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Investigating the role of active site residues of Rhodotorula gracilis d-amino acid oxidase on its substrate specificity

โœ Scribed by Angelo Boselli; Luciano Piubelli; Gianluca Molla; Mirella S. Pilone; Loredano Pollegioni; Silvia Sacchi


Book ID
116308713
Publisher
Elsevier Science
Year
2007
Tongue
English
Weight
476 KB
Volume
89
Category
Article
ISSN
0300-9084

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On the mechanism of Rhodotorula gracilis
โœ Angelo Boselli; Luciano Piubelli; Gianluca Molla; Silvia Sacchi; Mirella S. Pilo ๐Ÿ“‚ Article ๐Ÿ“… 2004 ๐Ÿ› Elsevier Science ๐ŸŒ English โš– 411 KB

Serine 335 at the active site of d-amino acid oxidase from the yeast Rhodotorula gracilis (RgDAAO) is not conserved in other DAAO sequences. To assess its role in catalysis, it was mutated to Gly, the residue present in mammalian DAAO, an enzyme with a 35-fold lower turnover number with d-alanine. T