The Acylamide Amidohydrolase of Candida utilis: Purification and Properties
Copyright policy )The Acylamide Amidohydrolase of Candida utilis: Purification and Properties
SUMMARY: The amidohydrolase formed in the later stages of growth on glucose peptone medium by Candida utilis was purified 60-fold from cell-free extracts. The purified enzyme hydrolysed mono- and di-carboxylic acid amides, benzamide, nicotinamide, pyrazinamide and certain β-hydroxyl substituted fatty acid amides, was inactive on l-asparagine and l-glutamine and was competitively inhibited by urea and N-methylurea. Acetamide and nicotinamide together showed mutual competition.
Niacinamide, Chromatography, Cell-Free System, Transferases, Proteins, Urea, Hydrogen-Ion Concentration, Amides, Amidohydrolases, Candida
Niacinamide, Chromatography, Cell-Free System, Transferases, Proteins, Urea, Hydrogen-Ion Concentration, Amides, Amidohydrolases, Candida
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