Activation of a peroxisomal Pichia pastoris d-amino acid oxidase, which uses d-alanine as a preferred substrate, depends on pyruvate carboxylaseKlompmaker, S. H., Kilic, A., Baerends, R. J., Veenhuis, M. & van der Klei, I. J., Sep-2010, In : Fems Yeast Research. 10, 6, p. 708-716 9 p.
Research output: Contribution to journal › Article › Academic › peer-review
d-Amino acid oxidase (DAO) is an important flavo-enzyme that catalyzes the oxidative deamination of d-amino acids into the corresponding alpha-keto acid, ammonia and H(2)O(2). We identified two amino acid oxidases in the methylotrophic yeast Pichia pastoris: Dao1p, which preferentially uses d-alanine as a substrate, and Dao2p, which uses d-aspartate as a preferred substrate. Dao1p has a molecular mass of 38.2 kDa and a pH optimum of 9.6. This enzyme was localized to peroxisomes, albeit a typical peroxisomal targeting signal is lacking. Interestingly, P. pastoris mutant strains, defective in the enzyme pyruvate carboxylase, showed a pronounced growth defect on d-alanine, concomitant with a significant reduction in Dao1p activity relative to the wild-type control. This indicates that pyruvate carboxylase functions in import and/or activation of P. pastoris Dao1p.
|Number of pages||9|
|Journal||Fems Yeast Research|
|Publication status||Published - Sep-2010|
- d-amino acid oxidase, peroxisome, pyruvate carboxylase, Pichia pastoris, moonlighting, HANSENULA-POLYMORPHA, SACCHAROMYCES-CEREVISIAE, TARGETING SIGNAL, CANDIDA-BOIDINII, ALCOHOL OXIDASE, METHANOL OXIDASE, YEAST, GENE, PROTEIN, GROWTH