EC Number |
General Information |
Reference |
---|
1.3.7.7 | physiological function |
light-independent protochlorophyllide reductase is required for protochlorophyllide reduction in the dark |
672764 |
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 |
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 is a determinant enzyme for greening ability in the dark |
713252 |
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 | evolution |
the enzyme is involved in the biosynthesis of chlorophylls and bacteriochlorophylls in gymnosperm, ferns, algae, and photosynthetic bacteria |
725877 |
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 | metabolism |
chlorophyll biosynthesis is catalyzed by two multi subunit enzymes; a light-dependent and a light-independent protochlorophyllide oxidoreductase |
725926 |
1.3.7.7 | metabolism |
protochlorophyllide reduction is a key regulatory step in Chl biosynthesis |
726104 |
1.3.7.7 | more |
dark-grown seedlings of Pinus mugo accumulate chlorophyll and its precursor protochlorophyllide |
726104 |