Adenosine 5′-pyrophosphate sulphurylase in baker's yeast
Keyword(s):
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 Pi to yield ADP, also catalyses an exchange of Pi 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 Pi are more complex and the enzyme is not inhibited by Pi up to 20.0mm.
2016 ◽
Vol 41
(37)
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pp. 16415-16427
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2019 ◽
Vol 22
(06)
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pp. 1599-1606
1981 ◽
Vol 31
(1)
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pp. 290-294
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2014 ◽
Vol 13
(12)
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pp. 3153-3160
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1967 ◽
Vol 132
(2)
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pp. 232-243
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1978 ◽
Vol 253
(7)
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pp. 2392-2399
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