ISSN:
1432-072X
Keywords:
Dihydropyrimidinase
;
Purification
;
Dihydropyrimidine
;
Hydantoin
;
Pseudomonas stutzeri
Source:
Springer Online Journal Archives 1860-2000
Topics:
Biology
Notes:
Abstract Dihydropyrimidinase from Pseudomonas stutzeri ATCC 17588 was purified 100-fold and characterized. It was found that dihydrouracil, dihydrothymine and hydantoin could serve as substrates for the partially purified enzyme. The K m values for dihydrouracil, dihydrothymine and hydantoin were determined to be 19.6 μM, 21.3 μM and 36.4 μM, respectively, while their respective V max values were 0.836 μmol/min, 0.666 μmol/min and 2.21 μmol/min. Between pH 7.5 and 9.0, enzyme activity was shown to be maximal. The optimum temperature for enzyme activity was 45 °C. Using gel filtration, the molecular weight of the enzyme was calculated to be approximately 115000 Da. Metal ions were found to influence the level of enzyme activity. Dihydropyrimidinase activity was stimulated by magnesium ions and inhibited by either zinc or copper ions.
Type of Medium:
Electronic Resource
URL:
http://dx.doi.org/10.1007/BF00248895
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