Activation of sulphate in Anabaena cylindrica

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Abstract
Crude cell-free extracts of Anabaena cylindrica synthesized adenosine-5′-phosphosulphate (AP35S) and 3′-phosphoadenosine-5′-phosphosulphate (PAP35S) from 35SO4 2- in the presence of Mg2+, ATP and inorganic pyrophosphatase. Maximum AP35S and PAP35S were produced at pH 7.15 and 8.05, respectively. APS kinase was detected in the supernatant of crude cell-free extracts by a spectrophotometric procedure. ATP-Sulphurylase had an absolute requirement for Mg2+ and less than 30% AP35S was formed when Mg2+ was replaced by either Mn2+ or Co2+. Nucleotide triphosphates other than ATP and 2′-deoxyATP were ineffective in this reaction. Maximum enzyme activity was observed at equimolar concentrations of Mg2+ and ATP and excess of either of these was inhibitory. Other nucleotide triphosphates, like GTP, UTP, CTP, TTP, ITP, or 2′-deoxyATP also inhibited the enzyme activity. Inhibition by GTP was competitive with respect to ATP. ATP-sulphurylase activity was not affected by cysteine, methionine or glutathione.