Literature DB >> 3127264

Cofactors in and as posttranslational protein modifications.

R B Rucker1, F Wold.   

Abstract

A symposium at the FASEB meeting in Las Vegas in May 1988 will be devoted to the role of cofactors (vitamins, coenzymes, prosthetic groups) in and as posttranslational protein modifications; the symposium is part of a thematic focus on metabolic regulation. In planning the symposium, we decided to consider metabolic regulation in its broadest context, which should include both the short-term activity modulations in the life of contemporary organisms and the adaptations of special molecular strategies over evolutionary time. We further decided to focus the symposium context on the involvement of cofactors both as catalytic participants in and as substrates or end products of posttranslational modifications. As a preview of the actual symposium, the present discussion is an attempt to enumerate cases of cofactor involvement in these different categories: 1) essential nutrients as participants in posttranslational modifications; 2) cofactors as donor substrates in reversible, regulatory modifications; and 3) cofactor incorporation or generation as covalent constituents of proteins. The actual symposium topics are taken from category 1: vitamin C and protein hydroxylation (K. I. Karivikkio) and vitamin K and protein carboxylation (J. W. Suttie) and category 3: biotinylation (H. G. Wood), phycobiliproteins (A. Glazer), and pyruvoyl enzymes (W. Dowhan).

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Year:  1988        PMID: 3127264     DOI: 10.1096/fasebj.2.7.3127264

Source DB:  PubMed          Journal:  FASEB J        ISSN: 0892-6638            Impact factor:   5.191


  4 in total

1.  A paralog of lysyl-tRNA synthetase aminoacylates a conserved lysine residue in translation elongation factor P.

Authors:  Tatsuo Yanagisawa; Tomomi Sumida; Ryohei Ishii; Chie Takemoto; Shigeyuki Yokoyama
Journal:  Nat Struct Mol Biol       Date:  2010-08-22       Impact factor: 15.369

Review 2.  Covalent attachment of flavin adenine dinucleotide (FAD) and flavin mononucleotide (FMN) to enzymes: the current state of affairs.

Authors:  M Mewies; W S McIntire; N S Scrutton
Journal:  Protein Sci       Date:  1998-01       Impact factor: 6.725

3.  Inhibition of angiogenesis and tumor growth in the brain. Suppression of endothelial cell turnover by penicillamine and the depletion of copper, an angiogenic cofactor.

Authors:  S S Brem; D Zagzag; A M Tsanaclis; S Gately; M P Elkouby; S E Brien
Journal:  Am J Pathol       Date:  1990-11       Impact factor: 4.307

4.  Small cofactors may assist protein emergence from RNA world: clues from RNA-protein complexes.

Authors:  Liang Shen; Hong-Fang Ji
Journal:  PLoS One       Date:  2011-07-18       Impact factor: 3.240

  4 in total

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