On the mechanism of Rhodotorula gracilis
โ
Angelo Boselli; Luciano Piubelli; Gianluca Molla; Silvia Sacchi; Mirella S. Pilo
๐
Article
๐
2004
๐
Elsevier Science
๐
English
โ 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