Adenosine 5'-pyrophosphate sulphurylase in baker's yeast.

ADP sulphurylase from baker's yeast was purified and its properties were studied. The enzyme is very heat-labile and its activity shows linear kinetics over narrow ranges of time and protein concentration. It is not activated by metals and is inhibited by thiol-reactive compounds. The enzyme, which replaces inorganic sulphate in adenosine 5'-sulphatophosphate with P(i) to yield ADP, also catalyses an exchange of P(i) into ADP. Kinetic studies show that the enzyme has a high affinity for adenosine 5'-sulphatophosphate, although concentrations in excess of 1.0mm are inhibitory. However, the kinetics for P(i) are more complex and the enzyme is not inhibited by P(i) up to 20.0mm.