Human liver 6-pyruvoyl tetrahydropterin reductase is biochemically and immunologically indistinguishable from aldose reductase

P Steinerstauch; B Wermuth; W Leimbacher; H C Curtius

doi:10.1016/0006-291x(89)91786-5

Human liver 6-pyruvoyl tetrahydropterin reductase is biochemically and immunologically indistinguishable from aldose reductase

Biochem Biophys Res Commun. 1989 Nov 15;164(3):1130-6. doi: 10.1016/0006-291x(89)91786-5.

Authors

P Steinerstauch¹, B Wermuth, W Leimbacher, H C Curtius

Affiliation

¹ Department of Pediatrics, University of Zurich, Switzerland.

PMID: 2511841
DOI: 10.1016/0006-291x(89)91786-5

Abstract

6-Pyruvoyl tetrahydropterin reductase has been implicated in the biosynthesis of tetrahydrobiopterin. Using immunochemical and biochemical techniques the purified human liver enzyme was shown to be identical to aldose reductase. This suggests that 6-pyruvoyl tetrahydropterin reductase may play an additional role in the reduction of aldehydes derived from the biogenic amine neuro-transmitters and corticosteroid hormones as well as in the pathogenesis of diabetic complications, as has been postulated for aldose reductase.

Publication types

Comparative Study
Research Support, Non-U.S. Gov't

MeSH terms

Aldehyde Reductase / immunology
Aldehyde Reductase / metabolism*
Animals
Antibodies, Monoclonal* / isolation & purification
Blotting, Western
Humans
Immunodiffusion
Ketone Oxidoreductases / immunology
Ketone Oxidoreductases / metabolism*
Kinetics
Liver / enzymology*
Mice
Mice, Inbred BALB C / immunology
Substrate Specificity
Sugar Alcohol Dehydrogenases / metabolism*

Substances

Antibodies, Monoclonal
Sugar Alcohol Dehydrogenases
Aldehyde Reductase
Ketone Oxidoreductases
6-pyruvoyl tetrahydropterin (2'-oxo)reductase