Linked Life Data

5854583

Source:http://linkedlifedata.com/resource/pubmed/id/5854583

Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
6
pubmed:dateCreated
1966-3-23
pubmed:abstractText
Gaudy, Elizabeth T. (University of Illinois, Urbana), and R. S. Wolfe. Ureidoglycolate synthetase of Streptococcus allantoicus. II. Properties of the enzyme and reaction equilibrium. J. Bacteriol. 90:1531-1536. 1965.-The properties of ureidoglycolate synthetase from Streptococcus allantoicus grown on allantoin were studied, by use of the purified enzyme preparation and crystalline sodium ureidoglycolate. Ureidoglycolate synthetase activity was maximal over the pH range of 8.4 to 8.8. No cofactors were required for the reaction. Enzyme activity was inhibited by p-chloromercuribenzoate at relatively high concentrations, by Hg(++) or Zn(++) ions, and to a lesser extent by several other metal cations. The maximal velocity for the purified ureidoglycolate synthetase, determined graphically from a Lineweaver-Burk plot, was 220 mumoles of glyoxylate formed per min per mg of protein. The substrate concentration required for half-maximal velocity was 3.3 x 10(-2)m. The equilibrium constant for the synthesis of ureidoglycolate was determined in a series of reaction mixtures covering a wide range of initial concentrations of reactants. The position of the equilibrium was not affected by a change in pH or by the presence of enzyme. The equilibrium constant for the reaction in the direction of synthesis was 7.6, corresponding to a negative free energy change of 1,230 cal per mole.
pubmed:commentsCorrections
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:month
Dec
pubmed:issn
0021-9193
pubmed:author
pubmed:issnType
Print
pubmed:volume
90
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
1531-6
pubmed:dateRevised
2009-11-18
pubmed:meshHeading
pubmed:year
1965
pubmed:articleTitle
Ureidoglycolate synthetase of Streptococcus allantoicus. II. Properties of the enzyme and reaction equilibrium.
pubmed:publicationType
Journal Article, In Vitro