Aminomalonic acid: Identification in Escherichia coli and atherosclerotic plaque

Abstract

Aminomalonic acid (Ama) has been isolated from proteins of Escherichia coli and human atherosclerotic plaque. The presence of Ama has important biological implications because the malonic acid moiety potentially imparts calcium binding properties to protein. Ama was obtained by anaerobic alkaline hydrolysis and identified by chromatographic behavior, quantitative acid-mediated decarboxylation to glycine, and unambiguous gas chromatographic/mass spectral detection. The chromatographic, chemical, and mass spectral properties of naturally occurring Ama were identical to those of the synthetic compound. Amino acid analysis and GC/mass spectrometry also revealed the presence of β-carboxyaspartic acid and γ-carboxyglutamic acid in the base hydrolysate of human atherosclerotic plaque. The ratio of Ama to β-carboxyaspartic acid to γ-carboxyglutamic acid was 20:1:10, and the quantity of Ama per 1,000 glycine residues was 0.2. Ama is a relatively unstable, minor amino acid in complex structures such as bacteria or tissues. This may explain why it has escaped detection previously, despite intensive investigation.