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Human Erythrocyte D-Aspartyl/L-Isoaspartyl Methyltransferases: Enzymes that Recognize Age-Damaged Proteins

  • Diego Ingrosso
  • Steven Clarke
Part of the Advances in Experimental Medicine and Biology book series (AEMB, volume 307)

Abstract

Among the large number of protein post-biosynthetic modifications described so far are a group of non-enzymatic reactions that reflect the spontaneous, intrinsic, decomposition of these macromolecules as they age in cells. These alterations include oxidation (1), formation of advanced glycosylation end products (2), and linked deamination/isomerization/ racemization reactions (3). Our interest has been focused on the latter reactions that lead to the loss of L-aspartyl and L-asparaginyl residues in proteins and the recognition of the damaged proteins by enzymes that can lead to their cellular removal by repair or degradation reactions (4–9).

Keywords

Human Erythrocyte Methyl Transferase Isopeptide Bond Aspartyl Residue Protein Carboxyl 
These keywords were added by machine and not by the authors. This process is experimental and the keywords may be updated as the learning algorithm improves.

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Copyright information

© Plenum Press, New York 1991

Authors and Affiliations

  • Diego Ingrosso
    • 1
    • 2
  • Steven Clarke
    • 2
  1. 1.Istituto di Biochimica delle Macromolecole I Facoltà di Medicina e ChirurgiaUniversità di NapoliNapoliItaly
  2. 2.Department of Chemistry and Biochemistry and the Molecular Biology InstituteUniversity of California Los AngelesLos AngelesUSA

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