Document Detail

Creatinine inhibits D-amino acid oxidase.
MedLine Citation:
PMID:  12053066     Owner:  NLM     Status:  MEDLINE    
Inhibition of D-amino acid oxidase (DAO) activity by various uremic retention products and guanidino compounds was investigated. Creatinine (CTN) was found to inhibit DAO at a similar concentration in the sera of uremic patients. The inhibition was competitive and the K(i) value was 2.7 mM. Moreover, CTN was shown to interact with flavin adenine dinucleotide (FAD), a coenzyme of DAO. The UV spectral change of FAD bound to DAO was observed in the visible region by addition of CTN. These findings suggest that the increase in serum and tissue CTN concentrations might be responsible, in part, for the increase in D-amino acids in the sera of uremic patients.
Y Nohara; J Suzuki; T Kinoshita; M Watanabe
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Publication Detail:
Type:  In Vitro; Journal Article    
Journal Detail:
Title:  Nephron     Volume:  91     ISSN:  0028-2766     ISO Abbreviation:  Nephron     Publication Date:  2002 Jun 
Date Detail:
Created Date:  2002-06-07     Completed Date:  2003-02-07     Revised Date:  2006-11-15    
Medline Journal Info:
Nlm Unique ID:  0331777     Medline TA:  Nephron     Country:  Switzerland    
Other Details:
Languages:  eng     Pagination:  281-5     Citation Subset:  IM    
Copyright Information:
Copyright 2002 S. Karger AG, Basel
Faculty of Pharmaceutical Sciences, Teikyo University, Sagamiko, Kanagawa, Japan.
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MeSH Terms
Alanine / blood
Alanine Transaminase / metabolism
Creatinine / blood,  pharmacology*
D-Amino-Acid Oxidase / antagonists & inhibitors*,  metabolism*
Enzyme Activation / drug effects
Flavin-Adenine Dinucleotide / metabolism
Serine / blood
Uremia / enzymology*
Reg. No./Substance:
146-14-5/Flavin-Adenine Dinucleotide; 56-41-7/Alanine; 56-45-1/Serine; 60-27-5/Creatinine; EC Oxidase; EC Transaminase

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