Linked Life Data

9650588

Source:http://linkedlifedata.com/resource/pubmed/id/9650588

Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
2
pubmed:dateCreated
1998-7-27
pubmed:abstractText
An exopolyphosphatase (polyPase) with a specific activity of 60 U/mg protein has been purified from the vacuolar sap of Saccharomyces cerevisiae. The molecular mass of the intact enzyme was found to be 245 kDa. It is highly specific towards high-molecular polyphosphates (polyP). The activity with polyP9 is 24% of that with polyP208. The apparent Km for polyP15 and polyP208 hydrolysis is 93 and 2.4 microM, respectively. The enzyme is slightly active with polyP3 and adenosine-5'-tetraphosphate, but does not hydrolyze pyrophosphate, ATP, GTP and p-nitrophenylphosphate. It is stimulated by divalent metal cations. Co2+, the best activator, stimulates it 6-fold. Antibodies that inhibit the cell envelope and cytosol polyPases of S. cerevisiae have no effect on the vacuolar polyPase. The vacuolar polyPase differs from other yeast polyPases in molecular mass, substrate specificity and effects of activators.
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:month
Jun
pubmed:issn
0014-5793
pubmed:author
pubmed:issnType
Print
pubmed:day
12
pubmed:volume
429
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
194-6
pubmed:dateRevised
2006-11-15
pubmed:meshHeading
pubmed:year
1998
pubmed:articleTitle
Purification and properties of exopolyphosphatase isolated from Saccharomyces cerevisiae vacuoles.
pubmed:affiliation
Institute of Biochemistry and Physiology of Microorganisms of the Russian Academy of Sciences, Moscow region, Pushchino.
pubmed:publicationType
Journal Article, Research Support, Non-U.S. Gov't