Journal
ARCHIVES OF BIOCHEMISTRY AND BIOPHYSICS
Volume 412, Issue 1, Pages 3-12Publisher
ACADEMIC PRESS INC ELSEVIER SCIENCE
DOI: 10.1016/S0003-9861(02)00730-0
Keywords
peptidylglycine alpha-amidating monooxygenase; glutathione S-transferase; glutathione; LTC4; xenobiotic detoxification
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Funding
- NIGMS NIH HHS [R01-GM62767, R15-GM67257] Funding Source: Medline
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The C-terminal alpha-amide moiety of most peptide hormones arises by the posttranslational cleavage of a glycine-extended precursor in a reaction catalyzed by bifunctional peptidylglycine alpha-amidating monooxygenase (PAM). Glutathione and the S-alkylated glutathiones have a C-terminal glycine and are, thus, potential substrates for PAM. The addition of PAM to glutathione, a series of S-alkylated glutathiones, and leukotriene C-4 results in the consumption Of O-2 and the production of the corresponding amidated peptide and glyoxylate. This reaction proceeds in two steps with the intermediate formation of a C-terminal alpha-hydroxyglycine-extended peptide. Amidated glutathione (gammaGlu-Cys-amide) is a relatively poor substrate for glutathione S-transferase with a V/K value that is 1.3% of that for glutathione. Peptide substrates containing a penultimate hydrophobic or sulfur-containing amino acid exhibit the highest (V/K)(app) values for PAM-catalyzed amidation. The S-alkylated glutathiones incorporate both features in the penultimate position with S-decylglutathione having the highest (V/K)(app) of the substrates described in this report. (C) 2003 Elsevier Science (USA). All rights reserved.
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