Document Detail

Activation of a peroxisomal Pichia pastoris D-amino acid oxidase, which uses d-alanine as a preferred substrate, depends on pyruvate carboxylase.
MedLine Citation:
PMID:  20550580     Owner:  NLM     Status:  MEDLINE    
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.
Sandra H Klompmaker; Aysun Kilic; Richard J Baerends; Marten Veenhuis; Ida J van der Klei
Publication Detail:
Type:  Journal Article     Date:  2010-05-17
Journal Detail:
Title:  FEMS yeast research     Volume:  10     ISSN:  1567-1364     ISO Abbreviation:  FEMS Yeast Res.     Publication Date:  2010 Sep 
Date Detail:
Created Date:  2010-08-11     Completed Date:  2010-11-24     Revised Date:  -    
Medline Journal Info:
Nlm Unique ID:  101085384     Medline TA:  FEMS Yeast Res     Country:  England    
Other Details:
Languages:  eng     Pagination:  708-16     Citation Subset:  IM    
Molecular Cell Biology, University of Groningen, AA Haren, The Netherlands.
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MeSH Terms
Alanine / 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
Reg. No./Substance:
0/Culture Media; 56-41-7/Alanine; EC Oxidase; EC Carboxylase

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