Hydroxyproline-2-epimerase of pseudomonas: Active-site peptides
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Hydroxyproline-2-epimerase was treated with14C-iodoacetate under conditions that produced almost complete inactivation of the enzyme and concomitant incorporation of almost one molar equivalent of iodoacetate. Both processes were prevented by saturating concentrations of substrate. From reaction mixtures in which both incorporation and inactivation were 85 to 90% complete, two radioactive tryptic peptides were isolated by paper chromatography-electrophoresis. The incorporated radioactivity was divided between the peptides in an approximately 2:1 ratio. Analysis of the isolated peptides suggested that they both contained 9 amino acids and had similar composition; one appeared to be a lysine, the second an arginine peptide. Attempts to sequence each peptide failed, apparently because of the conversion of the S-carboxymethylcysteine to S-carboxymethylcysteine sulfone, indicating that the cysteine residue wasN-terminal in each peptide.
KeywordsPeptide Sulfone Cysteine Lysine Arginine
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- 4.Zervos, C., and Adams, E., Fed. Proc. 31, 925 (1972).Google Scholar
- 5.Zervos, C., Fed. Proc. 32, 474 (1973).Google Scholar
- 6.Adams, E., Int'l. Rev. Connective Tissue Research 5, 1–91 (1970).Google Scholar
- 8.Rose, I. A., Ann. Rev. Biochem. 35, 23–56 (1966).Google Scholar
- 12.Pétra, P. H., and Neurath, H., Biochemistry 10, 2171–3177 (1971).Google Scholar