Detail of "16874-75-2"

Reference

Sindbis virus RNA polymerase is degraded by the N-end rule pathway

Sindbis virus RNA polymerase is degraded by the N-end rule pathway. De Groot, Raoul J.; Rumenape, Tillmann; Kuhn, Richard J.; Strauss, Ellen G.; Strauss, James H. (Div. Biol., California Inst. Technol., Pasadena, CA 91125, USA). Proc. Natl. Acad. Sci. U. S. A., 88(20), 8967-71 (English) 1991. CODEN: PNASA6. ISSN: 0027-8424. DOCUMENT TYPE: Journal CA Section: 10 (Microbial, Algal, and Fungal Biochemistry) Upon infection of animal cells by Sindbis virus, four nonstructural (ns) proteins, termed nsP1-4 in order from 5' to 3' in the genome, are produced by posttranslational cleavage of a polyprotein. NsP4 is believed to function as the viral RNA polymerase and is short-lived in infected cells. This report shows that nsP4 produced in reticulocyte lysates is degraded by the N-end rule pathway, one ubiquitin-dependent proteolytic pathway. When the N-terminal residue of nsP4 is changed by mutagenesis, the metabolic stabilities of the mutant nsP4s follow the N-end rule, in that the half-life of nsP4 bearing different N-terminal residues decreases in the order Met > Ala > Tyr 3 Phe > Arg. Addn. of dipeptides Tyr-Ala, Trp-Ala, or Phe-Ala to the translation mixt. inhibits degrdn. of Tyr-nsP4 and Phe-nsP4, but not of Arg-nsP4. Conversely, dipeptides His-Ala, Arg-Ala, and Lys-Ala inhibit the degrdn. of Arg-nsP4 but not of Tyr-nsP4 or Phe-nsP4. 40968-45-4 and 16874-75-2 which are cas registry numbers of substances are two of reagents here. There is no lysine in the first 43 residues of nsP4 that is required for its degrdn., indicating that a more distal lysine functions as the ubiquitin acceptor. Strict control of nsP4 concn. appears to be an important aspect of the virus life cycle, since the concn. of nsP4 in infected cells is regulated at three levels: translation of nsP4 requires readthrough of an opal termination codon such that it is underproduced; differential processing by the virus-encoded proteinase results in temporal regulation of nsP4; and nsP4 itself is a short-lived protein degraded by the ubiquitin-dependent N-end rule pathway. .

Metabolism of peptides containing L-alanine by rat hepatocytes

Metabolism of peptides containing L-alanine by rat hepatocytes. Rognstad, Robert (Cedars-Sinai Med. Cent. 3695-73-6 and 16874-75-2 are also occured in this study., Los Angeles, CA 90048, USA). Med. Sci. Res., 15(2), 71 (English) 1987. CODEN: MSCREJ. DOCUMENT TYPE: Journal CA Section: 13 (Mammalian Biochemistry) Rat hepatocytes formed glucose at a high rate from short peptides contg. L-alanine (I). Rates were comparable from di- through penta-I as well as from I itself. Rates with dipeptides contg. I + another amino acid were lower but above endogenous rates. The rate of I appearance from tri-I suggested that the peptidase activity is on the outer surface of the plasma membrane. Thus, the liver may play a role in degrading short-chain peptides in the circulation. .