Molecular and Cellular Biochemistry

, Volume 8, Issue 2, pp 113–121 | Cite as

Hydroxyproline-2-epimerase of pseudomonas: Active-site peptides

  • Constantine Zervos
  • Elijah Adams
Review and general articles b. general articles

Summary

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.

Keywords

Peptide Sulfone Cysteine Lysine Arginine 

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Copyright information

© Dr. W. Junk b.v. Publishers 1975

Authors and Affiliations

  • Constantine Zervos
    • 1
  • Elijah Adams
    • 1
  1. 1.From the Department of Biological ChemistryUniversity of Maryland School of MedicineBaltimoreUSA

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