EC Number   |
General Information |
Reference |
|---|
   1.3.7.7 | more |
dark-grown seedlings of Pinus sylvestris accumulate chlorophyll and its precursor protochlorophyllide |
726104 |
| 1.3.7.7 | more |
some purple bacteria contain Bchl b, and heliobacteria such as Heliobacillus mobilis contain Bchl g, as compared to Chl a and Chl b of higher plants |
726526 |
| 1.3.7.7 | more |
the homodimeric subunit ChlL2 transfers electrons to the corresponding heterotetrameric catalytic subunit (ChlN/ChlB)2, transfer of a single electron from the [4Fe-4S] cluster of ChlL2 onto a second [4Fe-4S] cluster located on (ChlN/ChlB)2 |
725877 |
| 1.3.7.7 | more |
the organism contains another type of Chl, bacteriochlorophyll (Bchl) a, as compared to Chl a and Chl b of higher plants |
726526 |
| 1.3.7.7 | more |
the organism contains another type of Chl, bacteriochlorophyll (Bchl) a, as compared to Chl a and Chl b of higher plants. Residue Asp36 is not necessary for enzyme complex formation but for enzyme activity. Subunit BchB possesses a unique C-terminal region consisting of approximately 100 amino acid residues (Phe422-Arg525), which is probably important for protochlorophyllide reduction |
726526 |
| 1.3.7.7 | more |
transient protein-protein interaction of ChlL2 and (ChlN/ChlB)2 is essential for the ATP-dependent electron transfer processes catalyzed by DPOR. Efficient octameric (ChlN/ChlB)2(ChlL2)2 enzyme complex formation required the presence of protochlorophyllide. Complete ATP hydrolysis is a prerequisite for intersubunit electron transfer |
725412 |
| 1.3.7.7 | more |
upon complex formation, substantial ATP-dependent conformational rearrangements of L2 trigger the protein-protein interactions with (NB)2 as well as the electron transduction via redox-active [4Fe-4S] clusters, dynamic interplay between L2 and (NB)2. Asp155 is responsible for positioning and/or activating a specific water molecule for the subsequent ATP hydrolysis, whereas Lys37 of the P-loop possibly assists the release of gamma-phosphate upon ATP hydrolysis |
726394 |
| 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 |
