Kinetics of activation of l-lactate dehydrogenase from Streptococcus lactis by fructose 1,6-bisphosphate Export

@article{citeulike:2405535, abstract = {1. A lag is observed before the steady state during pyruvate reduction catalysed by lactate dehydrogenase from Streptococcus lactis. The lag is abolished by preincubation of enzyme with the activator fructose 1,6-bisphosphate before mixing with the substrates. The rate constants for the lag phase showed a linear dependence on fructose-1,6-bisphosphate concentration, with a second-order rate constant of 2.0 - 104 M-1 s-1, but were independent of enzyme concentration. 2. Binding of fructose 1,6-bisphosphate produces a decrease in the protein fluorescence of the enzyme. The second-order rate constant for the fluorescence change is twice that for the lag in pyruvate reduction. 3. The results suggest that binding of fructose 1,6-bisphosphate induces a conformational change in the enzyme, producing a form with reduced protein fluorescence and increased activity towards pyruvate reduction.}, author = {Hardman, Michael J. and Crow, Vaughan L. and Cruickshank, Denise S. and Pritchard, Graham G.}, citeulike-article-id = {2405535}, citeulike-linkout-0 = {http://www.blackwell-synergy.com/doi/abs/10.1111/j.1432-1033.1985.tb08636.x}, citeulike-linkout-1 = {http://dx.doi.org/10.1111/j.1432-1033.1985.tb08636.x}, doi = {10.1111/j.1432-1033.1985.tb08636.x}, journal = {European Journal of Biochemistry}, keywords = {16bisphosphate, 16diphosphate, dehydrogenase, fbp, fructose, kinetics, lactate, ldh, streptococcus}, number = {1}, pages = {179--183}, posted-at = {2008-02-21 07:48:26}, priority = {5}, title = {Kinetics of activation of l-lactate dehydrogenase from Streptococcus lactis by fructose 1,6-bisphosphate}, url = {http://dx.doi.org/10.1111/j.1432-1033.1985.tb08636.x}, volume = {146}, year = {1985} }

TY - JOUR ID - citeulike:2405535 L3 - citeulike-article-id:2405535 N2 - 1. A lag is observed before the steady state during pyruvate reduction catalysed by lactate dehydrogenase from Streptococcus lactis. The lag is abolished by preincubation of enzyme with the activator fructose 1,6-bisphosphate before mixing with the substrates. The rate constants for the lag phase showed a linear dependence on fructose-1,6-bisphosphate concentration, with a second-order rate constant of 2.0 - 104 M-1 s-1, but were independent of enzyme concentration. 2. Binding of fructose 1,6-bisphosphate produces a decrease in the protein fluorescence of the enzyme. The second-order rate constant for the fluorescence change is twice that for the lag in pyruvate reduction. 3. The results suggest that binding of fructose 1,6-bisphosphate induces a conformational change in the enzyme, producing a form with reduced protein fluorescence and increased activity towards pyruvate reduction. IS - 1 JF - European Journal of Biochemistry EP - 183 TI - Kinetics of activation of l-lactate dehydrogenase from Streptococcus lactis by fructose 1,6-bisphosphate VL - 146 SP - 179 KW - 16bisphosphate KW - 16diphosphate KW - dehydrogenase KW - fbp KW - fructose KW - kinetics KW - lactate KW - ldh KW - streptococcus AU - Hardman, Michael AU - Crow, Vaughan AU - Cruickshank, Denise AU - Pritchard, Graham PY - 1985/// UR - http://dx.doi.org/10.1111/j.1432-1033.1985.tb08636.x ER -