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. 1972 Jul;128(3):647–654. doi: 10.1042/bj1280647

Adenosine 5′-pyrophosphate sulphurylase in baker's yeast

C A Adams 1, D J D Nicholas 1
PMCID: PMC1173816  PMID: 4564258

Abstract

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.

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Selected References

These references are in PubMed. This may not be the complete list of references from this article.

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