EC Number   |
General Information |
Reference |
|---|
   1.3.7.7 | malfunction |
a strain lacking DPOR contains about 25% of the wild-type level of photosystems PSII and PSI when cultivated under light-activated heterotrophic growth conditions. Deletion of the chlL gene abolishes activity of the DPOR enzyme. Absence of the chlL gene causes a further 20% decrease in Chl content and therefore the resulting (pCER:por)/Dpor/DchlL strain termed SynPORreg reaches only 60-70% of Chl content present in wild-type |
726255 |
| 1.3.7.7 | metabolism |
chlorophyll biosynthesis is catalyzed by two multi subunit enzymes; a light-dependent and a light-independent protochlorophyllide oxidoreductase |
725926 |
| 1.3.7.7 | evolution |
cyanobacteria, algae, bryophytes, pteridophytes and gymnosperms use an additional, light-independent enzyme dubbed dark-operative Pchlide oxidoreductase for chlorophyll biosynthesis, besides a light-dependent enzyme, mechanisms of protochlorophyllide a reduction in photosynthetic organisms, ooverview |
726526 |
| 1.3.7.7 | evolution |
cyanobacteria, algae, bryophytes, pteridophytes and gymnosperms use an additional, light-independent enzyme dubbed dark-operative Pchlide oxidoreductase for chlorophyll biosynthesis, besides a light-dependent enzyme, mechanisms of protochlorophyllide a reduction in photosynthetic organisms, overview |
726526 |
| 1.3.7.7 | more |
dark-grown seedlings of Pinus mugo accumulate chlorophyll and its precursor protochlorophyllide |
726104 |
| 1.3.7.7 | more |
dark-grown seedlings of Pinus sylvestris accumulate chlorophyll and its precursor protochlorophyllide |
726104 |
| 1.3.7.7 | physiological function |
DPOR is a determinant enzyme for greening ability in the dark |
713252 |
| 1.3.7.7 | physiological function |
DPOR performs reduction of the C17-C18 double bond of protochlorophyllide to form chlorophyllide a, the direct precursor of chlorophyll a in a light-independent, dark-operative way of action |
-, 713102 |
| 1.3.7.7 | physiological function |
DPOR plays a key role in the ability to synthesize chlorophyll in darkness |
712984 |
| 1.3.7.7 | physiological function |
during chlorophyll biosynthesis in photosynthetic bacteria, cyanobacteria, green algae and gymnosperms, dark-operative protochlorophyllide oxidoreductase, a nitrogenase-like metalloenzyme, catalyzes the chemically challenging two-electron reduction of the fully conjugated ring system of protochlorophyllide a. The reduction of the C-17=C-18 double bond results in the characteristic ring architecture of all chlorophylls, thereby altering the absorption properties of the molecule and providing the basis for light-capturing and energytransduction processes of photosynthesis |
726394 |
