The ribulose bisphosphate carboxylase/oxygenase of Prochlorothrix hollandica: purification, subunit structure and partial N-terminal sequence analysis of the large subunit.

Ribulose-1, 5-Bisphosphate Carboxylase/Oxygenase Gene Sequencing in Taxonomic Delineation of Padina Species in theNorthern Coast of the Persian Gulf, (IRAN)

Taxonomic study of the genus Padina (Dictyotales, Phaeophyceae) from the Persian Gulf coast was conducted based on morphology and molecular phylogenetic analyses using chloroplast encoded large subunit RuBisCo (rbcL) gene sequences. Detailed descriptions of each species found in this study are described. Several morphological characters, such as number of cell layers composing the thallus, pr...

Post-translational modifications in the large subunit of ribulose bisphosphate carboxylase/oxygenase.

Two adjacent N-terminal tryptic peptides of the large subunit of ribulose bisphosphate carboxylase/oxygenase [3-phospho-D-glycerate carboxy-lyase (dimerizing), EC 4.1.1.39] from spinach, wheat, tobacco, and muskmelon were removed by limited tryptic proteolysis. Characterization by peptide sequencing, amino acid composition, and tandem mass spectrometry revealed that the N-terminal residue from ...

Reaction-intermediate analogue binding by ribulose bisphosphate carboxylase/oxygenase causes specific changes in proteolytic sensitivity: the amino-terminal residue of the large subunit is acetylated proline.

Trypsin rapidly inactivated the catalytic activities of spinach ribulose bisphosphate carboxylase/oxygenase [3-phospho-D-glycerate carboxy-lyase (dimerizing), EC 4.1.1.39], but the stoichiometry of binding of the reaction-intermediate analogue carboxyarabinitol bisphosphate was only slightly reduced after proteolysis. Electrophoretic analysis indicated that several forms of the large subunit we...

Isolated Spinach Ribulose-1,5-Bisphosphate Carboxylase/Oxygenase Large Subunit εN- Methyltransferase and Method of Inactivating Ribulose-1,5-Bisphosphatase Carboxylase/ Oxygenase Large Subunit εN-Methyltransferase Activity

Preliminary structural studies of ribulose-1,5-bisphosphate carboxylase/oxygenase from Rhodospirillum rubrum.

Ribulose-1,5-bisphosphate carboxylase/oxygenase (EC 4.1.1.39) from Rhodospirillum rubrum has been crystallized in a form that is suitable for structural studies by x-ray diffraction. The asymmetric unit of the crystal contains one dimeric enzyme molecule of molecular mass 101,000 Da. The enzyme was activated prior to crystallization and is presumed to be in the CO2-activated state in the crysta...