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PredicateObject
rdf:type
lifeskim:mentions
pubmed:dateCreated
1961-12-1
pubmed:abstractText
Sagers, Richard D. (University of Illinois, Urbana), Moshe Benziman, and I. C. Gunsalus. Acetate formation in Clostridium acidiurici: Acetokinase. J. Bacteriol. 82:233-238. 1961.-To define the energy-yielding reaction(s) during fermentation of purines by Clostridium acidi-urici, an eightfold purified acetokinase was obtained by protamine and ammonium sulfate fractionation of crude extracts. Enzyme activity was determined by measuring the disappearance of acetyl phosphate using adenosine diphosphate (ADP) as phosphate acceptor or by following the generation of acetyl phosphate from adenosine triphosphate (ATP) + acetate. The optimal pH for the reaction was observed to be 7.4. K(m) values for acetyl phosphate, ADP, and magnesium ions were shown to be 2.1 x 10(-3)m, 3.2 x 10(-3)m, and 2.4 x 10(-3)m, respectively. Acetyl phosphate disappearance is dependent upon ADP and is stoichiometric with addition of the latter. The acetokinase reaction probably represents the major energy-yielding reaction during purine fermentation by this organism. A pathway for acetate generation from formiminoglycine is proposed, and evidence for a number of enzyme activities intermediate between formiminoglycine degradation and acetate formation is given. The enzyme activities demonstrated are compatible with the over-all purine fermentation rate by whole cells.
pubmed:commentsCorrections
pubmed:keyword
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
OM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:month
Aug
pubmed:issn
0021-9193
pubmed:author
pubmed:issnType
Print
pubmed:volume
82
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
233-8
pubmed:dateRevised
2009-11-18
pubmed:meshHeading
pubmed:year
1961
pubmed:articleTitle
Acetate formation in Clostridium acidi-urici: acetokinase.
pubmed:publicationType
Journal Article