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Activation of a peroxisomal Pichia pastoris d-amino acid oxidase, which uses d-alanine as a preferred substrate, depends on pyruvate carboxylase

Klompmaker, 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.

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DOI

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.

Original languageEnglish
Pages (from-to)708-716
Number of pages9
JournalFems Yeast Research
Volume10
Issue number6
Publication statusPublished - Sep-2010

    Keywords

  • 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

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