Production of angiotensin-converting enzyme inhibitors from baker's yeast glyceraldehyde-3-phosphate dehydrogenase

Faculty of Pharmaceutical Sciences, Osaka University, Japan.
Journal of pharmacobio-dynamics 01/1991; 13(12):766-71. DOI: 10.1248/bpb1978.13.766
Source: PubMed


Angiotensin-converting enzyme (ACE) inhibitors were excised from the molecule of glyceraldehyde-3-phosphate dehydrogenase (GAPDH) preparation of baker's yeast by heating at 120 degrees C in 1 M AcOH-20 mM HCl. Three inhibitors were then purified by gel-permeation and reverse-phase chromatographies. One of the yeast ACE inhibitors, YG-3, was GAPDH peptide 79-89 (Pro-Ala-Asn-Leu-Pro-Trp-Gly-Ser-Ser-Asn-Val, IC50:18 microM), and contained the sequence homologous to vertebrate ACE inhibitors (GAPDH peptides 79-86 or 81-88). Other inhibitors, YG-1 (Gly-His-Lys-Ile-Ala-Thr-Phe-Gln-Glu-Arg, IC50: 0.4 microM) and YG-2 (Gly-Lys-Lys-Ile-Ala-Thr-Tyr-Gln-Glu-Arg, IC50: 2 microM), corresponded to amino acid residues 68-77 in two different forms of yeast GAPDH, respectively. Their sequences were quite different from those of the venom peptide family. YG-1 was the most potent ACE inhibitor among yeast and vertebrate GAPDH peptides excised by acid-limited proteolysis. Thus, yeast GAPDH seems to be an excellent source of naturally occurring ACE inhibitors.

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    • "Many research groups have been screened for novel ACE inhibitors of microbial origin such as Doratomyces putredinis, Nocardia orientalis (Ando, 1987), Virgaria nigra (Ando, 1988), Actinomycetes (Kido, 1983), baker's yeast (Kohama, 1990) and Basidiomycetes (Lee, 2003). WF-10129, obtained from Doratomyces putredinis, is an ACE inhibitor resembling to the potent synthetic ACE inhibitor, enalapril, and is a substituted N-carboxymethyl dipeptide. "
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