EC Number   |
General Information |
Reference |
|---|
   1.3.7.13 | 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 |
| 1.3.7.13 | 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 Genomic comparison reveals that BciB had been replaced by BciA during evolution of the marine cyanobacterium Synechococcus, and coincided with replacement of Fe-superoxide dismutase (SOD) with Ni-SOD.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 |
| 1.3.7.13 | 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 |
| 1.3.7.13 | evolution |
two unrelated classes of C8-vinyl reductase are known to exist, BciA and BciB |
744270 |
| 1.3.7.13 | 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 |
| 1.3.7.13 | metabolism |
bacteriochlorophyll a (BChl) is an essential pigment for anoxygenic photosynthesis. In late steps of the BChl biosynthesis, the C8 vinyl group and C7=C8 double bond of 8-vinyl chlorophyllide a (8 V-Chlide) are reduced by a C8 vinyl reductase (8VR), BciA (EC 1.3.1.75) or BciB and a nitrogenase-like enzyme, chlorophyllide a oxidoreductase (COR, EC 1.3.7.15), respectively, to produce 3-vinyl-bacteriochlorphyllide a |
762912 |
| 1.3.7.13 | metabolism |
during chlorophyll synthesis, chlorophyllide with a vinyl group at position 8 is produced as a precursor. The divinyl chlorophyllide has two vinyl groups, at positions 3 and 8, respectively. The vinyl group at position 8 is reduced to an ethyl group by 8-vinyl (8V) reductase to form chlorophyllide, which is then esterified with phytyl diphosphate to give chlorophyll. In photosynthetic bacteria, photosynthesis-related genes form clusters. The BciB gene encodes the 8V reductase. BciB contains an [Fe-S] cluster, has FAD as a cofactor, and uses ferredoxin (Fd) as a reductant |
-, 762685 |
| 1.3.7.13 | metabolism |
during chlorophyll synthesis, chlorophyllide with a vinyl group at position 8 is produced as a precursor. The divinyl chlorophyllide has two vinyl groups, at positions 3 and 8, respectively. The vinyl group at position 8 is reduced to an ethyl group by 8-vinyl (8V) reductase to form chlorophyllide, which is then esterified with phytyl diphosphate to give chlorophyll. In photosynthetic bacteria, photosynthesis-related genes form clusters. The BciB gene encodes the 8V reductase. BciB contains an [Fe-S] cluster, has FAD as a cofactor, and uses ferredoxin (Fd) as a reductant. BciB of Synechocystis PCC6803, a model cyanobacterium without chlorophyll b, exhibits both 7-hydroxymethyl chlorophyll a reductase and 8V reductase activity. Synechocystis BciB can convert chlorophyll b to chlorophyll a, but in Synechocystis, such activity has no impact on its metabolism, since it does not synthesize chlorophyll b |
762685 |
| 1.3.7.13 | metabolism |
the enzyme is involved the chlorophyll biosynthetic pathways of oxygenic photosynthetic organisms. At the later steps of chlorophyll biosynthesis, 3,8-divinyl-chlorophyllide (Chlide) a is converted to monovinyl (MV)-Chlide a by DVR. Involvement of DVR in Chl c biosynthesis |
746037 |
| 1.3.7.13 | metabolism |
the majority of (B)Chls utilized for light-harvesting carry an ethyl group at the C8 position (8E) of the macrocycle. This group is produced by the reduction of a vinyl group (8V), catalysed by an 8V reductase, 8VR, resulting in the production of an 8E pigment |
744270 |
