Q T=H0 W~ ~a p]j J,Yq s`t.Z ~.RV `tf/,i? @Ja'J d'5 G.9U0 J?X: 0 [u'0 ^g]1 Fjb 7h` 7q+ t(3+ X[O" ym^ W* G8k.i;, 9E4 x,M a0 0c7 ^+Q.pQg mInhibitory effect of sulfate on the hydrolysis of isocitrate by mitochondrial oxalosuccinate lyase from Escherichia coli.
The kinetic properties of oxalosuccinate lyase from E. coli (EC 4.1.3.2) have been studied. This enzyme is inhibited by SO4(2-) or SO3(-) in the presence of ATP (Ure I (Sulfate Activation of Isocitrate Lyase from Escherichia coli), S. K. Akhtar, and B. D. Carrell, Microbiology, 143, 1855-1859, 1997). In this paper we have studied the effect of sulfate and phosphate anions on the enzymatic hydrolysis of isocitrate by the oxalosuccinate lyase. We found that the sulfate anion has a potent inhibitory effect on the enzyme activity, while phosphates are not inhibitory. A mechanism 3125841983
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