nucleoside-q and 3-(3-amino-3-carboxypropyl)uridine

nucleoside-q has been researched along with 3-(3-amino-3-carboxypropyl)uridine* in 2 studies

Reviews

1 review(s) available for nucleoside-q and 3-(3-amino-3-carboxypropyl)uridine

ArticleYear
S-adenosylmethionine: nothing goes to waste.
    Trends in biochemical sciences, 2004, Volume: 29, Issue:5

    S-adenosylmethionine (SAM or AdoMet) is a biological sulfonium compound known as the major biological methyl donor in reactions catalyzed by methyltransferases. SAM is also used as a source of methylene groups (in the synthesis of cyclopropyl fatty acids), amino groups (in the synthesis of 7,8-diaminoperlagonic acid, a precursor of biotin), ribosyl groups (in the synthesis of epoxyqueuosine, a modified nucleoside in tRNAs) and aminopropyl groups (in the synthesis of ethylene and polyamines). Even though the mechanism of most of these reactions has not been extensively characterized, it is likely that the chemistry at work is mainly driven by the electrophilic character of the carbon centers that are adjacent to the positively charged sulfur atom of SAM. In addition, SAM, upon one-electron reduction, is a source of 5'-deoxyadenosyl radicals, which initiate many metabolic reactions and biosynthetic pathways by hydrogen-atom abstraction. SAM presents a unique situation in which all constituent parts have a chemical use.

    Topics: 4-Butyrolactone; Acetyltransferases; Amino Acids, Cyclic; Amino Acids, Diamino; Animals; Cyclopropanes; Fatty Acids; Humans; Intramolecular Transferases; Models, Chemical; Nucleoside Q; Ribonucleotide Reductases; S-Adenosylmethionine; Spermidine; Uridine

2004

Other Studies

1 other study(ies) available for nucleoside-q and 3-(3-amino-3-carboxypropyl)uridine

ArticleYear
Structural comparison of human, bovine, rat, and Walker 256 carcinosarcoma asparaginyl-tRNA.
    Biochimica et biophysica acta, 1980, Dec-11, Volume: 610, Issue:2

    The complete nucleotide sequences of human placenta, human liver, and bovine liver tRNAAsn have been determined. A comparison of these tRNA structures with the previously reported nucleotide sequences of rat liver and Walker 256 carcinosarcoma tRNAAns reveals that the primary nucleotide sequences of the major species of mammalian cytoplasmic tRNAasn are conserved in higher eucaryotes. The complete nucleotide sequence of these tRNAs is: pG-U-C-U-C-U-G-U-m1G-m2G-C-G-C-A-A-D-C-G-G-D-X-A-G-C-G-C-m2(2)G-psi-psi-C-G-G-C-U-Q(G)-U-U-t6A-A-C-C-G-A-A-A-G-m7G-D-U-G-G-U-G-G-Z-psi-C-G-m1A-G-C-C-C-A-C-C-C-A-G-G-G-A-C-G-C-C-AOH where X is 3-(3-amino-3-carboxyl-n-propyl)uridine, Q is 7-(4,5-cis-dihydroxyl-1-cyclopenten-3-yl-aminomethyl)-7-deazaguanosine, Z is an unknown modified nucleotide, and Q(G) represents the replacement of Q nucleoside by G nucleoside in Walker 256 carcinosarcoma tRNAAsn. These primary structures were determined by combined use of the 3H- and 32P-post-labeling techniques. Sequences were compared by tritium nucleoside trialcohol analysis, completed RNAase T1 digestion followed by 3H-labeled fingerprinting on polyethylenimine-impregnated cellulose by two-dimensional thin-layer chromatography (TLC), and polyacrylamide gel electrophoresis of either 5'-32P- and/or 3'-[32P]pCp-labeled tRNA after partial ribonuclease digestions.

    Topics: Animals; Aspartate-tRNA Ligase; Base Sequence; Biological Evolution; Carcinoma 256, Walker; Cattle; Female; Humans; Liver; Nucleoside Q; Placenta; Pregnancy; Rats; RNA, Transfer, Amino Acyl; Species Specificity; Uridine

1980