Sawhney S K, Nicholas D J
Biochem J. 1977 Apr 15;164(1):161-7. doi: 10.1042/bj1640161.
Production of adenosine 5'-[35S]sulphatophosphate by a partially purified ATP sulphurylase from Anabaena cylindrica was inhibited by AMP, ADP and P1. Decreases in enzyme activity in the presence of these inhibitors were reversed by increasing the concentrations of ATP. The adenine nucleotides inhibited the enzyme competitively with respect to ATP. In the presence of P1, ATP showed a positive co-operative effect on enzyme activity. The inhibition by P1 was enhanced by increasing concentrations of MG2+. The effects of the adenine nucleotides and the interaction of P1 and Mg2+ on ATP sulphurylase activity are discussed in relation to the regulation of sulphate assimilation via the energy metabolism of the alga.
来自圆柱鱼腥藻的部分纯化的ATP硫酸化酶生成5'-[35S]硫酸磷酸腺苷的过程受到AMP、ADP和P1的抑制。在这些抑制剂存在的情况下,酶活性的降低可通过增加ATP浓度来逆转。腺嘌呤核苷酸相对于ATP对该酶具有竞争性抑制作用。在P1存在的情况下,ATP对酶活性表现出正协同效应。P1的抑制作用会随着Mg2+浓度的增加而增强。结合藻类能量代谢对硫酸盐同化作用的调节,讨论了腺嘌呤核苷酸的作用以及P1和Mg2+对ATP硫酸化酶活性的相互作用。