Human carbonyl and aldose reductases: new catalytic functions in tetrahydrobiopterin biosynthesis.
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.
Park
Y S
YS
Department of Pediatrics, University of Zürich, Switzerland.
Heizmann
C W
CW
Wermuth
B
B
Levine
R A
RA
Steinerstauch
P
P
Guzman
J
J
Blau
N
N
D000429:Alcohol Oxidoreductases / Q000302:isolation & purification / Q000378:metabolism*; D000449:Aldehyde Reductase / Q000302:isolation & purification / Q000378:metabolism*; D000074408:Aldo-Keto Reductases; D001708:Biopterins / Q000031:analogs & derivatives* / Q000096:biosynthesis; D001921:Brain / Q000201:enzymology; D002850:Chromatography, Gel; D006801:Humans; D007700:Kinetics
D001708:Biopterins; D000429:Alcohol Oxidoreductases; D000074408:Aldo-Keto Reductases; C022630:sepiapterin reductase; D000449:Aldehyde Reductase; C003402:sapropterin