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Homocysteine thiolactone and protein homocysteinylation: mechanistic studies with model peptides and proteins
Author(s) -
Hop Cornelis E. C. A.,
Bakhtiar Ray
Publication year - 2002
Publication title -
rapid communications in mass spectrometry
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 0.528
H-Index - 136
eISSN - 1097-0231
pISSN - 0951-4198
DOI - 10.1002/rcm.681
Subject(s) - chemistry , homocysteine , thiolactone , lysine , biochemistry , covalent bond , amino acid , stereochemistry , organic chemistry
In vitro incubations were performed to show that homocysteine thiolactone could generate covalent adducts with model peptides and proteins. MS and MS/MS data suggest that the thiolactone reacts with the side‐chain amino group of lysine residues as well as with the N‐terminal amino group or C‐terminal carboxy group. For larger peptides and proteins, the contribution from the ∈‐amino groups of lysine residues should be predominant. These data could help explain the detrimental effects of elevated levels of homocysteine and homocysteine thiolactone. Copyright © 2002 John Wiley & Sons, Ltd.