| Activation of a peroxisomal Pichia pastoris D-amino acid oxidase, which uses d-alanine as a preferred substrate, depends on pyruvate carboxylase. | |
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MedLine Citation:
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PMID: 20550580 Owner: NLM Status: MEDLINE |
Abstract/OtherAbstract:
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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. |
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Authors:
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Sandra H Klompmaker; Aysun Kilic; Richard J Baerends; Marten Veenhuis; Ida J van der Klei |
Publication Detail:
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Type: Journal Article Date: 2010-05-17 |
Journal Detail:
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Title: FEMS yeast research Volume: 10 ISSN: 1567-1364 ISO Abbreviation: FEMS Yeast Res. Publication Date: 2010 Sep |
Date Detail:
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Created Date: 2010-08-11 Completed Date: 2010-11-24 Revised Date: - |
Medline Journal Info:
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Nlm Unique ID: 101085384 Medline TA: FEMS Yeast Res Country: England |
Other Details:
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Languages: eng Pagination: 708-16 Citation Subset: IM |
Affiliation:
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Molecular Cell Biology, University of Groningen, AA Haren, The Netherlands. |
Export Citation:
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| MeSH Terms | |
Descriptor/Qualifier:
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Alanine
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metabolism* Amino Acid Sequence Culture Media / chemistry D-Amino-Acid Oxidase / chemistry, genetics, metabolism* Enzyme Stability Hydrogen-Ion Concentration Molecular Sequence Data Molecular Weight Peroxisomes / enzymology* Pichia / enzymology*, growth & development Pyruvate Carboxylase / genetics, metabolism* Sequence Alignment Sequence Homology Substrate Specificity Temperature |
| Chemical | |
Reg. No./Substance:
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0/Culture Media; 56-41-7/Alanine; EC 1.4.3.3/D-Amino-Acid Oxidase; EC 6.4.1.1/Pyruvate Carboxylase |
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine
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