Zinc binding in peptide models of angiotensin-I converting enzyme active sites studied through 1H-NMR and chemical shift perturbation mapping

Biopolymers. 2003 Jun;69(2):244-52. doi: 10.1002/bip.10362.

Abstract

We report the design and synthesis through solid phase 9-flourenylmethoxycarbonyl (Fmoc) chemistry of the two angiotensin-I converting enzyme active sites possessing the general sequence HEMGHX(23)EAIGDX(3). Their zinc-binding properties were monitored in solution through high-resolution (1)H-NMR. The obtained data were analyzed in terms of chemical shift differences. The results indicate that zinc binds to the HEMGH and the EAIGD characteristic motifs, and suggest possible coordination modes of zinc in the native enzyme.

Publication types

  • Research Support, Non-U.S. Gov't

MeSH terms

  • Amino Acid Motifs
  • Amino Acid Sequence
  • Binding Sites
  • Humans
  • Isoenzymes / chemistry
  • Isoenzymes / metabolism
  • Models, Molecular
  • Molecular Sequence Data
  • Nuclear Magnetic Resonance, Biomolecular / methods*
  • Peptide Fragments / chemical synthesis
  • Peptide Fragments / chemistry
  • Peptide Fragments / metabolism
  • Peptide Mapping
  • Peptidyl-Dipeptidase A / chemistry*
  • Peptidyl-Dipeptidase A / metabolism*
  • Protein Conformation
  • Protons
  • Sequence Homology, Amino Acid
  • Solutions
  • Thermolysin / chemistry
  • Thermolysin / metabolism
  • Zinc / metabolism*

Substances

  • Isoenzymes
  • Peptide Fragments
  • Protons
  • Solutions
  • Peptidyl-Dipeptidase A
  • Thermolysin
  • Zinc