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4.1.1.39: ribulose-bisphosphate carboxylase

This is an abbreviated version!
For detailed information about ribulose-bisphosphate carboxylase, go to the full flat file.

Word Map on EC 4.1.1.39

Reaction

2 3-phospho-D-glycerate + 2 H+ =

D-ribulose 1,5-bisphosphate
+
CO2
+
H2O

Synonyms

AF_1638, archaeal Rubisco, barley rubisco, Carboxydismutase, CbbL-1, CbbL-2, CbbL1 protein, CbbL2 protein, CbbM, CbbS-1, CbbS-2, D-ribulose 1,5-bisphosphate carboxylase/oxygenase, D-Ribulose 1,5-diphosphate carboxylase, D-Ribulose-1,5-bisphosphate carboxylase, D-ribulose-1,5-bisphosphate carboxylase/oxygenase, Diphosphoribulose carboxylase, form I RubisCO, Form II Rubisco, form III ribulose-1,5-bisphosphate carboxylase/oxygenase, Galdieria Rubisco, green-like type rubisco, LESS17, MbR, Pk-Rubisco, PSS15, PSSU1, Rbc, rbcL, RbcL2, rbcLS, rbcS, RbcS-T, rbcS1, red-type form I RuBisCO, ribulose 1, 5-bisphosphate carboxylase/oxygenase, ribulose 1,5 bisphosphate carboxylase/oxygenase, Ribulose 1,5-bisphosphate carboxylase, Ribulose 1,5-bisphosphate carboxylase-oxygenase, Ribulose 1,5-bisphosphate carboxylase/oxygenase, Ribulose 1,5-diphosphate carboxylase, Ribulose 1,5-diphosphate carboxylase/oxygenase, ribulose bisphosphate carboxylase, Ribulose bisphosphate carboxylase large chain, Ribulose bisphosphate carboxylase-oxygenase, ribulose bisphosphate carboxylase/oxygenase, ribulose bisphosphate carboxylase/oxygenase large subunit, Ribulose diphosphate carboxylase, Ribulose diphosphate carboxylase/oxygenase, ribulose-1, 5-bisphosphate carboxylase/oxygenase, ribulose-1,5-bisphosphate (RuBP) carboxylase/oxygenase, ribulose-1,5-bisphosphate carboxylase, ribulose-1,5-bisphosphate carboxylase/oxygenase, ribulose-1,5-bisphosphate carboxylase/oxygenase large subunit, ribulose-1,5-bisphosphate carboxylase/oxygenase small subunit, ribulose-bisphosphate carboxylase, ribulose-bisphosphate carboxylase/oxygenase, RLP, Rubisco, RubisCO 1, RuBisCO 2, RubisCO redlike form I, Rubisco small subunit, RuBisCO-like protein, Rubisco-LSU, RubiscoL, RuBP carboxylase, RuBP carboxylase/oxygenase, RuBPC, RuBPcase, RuBPCO, Tk-Rubisco, TK2290, type III ribulose 1,5-bisphosphate carboxylase/oxygenase, type III Rubisco, Water stress responsive proteins 1, 2 and 14

ECTree

     4 Lyases
         4.1 Carbon-carbon lyases
             4.1.1 Carboxy-lyases
                4.1.1.39 ribulose-bisphosphate carboxylase

Crystallization

Crystallization on EC 4.1.1.39 - ribulose-bisphosphate carboxylase

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CRYSTALLIZATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
analysis of the 1.4-A X-ray crystal structure of Chlamydomonas Rubisco reveal that all but one (Glu-92) of the conserved residues are in contact with large subunits and cluster near the amino- or carboxyl-terminal ends of large subunit alpha-helix 8, which is a structural element of the alpha/beta-barrel active site. Small subunit residues Glu-43 and Trp-73 identify a possible structural connection between active site alpha-helix 8 and the highly variable small subunit loop between beta-strands A and B, which can also influence Rubisco CO2/O2 specificity
-
determination of crystal structures of L290F and L290F/A222T mutant enzymes to 2.3 A and 2.05 A resolution, hanging-drop vapor diffusion method at 20°C, crystals belong to space group P2(1). Cell dimensions of L290F: a = 121.0 A, b = 177.7 A, c = 122.7 A, beta = 117.7°. Cell dimensions of L290F/A222T: a = 126.0 A, b = 178.2 A, c = 120.5 A, beta = 120.5 A
-
hanging drop vapour diffusion method using 50 mM HEPES (pH 7.5), 0.05-0.2 M NaCl, 7-12% poly(ethylene glycol) 4000, 10 mM NaHCO3, and 5 mM MgCl2
-
hanging drop vapor diffusion method, in the presence of ammonium sulfate (about 2 M) and 2 mM Mg2+
cryoelectron microscopy is used to produce an 11-A density map of the Rubisco-Rubisco large subunit methyltransferase (RLSMT) complex. The atomic model of the complex, obtained by fitting crystal structures of Rubisco and Rubisco large subunit methyltransferase into the density map, shows that the extensive contact regions between the 2 proteins are mainly mediated by hydrophobic residues and leucine-rich repeats
-
in complex with NADPH, 6-phosphogluconate, or 2-carboxy-D-arabinitol 1,5-bisphosphate, hanging drop vapor diffusion method, using 75 mM HEPES-KOH (pH 7.75 at 20°C), 9% (w/v) polyethylene glycol 4000, and 25% (v/v) glycerol
hanging drop vapor diffusion method, with substrate ribulose 1,5-bisphosphate, using 10-12% (w/v) polyethylene glycol 6000 in 100 mM HEPES pH 7.0
complexed with 2-carboxyarabinitol bisphosphate
-
cryoelectron microscopy is used to produce an 11-A density map of the Rubisco-Rubisco large subunit methyltransferase (RLSMT) complex. The atomic model of the complex, obtained by fitting crystal structures of Rubisco and Rubisco large subunit methyltransferase into the density map, shows that the extensive contact regions between the 2 proteins are mainly mediated by hydrophobic residues and leucine-rich repeats
-
crystal structure of an enzyme complex containing EC 4.1.1.39
-
hanging drop vapor diffusion method, using 100 mM acetate buffer (pH 6.0), 80-100 mM CaCl2, 5-6% (w/v) polyethylene glycol 6,000, and 10% (v/v) 2-methylpentane-2,4-diol
sitting or hanging drop vapor diffusion, space group P3(1)21 or P3(2)21, cell parameters a : b : 233.7 A, c : 93.1 A
-
structure of mutant T289D with substrate analogue 2-carboxyl-D-arabinitol 1,5-bisphosphate, at 2.25 A resolution