EC Number   |
General Information |
Reference |
|---|
    1.3.1.75 | evolution |
BciA (NADPH-dependent C8 divinyl reductase) is a much faster and less energy consuming catalytic enzyme than the chlorophyllide oxidoreductase (COR, EC 1.3.7.15). This finding implies that the bciA gene was acquired in each ancestral lineage by multiple horizontal gene transfer events after the establishment of anoxygenic photosynthesis. The high demand of Chl for large antenna complexes might have a major selective pressure for the evolutionary acquisition of an auxiliary divinyl reductase, BciA. Compared to the enzymatic activity of a-COR from Rhodobacter capsulatus, BciA has a lower affinity for DV-Chlide a but a much higher specific activity |
-, 763382 |
| 1.3.1.75 | evolution |
either F-DVR or N-DVR is found in most photosynthetic organisms, yet both F-DVR and N-DVR exist in the genome of diatoms that contain Chl a and Chl c1 |
746037 |
| 1.3.1.75 | evolution |
either F-DVR or N-DVR is found in most photosynthetic organisms, yet both F-DVR and N-DVR exist in the genome of diatoms that contain Chl a and Chl c1. Diatom N-DVR has evolved to function in Chl a biosynthesis, and diatom F-DVR is responsible for the biosynthesis of Chl c1 from Chl c2 |
746037 |
| 1.3.1.75 | evolution |
single DVR with broad substrate specificity is responsible for reducing the 8-vinyl groups of various chlorophyll intermediates in higher plants, but DVR proteins from different species have diverse and differing substrate preferences, although they are homologous |
746105 |
| 1.3.1.75 | evolution |
two isozymes of 8-vinyl reductase are described in oxygenic photosynthetic organisms: one encoded by BciA and another by BciB. Only BciB contains an [Fe-S] cluster and most cyanobacteria harbor this form, whereas a few contain BciA. Given this disparity in distribution. Cyanobacterial BciA encodes a functional 8-vinyl reductase, as evidenced by measuring the in vitro activity of recombinant Synechococcus and Acaryochloris BciA. Genomic comparison reveals that BciB had been replaced by BciA during evolution of the marine cyanobacterium Synechococcus, and coincided with replacement of Fe-superoxide dismutase (SOD) with Ni-SOD. These findings imply that the acquisition of BciA confers an adaptive advantage to cyanobacteria living in low-iron oceanic environments |
-, 762685 |
| 1.3.1.75 | evolution |
two unrelated classes of 8-vinyl reductases are known to exist in oxygenic phototrophs, BciA and BciB. Transcript and proteomic analysis of Acaryochloris marina reveal that both bciA and bciB are expressed and their encoded proteins are present in the cell, possibly in order to ensure that all synthesized chlorophyll pigment carries an ethyl group at C-8. The presence of two 8-vinyl reductases is unique for cyanobacteria. The phylogenetic positions of Acaryochloris marina BciA and BciB are both broadly consistent with those shown for Acaryochloris marina in the 16S rRNA trees, suggesting that the bciA and bciB genes have not been acquired by horizontal transfer. However, the positions of Synechococcus spp. in the BciA tree and the clade containing the green sulfur bacteria in the BciB tree are inconsistent with the 16S rRNA phylogeny, indicating that there may have been lateral transfer events during the evolution of both bciA and bciB |
-, 745221 |
| 1.3.1.75 | evolution |
two unrelated classes of C8-vinyl reductase are known to exist, BciA and BciB |
-, 744270 |
| 1.3.1.75 | malfunction |
loss of 8-vinyl reductase activity in Acaryochloris marina results in the production of 8-vinyl-Chl a and 8-vinyl-Chl d with a negative effect on viability of the cells |
-, 745221 |
| 1.3.1.75 | malfunction |
single mutants with deleted BciA or COR show production of the C8 ethyl group pigments, whereas the double mutant accumulates 8-vinyl-chlorophyllide, indicating that there is no enzyme other than BciA and COR functioning as the third DVR in Rhodobacter sphaeroides, which has no bciB gene. COR genes derived from other groups of anoxygenic photosynthetic bacteria and introduced into the double mutant all complement the organism and produce normal bacteriochlorophyll a |
-, 736444 |
| 1.3.1.75 | malfunction |
single mutants with deleted BciA or COR show production of the C8 ethyl group pigments, whereas the double mutant accumulates 8-vinyl-chlorophyllide, indicating that there is no enzyme other than BciA and COR functioning as the third DVR in Rhodobacter sphaeroides, which has no bciB gene. COR genes derived from other groups of anoxygenic photosynthetic bacteria and introduced into the double mutant all complement the organism and produce normal bacteriochlorophyll a, pigment compositions of wild-type and mutant strains, overview |
-, 736444 |
