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Cloning of the gene for monogalactosyldiacylglycerol synthase and its evolutionary origin.
The deduced amino acid sequence of the MGDG synthase cDNA showed homology with MurG of Bacillus subtilis and E. coli, which encode a glycosyltransferase catalyzing the last step of peptidoglycan synthesis in bacteria, which implies that the machinery of chloroplast membrane biosynthesis is evolutionarily derived from that of cell wall biosynthesis in bacteria. Expand
Distribution and physiology of aerobic bacteria containing bacteriochlorophyll a on the East and west coasts of australia.
Aerobic heterotrophic bacteria containing bacteriochlorophyll were isolated from specimens from a wide variety of marine environments on the west and east coasts of Australia and some strains showed denitrifying activity, and the optimal salinity for bacterial growth varied between strains. Expand
Enzymatic Conversion of Pheophorbide a to the Precursor of Pyropheophorbide a in Leaves of Chenopodium album
It appears that the enzyme catalyzes the demethylation of the carbomethoxy group at C-13 2 of pheophorbide a by hydrolysis to yield methanol and the precursor, C-132carboxyl-pyropheoph orbide a, which is converted to pyropheophorbid a by spontaneous decarboxylation. Expand
Re-examination of Mg-dechelation reaction in the degradation of chlorophylls using chlorophyllin a as a substrate
The Mg-dechelating activity of extracts of Chenopodium album (goosefoot) was investigated using an artificial substrate, chlorophyllin a, and the purified Mm-releasing protein showed neither peroxidase activity nor absorption bands in the visible region, and this indicates that the M g-re releasing protein is clearly distinct from horseradish peroxIDase, which is a heme-containing protein. Expand
Conversion of chlorophyllide to pheophorbide by Mg-dechelating substance in extracts of Chenopodium album
Pheophorbide formation in chlorophyll metabolism was studied using extracts of Chenopodium album. A new substance catalyzing the conversion of chlorophyllide a to pheophorbide a was found in theExpand
Characterization and Cloning of the Chlorophyll-Degrading Enzyme Pheophorbidase from Cotyledons of Radish1
Among 12 substrates tested, both enzymes were extremely specific for Pheids of the dihydroporphyrin and tetrahydropoiryrin types, indicating that they are responsible for the formation of these PyroPheids. Expand
Comparison of three Chlamydomonas strains which show distinctive oxidative stress tolerance.
The levels of intracellular free proline, which is supposed to ameliorate oxidative stress, were several tens of times higher in the marine Chlamydomonas strains than in C. reinhardtii, indicating that APX activity potentially contributes to the oxidative stress tolerance in ChlamYdom onas. Expand
Molecular cloning and characterization of a senescence-induced tau-class Glutathione S-transferase from barley leaves.
Senescence-induced tau-class GST (SIGST) in senescent leaves of barley is found and DNA sequence analysis shows that the cloned SIGST had only one base different from the barley embryo GST, ECGST, which indicates that SIGST is classified into the plant-specific tau class. Expand
Purification and Characterization of Two Isozymes of Chlorophyllase from Mature Leaves of Chenopodium album
Chlorophyllase (Chlase) was purified from mature leaves of Chenopodium album, and its enzymatic properties were investigated, and the optimum pH and K m values of these two Chlases were similar. Expand
A transcription factor with a leucine-zipper motif involved in light-dependent inhibition of expression of the puf operon in the photosynthetic bacterium Rhodobacter sphaeroides.
A trans-acting protein (SPB) that binds to the promoter region of the puf operon, which encodes the apoproteins of light-harvesting complex I and the reaction center is purified and cloned and indicated that spb was constitutively and monocistronically transcribed in R. sphaeroides, irrespective of growth conditions. Expand