Catalytic and regulatory properties of sulphur metabolizing enzymes in cyanobacterium <i style="">Synechococcus elongatus</i> PCC 7942

Abstract

<i style="">Synechococcus elongatus</i> PCC 7942 was able to grow with several S sources. The sulphur metabolizing enzymes <i style="">viz</i>. ATP sulphurylase, cysteine synthase, thiosulphate reductase and L- and D-cysteine desulphydrases were regulated by sulphur sources, particularly by sulphur amino acids and organic sulphate esters. Sulphur starvation reduced ATP sulphurylase and cysteine synthase whereas reduced glutathione appreciated Cys degradation activity. With partially purified enzymes apparent <i style="">K</i>m values for sulphate, ATP, D- and L-Cys, thiosulphate, sulphide and <i style="">O</i>-acetyl serine were in a range of 12-50 µ<i style="">M</i>. <i style="">p</i>-Nitrophenyl sulphate inhibited ATP sulphurylase competitively. Met was a feedback inhibitor of several key enzymes.