Work

Metabolism of the Phenylalanine Hydroxylation Cofactor

Year: 1967

Type: article

Abstract: A simple chemical method of reducing biopterin to 7,8-dihydrobiopterin has been described. The product of this reaction appears to be identical with the phenylalanine hydroxylation cofactor isolated from rat liver extracts. With the use of the synthetic compound, the TPNH-mediated enzymatic reduction of dihydrobiopterin to the tetrahydro level has been demonstrated. This reduction is catalyzed by dihydrofolate reductase. In the presence of 7,8-dihydrobiopterin, the reductase is an essential component of the phenylalanine-hydroxylating system. The TPN-dependent oxidation of dihydrobiopterin to sepiapterin has been shown to be catalyzed by another enzyme, sepiapterin reductase.

Source: Journal of Biological Chemistry

DOI: 10.1016/s0021-9258(18)95837-0

Author: Seymour Kaufman

Institutions: United States Public Health Service, National Institute of Mental Health

Language: English

Topic: Metabolism and Genetic Disorders

Subfield: Clinical Biochemistry

Field: Biochemistry, Genetics and Molecular Biology

Domain: Life Sciences

Open Access status: hybrid

Estimated APC paid: $3,430

OpenAlex ID: W1669877415

FWCI: 3.962

Cites: 32

Cited by: 180

Related to: 10