Linked Life Data

10814545

Source:http://linkedlifedata.com/resource/pubmed/id/10814545

Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
3
pubmed:dateCreated
2000-6-20
pubmed:abstractText
The sulfation of a nucleotide is an indispensable step for the sulfuryl group transfer in a biological system. The product and cosubstrate of sulfotransferase in physiological condition are adenosine 3',5'-bisphosphate (PAP) and 3'-phospho adenosine 5'-phosphosulfate (PAPS), respectively. We find that ribose and adenine, two major parts of the adenosine nucleotide, bind tightly to phenol sulfotransferase (PST) separately, and various nucleotides also bind tightly to PST. We determine the dissociation constants of a variety of nucleotides and examine their potential as cofactors or cosubstrates of PST. Using 4-nitrophenyl sulfate as the sulfuryl group donor, three nucleotides, adenosine 5'-monophosphate (AMP), adenosine 2',5'-bisphosphate (2',5'-PAP), and adenosine 2':3'-cyclic phosphate 5'-phosphate (2':3'-cyclic PAP), are shown here for the first time to be sulfated at 5'-phopho position by a PST catalyzed reaction. Spectrophotometry, HPLC, and (31)P NMR are used to determine the activity of PST and identify the sulfated nucleotides. The V(max) of PST and K(m) of these nucleotides are determined when they are used as cofactors or cosubstrates for the sulfuryl group transfer. The existence and possible physiological significance of these newly reported binding and sulfation of nucleotides by PST in biology is yet to be discovered.
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:month
May
pubmed:issn
0006-291X
pubmed:author
pubmed:copyrightInfo
Copyright 2000 Academic Press.
pubmed:issnType
Print
pubmed:day
19
pubmed:volume
271
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
818-22
pubmed:dateRevised
2006-11-15
pubmed:meshHeading
pubmed:year
2000
pubmed:articleTitle
Nucleotide binding and sulfation catalyzed by phenol sulfotransferase.
pubmed:affiliation
Department of Biological Science and Technology, College of Science, Hsinchu, Taiwan, Republic of China.
pubmed:publicationType
Journal Article, Research Support, Non-U.S. Gov't