SUMMARY: The yeast (CBS 5777, ATCC 56897) when grown on spermidine, diaminopropane, putrescine, diaminopentane, diaminohexane, acetylputrescine or 4-acetamidobutyrate as sole nitrogen source contained a deacetylase (EC 3.5.1.-) catalysing the removal of the acetyl group from -acetyl-β-alanine, 4-acetamidobutyrate and 5-acetamidopentanoate. The enzyme was synthesized early in the exponential growth phase when that had been grown in medium containing glucose and ammonium was transferred to medium in which putrescine replaced ammonium. The 4-acetamidobutyrate deacetylase was partially purified 250-fold. The stoicheiometry of the reaction was established using 4-acetamidobutyrate as substrate. The enzyme had a subunit relative molecular mass ( ) of 78 500 and a in the range 122000 to 143000. The pH optimum was 8·0. The for 4-acetamidobutyrate was 0·29 m. The enzyme was found in a number of other yeast species and was usually associated with high levels of diamine acetyltransferase and acetylputrescine oxidase. The role of this enzyme in the catabolism of di- and polyamines (including those organisms able to use these amines as carbon source) is discussed.


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