Linked Life Data

1482408

Source:http://linkedlifedata.com/resource/pubmed/id/1482408

Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
4
pubmed:dateCreated
1993-2-5
pubmed:abstractText
The relationship between the kinetics of the enzyme activity and the structural features of phenolic donor and of acceptor substrates was investigated with a sulfotransferase from Eubacterium A-44, a human intestinal bacterium. The enzyme catalyzed the transfer of the sulfate group from the sulfate esters of phenol having a lower pKa to phenols having a higher pKa. When the Km values for acceptor substrates were measured at their optimal pH, a linear plot for log10Km versus the pKa with a slope of 0.615 was obtained. In addition, it is considered that the effect of pH on the Km values for the various acceptors is due to ionization of free enzyme. The kinetic behavior of bacterial sulfotransferase differed from that of mammalian phenol sulfotransferase.
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:month
Dec
pubmed:issn
0158-5231
pubmed:author
pubmed:issnType
Print
pubmed:volume
28
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
725-34
pubmed:dateRevised
2008-11-21
pubmed:meshHeading
pubmed:year
1992
pubmed:articleTitle
Relationship between substrate activity and pKa value of phenols on sulfotransferase from Eubacterium A-44.
pubmed:affiliation
Faculty of Pharmaceutical Sciences, Toyama Medical and Pharmaceutical University, Japan.
pubmed:publicationType
Journal Article, Comparative Study