Comparative studies of ribulose-1,5-biphosphate carboxylase/oxygenase from Alcaligenes eutrophus H16 cells, in the active and CABP-inhibited forms.
RuBisCO (D-ribulose-1,5-biphosphate carboxylase/oxygenase; EC 4.1.1.39) has been isolated from the autotrophic hydrogen-oxidizing bacterium Alcaligenes eutrophus H16. Combining photon correlation and sedimentation analysis transport parameters of the enzyme were investigated in the active, (E.CO2.Mg2+) as a ternary complex, and inactive state, (E.CO2.Mg2+.CABP) as a quaternary complex, where RuBisCO is complexed with the transition state analogue CABP (2-C-carboxy-D-arabinitol-1,5-biphosphate). Within experimental error, no difference has been detected between the diffusion and sedimentation coefficients (D020,w = 2.72(+/- 0.07) x 10(-7) cm2 s-1, s020,w = 17.8(+/- 0.5)S) of active and CABP-complexed enzyme thus leading to the conclusion that the molecule, at least in solution, does not assume a different conformation when complexed with CABP.
Choe
H W
HW
Institut für Kristallographie, Freie Universitat Berlin, F.R.G.
Georgalis
Y
Y
Saenger
W
W
D000421:Alcaligenes / Q000201:enzymology*; D001426:Bacterial Proteins / Q000378:metabolism; D001692:Biological Transport; D010428:Pentosephosphates / Q000378:metabolism; D012273:Ribulose-Bisphosphate Carboxylase / Q000378:metabolism*; D013402:Sugar Alcohols / Q000378:metabolism
D001426:Bacterial Proteins; D010428:Pentosephosphates; D013402:Sugar Alcohols; C032687:2-carboxyarabinitol 1,5-biphosphate; D012273:Ribulose-Bisphosphate Carboxylase