EC Number   |
General Information |
Reference |
|---|
   1.3.7.5 | evolution |
Acaryochloris marina strain 11017 evolved to utilize specific PcyA enzymes for sensing wide range of spectrum upon both PCB and 181/182-DHBV binding and harvesting short-wavelength orange light upon only PCB binding. Phycocyanin a from Acaryochloris marina strain 11017 binds only phycocyanobilin (PCB) but not 181/182-DHBV |
-, 763021 |
| 1.3.7.5 | evolution |
Acaryochloris marina strain 11017 evolved to utilize specific PcyA enzymes for sensing wide range of spectrum upon both PCB and 181/182-DHBV binding and harvesting shortwavelength orange light upon only PCB binding. Phycocyanin a from Acaryochloris marina strain 11017 binds only phycocyanobilin (PCB) but not 181/182-DHBV |
-, 763021 |
| 1.3.7.5 | evolution |
comparison and discrimination of two bilin reductase families in bilin amide usage for photoconversions of BV-type and phytobilin-type phytochromes, mechanistic differences, overview |
-, 724287 |
| 1.3.7.5 | evolution |
phycocyanobilin:ferredoxin oxidoreductase (PcyA) is a member of the ferredoxin-dependent bilin reductase (FDBR) family |
762932 |
| 1.3.7.5 | evolution |
synthesis of linear tetrapyrrole chromophores in cyanobacteria, algae, and plants, ooverview |
-, 725252 |
| 1.3.7.5 | evolution |
the enzyme is a member of the ferredoxin-dependent biliverdin reductase (FDBR) family |
724131 |
| 1.3.7.5 | malfunction |
because PcyA and PebA, EC 1.3.7.6/1.3.7.3, utilize the same substrate, biliverdin IXalpha, severe overexpression of pebA can limit the availability of phycocyanobilin, which appears to be required for viability when cells are grown in continuous light |
-, 725252 |
| 1.3.7.5 | malfunction |
both the pcya1-1 mutant with the C-terminal extension of PCYA1 eliminated and efficient knockdown of PCYA1 expression by artificial microRNA exhibit no significant impact on algal phototrophic growth and photosynthetic proteins accumulation, indicating that the conserved FDBR domain is sufficient and minimally required for bilin biosynthesis and functioning. Chlamydomonas PCYA1 uniquely interacts with light-dependent protochlorophyllide oxidoreductase LPOR (protochlorophyllide reductase, EC 1.3.1.33) but not with ferredoxin:protochlorophyllide reductase DPOR (EC 1.3.7.7). The CTE domain of PCYA1 is dispensable for phototrophic growth and photosynthetic proteins accumulation |
-, 763107 |
| 1.3.7.5 | metabolism |
Acaryochloris marina strain 11017 exceptionally encodes two PcyA homologues, AmPcyAc and AmPcyAp. The enzymes AmPcyAc and AmPcyAp show completely different kinetics especially for 181/182-DHBV accumulation. High accumulation of 181/182-DHBV for extended periods is observed during the reaction catalyzed by AmPcyAc, whereas 181/182-DHBV is transiently accumulated for a short period during the reaction catalyzed by AmPcyAp. Phycocyanin a from Acaryochloris marina strain 11017 binds only phycocyanobilin (PCB) but not 181/182-DHBV |
-, 763021 |
| 1.3.7.5 | metabolism |
ferredoxin-dependent biliverdin reductase, PCYA1, is a key enzyme involved in the biosynthesis of bilins, mechanism of bilin-mediated regulation of chlorophyll biosynthesis, and regulatory mechanisms of tetrapyrrole biosynthesis in Chlamydomonas reinhardtii, overview |
-, 763107 |
