title: Coordination of divalent metal cation to amide group to form adduct ion in FAB mass spectrometry: implication of Zn2+ in enzymatic hydrolysis of amide bond.
abstract: The structures of complexes between amides and metal ions were examined by FAB mass spectrometry and collision-induced dissociation (CID). Zn2+ was coordinated by the amide carbonyl oxygen atom of N-tetradecylacetamide (1). In contrast, Ca2+ and Mg2+ were coordinated by the amide group of 1 in both the keto and enol forms. The catalytic role of Zn2+ at the active site of the hydrolases might partly be explained by the effective attack of Zn2+ on carbonyl oxygen atom of the scissile amide group.
authors.affiliation: Institute of Molecular & Cellular Biosciences, The University of Tokyo, Yayoi, Tokyo, Japan.
authors.forename: Hisayoshi
authors.initials: H
authors.lastname: Kobayashi
authors.forename: Naoko
authors.initials: N
authors.lastname: Morisaki
authors.forename: Hiroyuki
authors.initials: H
authors.lastname: Miyachi
authors.forename: Yuichi
authors.initials: Y
authors.lastname: Hashimoto
mesh_terms: D000577:Amides / Q000737:chemistry*; D002118:Calcium / Q000737:chemistry; D002413:Cations, Divalent / Q000737:chemistry*; D006867:Hydrolases / Q000737:chemistry; D006868:Hydrolysis; D007202:Indicators and Reagents; D008274:Magnesium / Q000737:chemistry; D009682:Magnetic Resonance Spectroscopy; D016339:Spectrometry, Mass, Fast Atom Bombardment; D015032:Zinc / Q000737:chemistry*
chemical_list: D000577:Amides; D002413:Cations, Divalent; D007202:Indicators and Reagents; D006867:Hydrolases; D008274:Magnesium; D015032:Zinc; D002118:Calcium