Results 211 to 220 of about 28,959 (255)
Reprogramme the E. coli metabolism by engineering a functional carbon-fixation pathway
Chen Y +8 more
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Ribulose-1,5-bisphosphate carboxylase-oxygenase.
Annual Review of Biochemistry, 1983INTRODUCTION 379 Role in Photosynthesis 379 Enzyme Reaction 380 MOLECULAR PROPERTIES .... . . . . . . . . . . .. . . . . . . . . . . . . . . . . . . . . . . . . . . . . . ... . . ... . . . .. 381 Native Enzyme 381 Subunit Structure 382 Is Bound Capper Involved? 384 CATALYTIC PROPERTIES .... . .....
H. Miziorko, G. Lorimer
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Regulation of Ribulose 1,5-Bisphosphate Carboxylase/Oxygenase Activity
Annual Review of Plant Physiology and Plant Molecular Biology, 1992INTRODUCTION . . . . . . ... .... .. .... ..... . ... 416 BIOCHEMICAL BASIS FOR INTRINSIC CHANGES IN ACTIVITy. .. .. . . .. . . . . . . . . . . 416 Influence of Sugar Phosphates . .. . . . . . . . . . . . . ... ... ... .. . ... . . . . . . . ... 417 EARLY EVIDENCE OF LIGHT REGULATION....... .. .. .. . . ... .... .. . .. . . ..
A. Portis
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Biochemistry, 1982
The primary deuterium kinetic isotope effect for the reaction of [3-2H]ribulose 1,5-bisphosphate with CO2 in the reaction catalyzed by ribulose-1,5-bisphosphate carboxylase has been determined. By use of highly purified substrates containing less than 0.13% of the C-3 epimer xylulose 1,5-bisphosphate (this material is known to be a potent competitive ...
J M, Sue, J R, Knowles
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The primary deuterium kinetic isotope effect for the reaction of [3-2H]ribulose 1,5-bisphosphate with CO2 in the reaction catalyzed by ribulose-1,5-bisphosphate carboxylase has been determined. By use of highly purified substrates containing less than 0.13% of the C-3 epimer xylulose 1,5-bisphosphate (this material is known to be a potent competitive ...
J M, Sue, J R, Knowles
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Ribulose-1,5-bisphosphate carboxylase/oxygenase from parsley
Biochemical and Biophysical Research Communications, 1978Abstract Ribulose-1,5-bisphosphate carboxylase/oxygenase from parsley leaves was purified by Sepharose 6B gel filtration at pH 8.3 as a single, colorless peak containing both activities. Approximately 0.2 g atom copper per mole enzyme was detected by atomic absorption spectroscopy, but this copper was not detectable by EPR spectrometry.
S D, McCurry +4 more
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Planta, 1991
Mutagenesis in vitro of the gene encoding the large subunit of ribulose-1,5-bisphosphate carboxylase/ oxygenase (EC 4.1.1.39) from Anacystis nidulans was used to generate novel enzymes. Two conserved residues, threonine 4 and lysine 11 in the N-terminus were changed. The substitution of threonine 4 with serine or valine had little effect on the kinetic
Kettleborough, C. A. +3 more
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Mutagenesis in vitro of the gene encoding the large subunit of ribulose-1,5-bisphosphate carboxylase/ oxygenase (EC 4.1.1.39) from Anacystis nidulans was used to generate novel enzymes. Two conserved residues, threonine 4 and lysine 11 in the N-terminus were changed. The substitution of threonine 4 with serine or valine had little effect on the kinetic
Kettleborough, C. A. +3 more
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Ribulose 1,5-bisphosphate carboxylase and phosphoribulokinase in Prochloron
Planta, 1983Cell-free extracts of Prochloron didemni were assayed for ribulose 1,5-bisphosphate (RuBP) carboxylase (EC 4.1.1.39) and phosphoribulokinase (EC 2.7.1.19), two key enzymes in the reductive pentose-phosphate cycle. In an RuBP-dependent reaction, the production of two molecules of 3-phosphoglycerate per molecule of CO2 fixed was shown ...
M A, Berhow, B A, McFadden
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Small subunit contacts in ribulose-1,5-bisphosphate carboxylase
Biochemistry, 1978The arrangement of subunits of ribulosebisphosphate carboxylase in solution has been studied by exposing the enzyme to the cross-linking agents tetranitromethane, dimethyl suberimidate, and dimethyl adipimidate, and the cleavable cross-linking agent, methyl 4-mercaptobutyrimidate followed by gel electrophoresis in the presence of dodecyl sulfate.
H, Roy +4 more
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Crystalline Ribulose 1,5-Bisphosphate Carboxylase-Oxygenase from Spinach
Science, 1979Spinach fraction I protein (ribulose 1,5-bisphosphate carboxylase-oxygenase, E.C. 4.1.1.39) was crystallized on both an analytical and a preparative scale by vapor diffusion with polyethylene glycol (molecular weight, 6000) used as the precipitant. The identity of the crystalline material with fraction I protein was shown by gel electrophoresis in the ...
S, Johal, D P, Bourque
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