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Predicate | Object |
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rdf:type | |
lifeskim:mentions | |
pubmed:issue |
1
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pubmed:dateCreated |
1981-5-13
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pubmed:abstractText |
In the reaction adenosine + L-homocysteine = S-adenosyl-L-homocysteine, catalyzed by S-adenosylhomo-cysteine hydrolase from beef liver (EC 3.3.1.1), 11 nucleosides are able to substitute for adenosine to generate their corresponding S-nucleosidylhomocysteine congeners: 3-deaza-adenosine, 2-aza-3-deazaadenosine, nebularine (purine ribonucleoside), formycin, N6-methyladenosine, 8-azaadenosine, adenosine N1-oxide, pyrazomycin, 8-aminoadenosine, inosine, and the carbocyclic analogue of adenosine [(+/-)-aristeromycin]. S-Adenosylhomocysteine hydrolase from lupin seeds is able to utilize all of these nucleosides except inosine to synthesize analogues of S-adenosylhomocysteine. There is no correlation between the ability of these nucleotides to function as substrates and their inhibitory potencies, except in the case of 3-deazaadenosine. The carbocyclic analogue of adenosine is the most potent inhibitor of S-adenosylhomocysteine hydrolase with a Ki of 5 X 10(-9) M. When incubated with 3T3-L1 fibroblasts, the carbocyclic analogue of adenosine caused a 20-fold increase in the cellular concentration of S-adenosyl-homocysteine. The cellular generation of S-2-aza-3-deaza-adenosylhomocysteine was observed when 3T3-L1 fibroblasts were incubated with 2-aza-3-deazaadenosine.
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pubmed:language |
eng
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pubmed:journal | |
pubmed:citationSubset |
IM
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pubmed:chemical | |
pubmed:status |
MEDLINE
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pubmed:month |
Jan
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pubmed:issn |
0006-2960
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pubmed:author | |
pubmed:issnType |
Print
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pubmed:day |
6
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pubmed:volume |
20
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pubmed:owner |
NLM
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pubmed:authorsComplete |
Y
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pubmed:pagination |
110-5
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pubmed:dateRevised |
2006-11-15
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pubmed:meshHeading |
pubmed-meshheading:7470463-Adenosine,
pubmed-meshheading:7470463-Adenosylhomocysteinase,
pubmed-meshheading:7470463-Animals,
pubmed-meshheading:7470463-Cattle,
pubmed-meshheading:7470463-Hydrolases,
pubmed-meshheading:7470463-Kinetics,
pubmed-meshheading:7470463-Liver,
pubmed-meshheading:7470463-Structure-Activity Relationship,
pubmed-meshheading:7470463-Substrate Specificity
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pubmed:year |
1981
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pubmed:articleTitle |
Adenosine analogues as substrates and inhibitors of S-adenosylhomocysteine hydrolase.
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pubmed:publicationType |
Journal Article
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