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Purification and properties of polyphosphatase fromSaccharomyces cerevisiae cytosol

✍ Scribed by Andreeva, Nadezhda; Kulakovskaya, Tatjana; Sidorov, Igor; Karpov, Alexander; Kulaev, Igor


Publisher
John Wiley and Sons
Year
1998
Tongue
English
Weight
144 KB
Volume
14
Category
Article
ISSN
0749-503X

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✦ Synopsis


A homogenous polyphosphatase preparation was obtained from Saccharomyces cerevisiae cytosol with a 3β€’8% yield and 3540-fold purification. The enzyme hydrolysed polyphosphate (polyP) with various chain lengths, including polyP 3 , and split P i off the end of the chain. It was inactive with respect to ATP, PP i , and p-nitrophenylphosphate. Its specific activity with polyP 15 was 283 U/mg protein. The polyphosphatase was a monomeric protein with a molecular mass of 40 kDa. This enzyme was inactive without divalent cations and with Cu 2+ and Ca 2+ . The ability of other divalent cations to activate the enzyme decreased in the following order: Co 2+ >Mn 2+ >Mg 2+ >Zn 2+ . A kinetic model of the hydrolysis of polyP 3 and action of Mg 2+ is proposed. 1998 John Wiley & Sons, Ltd.


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