Zinc binding in peptide models of angiotensin-I converting enzyme active sites studied through 1H-NMR and chemical shift perturbation mapping.
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.
Galanis
Athanassios S
AS
Department of Pharmacy, University of Patras, GR-26500, Patras, Greece.
Spyroulias
Georgios A
GA
Pierattelli
Roberta
R
Tzakos
Andreas
A
Troganis
Anastassios
A
Gerothanassis
Ioannis P
IP
Pairas
George
G
Manessi-Zoupa
Evy
E
Cordopatis
Paul
P
D020816:Amino Acid Motifs; D000595:Amino Acid Sequence; D001665:Binding Sites; D006801:Humans; D007527:Isoenzymes / Q000737:chemistry / Q000378:metabolism; D008958:Models, Molecular; D008969:Molecular Sequence Data; D019906:Nuclear Magnetic Resonance, Biomolecular / Q000379:methods*; D010446:Peptide Fragments / Q000138:chemical synthesis / Q000737:chemistry / Q000378:metabolism; D010449:Peptide Mapping; D007703:Peptidyl-Dipeptidase A / Q000737:chemistry* / Q000378:metabolism*; D011487:Protein Conformation; D011522:Protons; D017386:Sequence Homology, Amino Acid; D012996:Solutions; D013820:Thermolysin / Q000737:chemistry / Q000378:metabolism; D015032:Zinc / Q000378:metabolism*
D007527:Isoenzymes; D010446:Peptide Fragments; D011522:Protons; D012996:Solutions; D007703:Peptidyl-Dipeptidase A; D013820:Thermolysin; D015032:Zinc