EC Number   |
General Information |
Reference |
|---|
    1.3.1.33 | malfunction |
RNAi based simultaneous silencing of all forms of light-dependent NADPH:protochlorophyllide oxidoreductase genes results in the accumulation of protochlorophyllide in tobacco |
741187 |
| 1.3.1.33 | metabolism |
ferredoxin-dependent biliverdin reductase, PCYA1 (EC 1.3.7.5), 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. Chlamydomonas PCYA1 uniquely interacts with light-dependent protochlorophyllide oxidoreductase LPOR (protochlorophyllide reductase, EC 1.3.1.33) via its FDBR domain, but not with ferredoxin:protochlorophyllide reductase DPOR (EC 1.3.7.7). This interaction is specific to Chlamydomonas since the Arabidopsis thaliana homologous proteins do not interact with each other, yeast two-hybrid and pull down assay analyses of protein-protein interaction |
-, 763107 |
| 1.3.1.33 | metabolism |
the enzyme allows for the rapid formation of chlorophyll after illumination while avoiding photodamage. The formation of protochlorophyllide-enzyme(LPOR) complexes is an initial step of etioplast development. the formation of pigment-LPOR complexes in prolamellar bodies is essential for the rapid and safe conversion of etioplasts to chloroplasts during the dark-to-light transition |
758042 |
| 1.3.1.33 | metabolism |
the nonhomologous enzymes, the light-independent protochlorophyllide reductase (DPOR, EC 1.3.7.7) and the light-dependent protochlorophyllide oxidoreductase (LPOR), catalyze the reduction of protochlorophyllide (Pchlide) to chlorophyllide (Chlide) in the penultimate step of biosynthesis of chlorophyll (Chl) required for photosynthetic light absorption and energy conversion. The two enzymes differ with respect to the requirement of light for catalysis and oxygen sensitivity. Stereospecific reduction of the D ring of Pchlide (protochlorophyllide) to Chlide (chlorophyllide) catalyzed by light-independent protochlorophyllide a reductase (DPOR) occurs in anoxygenic phototrophs and photosynthetic eukaryotes except most gnetophytes and all angiosperms. The reduction of the D ring Pchlide to Chlide is brought about by light-dependent protochlorophyllide oxidoreductase (LPOR) in light in oxygenic phototrophs. The reduction of Chlide a to Bchlide a in anoxygenic phototrophs is catalyzed by the stereospecific reduction of ring B by chlorophyllide a oxidoreductase (COR, EC 1.3.7.15). Both MV Pchlide and DV Pchlide are phototransformed to MV Chlide a and DV Chlide a, respectively, by light-dependent Pchlide oxidoreductase (LPOR) in oxygenic phototrophs. In the absence of light, anoxygenic photosynthetic bacteria and oxygen evolving phototrophs catalyze Pchlide reduction by the light-independent Pchlide oxidoreductase (DPOR). The DV Chlide a is immediately converted to MV Chlide a by DV reductase |
-, 763678 |
| 1.3.1.33 | more |
a clear distinction of the DPOR and LPOR functions cannot be made as oxygen-sensitive DPOR, which is typically inactivated in the increased oxygen concentration, remains functional in Dinoroseobacter shibae. The TFT motif fragment from LPOR and BchL/ChlL is found to be absent from other SDR proteins and has no similarity with the Fe protein of nitrogenase NifH. The TFT motif is previously found to be present between the NAA motif,which is one of the NADPH binding sites, and the catalytic YxxxK motif. The mutation of conserved residues in TFT motif results in complete inhibition of the LPOR activity |
-, 763678 |
| 1.3.1.33 | more |
the TFT motif fragment from LPOR and BchL/ChlL is found to be absent from other SDR proteins and has no similarity with the Fe protein of nitrogenase NifH. The TFT motif is previously found to be present between the NAA motif, which is one of the NADPH binding sites, and the catalytic YxxxK motif. The mutation of conserved residues in TFT motif results in complete inhibition of the LPOR activity |
763678 |
| 1.3.1.33 | more |
the TFT motif fragment from LPOR and BchL/ChlL is found to be absent from other SDR proteins and has no similarity with the Fe protein of nitrogenase NifH. The TFT motif is previously found to be present between the NAA motif,which is one of the NADPH binding sites, and the catalytic YxxxK motif. The mutation of conserved residues in TFT motif results in complete inhibition of the LPOR activity |
763678 |
| 1.3.1.33 | physiological function |
in leaf of etiolated seedlings, prolamellar bodies are smaller in the etioplasts of mutant plants than in the wild type. In field-grown seedlings, the chloroplasts in the light-green sectors of mutant leaves exhibit decreased thylakoid stacking with a few plastglobules. PorB is essential for both prolamellar bodies and photoactive protochlorophyllide formation in dark conditions for light-dependent chlorophyll synthesis |
743467 |
| 1.3.1.33 | physiological function |
isoform POR1 supports photoacclimation, whereas isoform POR2 is responsible for daily chlorophyll synthesis |
741255 |
| 1.3.1.33 | physiological function |
key enzyme of chlorophyll biosynthesis in angiosperms. Photoenzyme, which catalyzes the light-activated trans-reduction of the C17-C18 double bond of the porphyrin ring of protochlorophyllides. Due to the light requirement, dark-grown angiosperms cannot synthesize chlorophyll |
763675 |
