-terminal alpha-helices, as seen in substrate-bound FDBRs, but RCC binding to RCCR is much looser than substrate binding to FDBRs |
712769 |
| 1.3.7.12 | evolution |
the enzyme belongs to the ferredoxin-dependent bilin reductase family, FDBR, and contains two conserved acidic residue sites (Glu151 and Asp288), which are involved in catalysis and/or substrate binding |
736190 |
