Document Detail

Human carbonyl and aldose reductases: new catalytic functions in tetrahydrobiopterin biosynthesis.
MedLine Citation:
PMID:  1902669     Owner:  NLM     Status:  MEDLINE    
New catalytic functions of human carbonyl- and aldose reductase in tetrahydrobiopterin biosynthesis are proposed. 6-Pyruvoyl tetrahydropterin, an intermediate in the biosynthesis of tetrahydrobiopterin, was converted to 6-lactoyl tetrahydropterin and 1'-hydroxy-2'-oxopropyl tetrahydropterin by carbonyl reductase under anaerobic condition. 1'-Hydroxy-2'-oxopropyl tetrahydropterin was subsequently metabolized to tetrahydrobiopterin by aldose reductase. Based on these results alternative pathways for the synthesis of tetrahydrobiopterin in patients with genetic defects of sepiapterin reductase are suggested.
Y S Park; C W Heizmann; B Wermuth; R A Levine; P Steinerstauch; J Guzman; N Blau
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Publication Detail:
Type:  Journal Article; Research Support, Non-U.S. Gov't    
Journal Detail:
Title:  Biochemical and biophysical research communications     Volume:  175     ISSN:  0006-291X     ISO Abbreviation:  Biochem. Biophys. Res. Commun.     Publication Date:  1991 Mar 
Date Detail:
Created Date:  1991-06-05     Completed Date:  1991-06-05     Revised Date:  2014-03-18    
Medline Journal Info:
Nlm Unique ID:  0372516     Medline TA:  Biochem Biophys Res Commun     Country:  UNITED STATES    
Other Details:
Languages:  eng     Pagination:  738-44     Citation Subset:  IM    
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MeSH Terms
Alcohol Oxidoreductases / isolation & purification,  metabolism*
Aldehyde Reductase / isolation & purification,  metabolism*
Biopterin / analogs & derivatives*,  biosynthesis
Brain / enzymology
Chromatography, Gel
Reg. No./Substance:
17528-72-2/5,6,7,8-tetrahydrobiopterin; 22150-76-1/Biopterin; EC 1.1.-/Alcohol Oxidoreductases; EC reductase; EC Reductase; EC reductase (NADPH)

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