| pubmed-article:8119887 | rdf:type | pubmed:Citation | lld:pubmed |
| pubmed-article:8119887 | lifeskim:mentions | umls-concept:C0024660 | lld:lifeskim |
| pubmed-article:8119887 | lifeskim:mentions | umls-concept:C0004015 | lld:lifeskim |
| pubmed-article:8119887 | lifeskim:mentions | umls-concept:C0025831 | lld:lifeskim |
| pubmed-article:8119887 | lifeskim:mentions | umls-concept:C1280500 | lld:lifeskim |
| pubmed-article:8119887 | lifeskim:mentions | umls-concept:C1709915 | lld:lifeskim |
| pubmed-article:8119887 | lifeskim:mentions | umls-concept:C1515926 | lld:lifeskim |
| pubmed-article:8119887 | lifeskim:mentions | umls-concept:C1530540 | lld:lifeskim |
| pubmed-article:8119887 | pubmed:issue | 8 | lld:pubmed |
| pubmed-article:8119887 | pubmed:dateCreated | 1994-4-1 | lld:pubmed |
| pubmed-article:8119887 | pubmed:databankReference | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:8119887 | pubmed:abstractText | Most mammalian S-adenosylmethionine (AdoMet)-dependent methyltransferases have a conserved aspartate residue in a sequence oDso (o denotes a hydrophobic amino acid and s denotes a small neutral amino acid). Rat guanidinoacetate methyltransferase has two aspartate residues (Asp-129 and Asp-134) conforming to the motif in close proximity to Tyr-136 that is photoaffinity-labeled by AdoMet (Takata, Y., and Fujioka, M. (1992) Biochemistry 31, 4369-4374). In order to investigate the role of these residues, we prepared variant forms of the enzyme by oligonucleotide-directed mutagenesis. Conversion of Asp-129 to asparagine or alanine resulted in a functional enzyme. Alteration of Asp-134 to glutamate (D134E) and asparagine (D134N) decreased activity, and replacement with alanine (D134A) led to inactivation. Decreases of 3- and 120-fold were found for kcat values of D134E and D134N, respectively. The Km values of D134E for AdoMet and those for guanidinoacetate were increased about 160- and 80-fold over the respective values of wild type. The corresponding increases in D134N were 800- and 50-fold, respectively. Conservative changes of the residues flanking Asp-134 had little effect on activity. Guanidinoacetate methyltransferase obeys an ordered Bi Bi mechanism in which AdoMet binds first. Thus, the large decreases in kcat/Km values for AdoMet indicate that Asp-134 is crucial for binding AdoMet. Spectroscopic studies indicated that the amino acid substitutions of Asp-134 resulted in no significant changes in the secondary and tertiary structures, and urea denaturation experiments showed that the altered enzymes were not destabilized. | lld:pubmed |
| pubmed-article:8119887 | pubmed:language | eng | lld:pubmed |
| pubmed-article:8119887 | pubmed:journal | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:8119887 | pubmed:citationSubset | IM | lld:pubmed |
| pubmed-article:8119887 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:8119887 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:8119887 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:8119887 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:8119887 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:8119887 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:8119887 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:8119887 | pubmed:status | MEDLINE | lld:pubmed |
| pubmed-article:8119887 | pubmed:month | Feb | lld:pubmed |
| pubmed-article:8119887 | pubmed:issn | 0021-9258 | lld:pubmed |
| pubmed-article:8119887 | pubmed:author | pubmed-author:TakataYY | lld:pubmed |
| pubmed-article:8119887 | pubmed:author | pubmed-author:KonishiKK | lld:pubmed |
| pubmed-article:8119887 | pubmed:author | pubmed-author:FujiokaMM | lld:pubmed |
| pubmed-article:8119887 | pubmed:author | pubmed-author:GomiTT | lld:pubmed |
| pubmed-article:8119887 | pubmed:issnType | Print | lld:pubmed |
| pubmed-article:8119887 | pubmed:day | 25 | lld:pubmed |
| pubmed-article:8119887 | pubmed:volume | 269 | lld:pubmed |
| pubmed-article:8119887 | pubmed:owner | NLM | lld:pubmed |
| pubmed-article:8119887 | pubmed:authorsComplete | Y | lld:pubmed |
| pubmed-article:8119887 | pubmed:pagination | 5537-42 | lld:pubmed |
| pubmed-article:8119887 | pubmed:dateRevised | 2006-11-15 | lld:pubmed |
| pubmed-article:8119887 | pubmed:meshHeading | pubmed-meshheading:8119887-... | lld:pubmed |
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| pubmed-article:8119887 | pubmed:meshHeading | pubmed-meshheading:8119887-... | lld:pubmed |
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| pubmed-article:8119887 | pubmed:meshHeading | pubmed-meshheading:8119887-... | lld:pubmed |
| pubmed-article:8119887 | pubmed:meshHeading | pubmed-meshheading:8119887-... | lld:pubmed |
| pubmed-article:8119887 | pubmed:meshHeading | pubmed-meshheading:8119887-... | lld:pubmed |
| pubmed-article:8119887 | pubmed:meshHeading | pubmed-meshheading:8119887-... | lld:pubmed |
| pubmed-article:8119887 | pubmed:year | 1994 | lld:pubmed |
| pubmed-article:8119887 | pubmed:articleTitle | Rat guanidinoacetate methyltransferase. Effect of site-directed alteration of an aspartic acid residue that is conserved across most mammalian S-adenosylmethionine-dependent methyltransferases. | lld:pubmed |
| pubmed-article:8119887 | pubmed:affiliation | Department of Biochemistry, Toyama Medical and Pharmaceutical University Faculty of Medicine, Japan. | lld:pubmed |
| pubmed-article:8119887 | pubmed:publicationType | Journal Article | lld:pubmed |
| pubmed-article:8119887 | pubmed:publicationType | Research Support, Non-U.S. Gov't | lld:pubmed |
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