Linked Life Data

12199107

Source:http://linkedlifedata.com/resource/pubmed/id/12199107

Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
1
pubmed:dateCreated
2002-8-29
pubmed:abstractText
Reactivity of thiamin monophosphate (TMP) as calf intestinal alkaline phosphatase substrate in model transformations is lower comparing with thiamin diphosphate (TDP) reactivity. Under these conditions alkaline phosphatase catalyzes TDP, ADP and AMP hydrolysis approximately at same rate. It was shown that TDP competes with p-nitrophenyl phosphate more effectively than TMP for the binding in the active site. At pH 8.5 and 30 degrees C Km values are as follows: (5.2 +/- 1.6) x 10(-3) M for TMP and (3.0 +/- 0.8) x 10(-4) M for TDP. Under the same conditions the Vmax/Km value for TDP hydrolysis is 53 times higher than the one for corresponding reaction of TMP. It was suggested that positively charged thiazolium ion of TMP interacts with the nearest environment at the active center and by this way reduces enzyme activity.
pubmed:language
rus
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:issn
0201-8470
pubmed:author
pubmed:issnType
Print
pubmed:volume
74
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
93-6
pubmed:dateRevised
2006-11-15
pubmed:meshHeading
pubmed:articleTitle
[Relative reactivity of thiamine monophosphate and thiamine diphosphate upon interaction with alkaline phosphatase].
pubmed:affiliation
Institute of Bioorganic Chemistry and Petrochemistry, NAS of Ukraine, Kyiv. vovk@bpci.kiev.ua
pubmed:publicationType
Journal Article, English Abstract