saturated dicarboxylic acids with the exception of oxalate, are less inhibitory as the molecular weight increases. Compounds with two cis-carboxyl groups are much more inhibitory than the corresponding trans-isomers
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recombinant enzyme at 2.2 A resolution. C-terminal domain present in all other members of fumarase II family is missing and enzyme contains an Arg residue as opposed to Trp in the active site. Activation of the carboxylic nucleophile by a hydrophobic environment is not required for lactonization
hanging-drop vapor-diffusion method, 2.6 A resolution, symmetric of hexagonal space group P6(5) with unit cell parameters: a = b = 231.52 A, c = 78.46 A, alpha = beta = 90°, gamma = 120°. There are four PpCMLE molecules, forming a homotetramer, in the asymmetric unit; hanging drop vapour diffusion method with 12-18% PEG8000, 5 mM dithiothreitol, and 40 mM sodium phosphate (pH 7.3)
Eulberg, D.; Lakner, S.; Golovleva, L.A.; Schlömann, M.
Characterization of a protocatechuate catabolic gene cluster from Rhodococcus opacus 1CP: evidence for a merged enzyme with 4-carboxymuconolactone-decarboxylating and 3-oxoadipate enol-lactone-hydrolyzing activity