| Literature DB >> 2387389 |
P J Groenen1, P R van den Ijssel, C E Voorter, H Bloemendal, W W de Jong.
Abstract
Of all aspartyl residues in bovine alpha A-crystallin, only Asp-151 exhibits pronounced racemization. Asp-151 is also one of the sites where peptide bond cleavage occurs in in vivo aging alpha A-crystallin. This aspartyl residue is followed by an alanyl residue and resides in a flexible carboxyl terminal extension of alpha-crystallin. Both in vivo and in vitro racemization studies indicate that the pronounced and site-specific racemization of Asp-151 proceeds via formation of a succinimide intermediate. The in vivo racemization of aspartyl residues in alpha A-crystallin is discussed with regard to the proposed tertiary structure of alpha-crystallin.Entities:
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Year: 1990 PMID: 2387389 DOI: 10.1016/0014-5793(90)81131-7
Source DB: PubMed Journal: FEBS Lett ISSN: 0014-5793 Impact factor: 4.124