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
Identification and role of ionizing functional groups at the active center of Rhodotorula gracilis D-amino acid oxidase
โ Scribed by Loredano Pollegioni; Christopher M. Harris; Gianluca Molla; Mirella S. Pilone; Sandro Ghisla
- Book ID
- 117103506
- Publisher
- Elsevier Science
- Year
- 2001
- Tongue
- English
- Weight
- 158 KB
- Volume
- 507
- Category
- Article
- ISSN
- 0014-5793
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This study reports on the development of a bioreactor for the production of a-keto acids from D,L-or D-amino acids using Rhodotorula gracilis o-amino acid oxidase. D-Amino acid oxidase was co-immobilized with catalase on Affi-Gel 10 matrix, and the reactor was operated as a continuous-stirred tank r
The cellular D-amino acid oxidase (DAAO) and catalase activities of Rhodotorula gracilis were greatly increased upon the treatment of the cells with cetyltrimethylammonium bromide (CTAB). However, these enzymes, slowly leaks out from the permeabilized cells. The released DAAO was rapidly inactivated