6-Methyltetrahydropterin. Isolation and Identification as the Highly Active Hydroxylase Cofactor from Tetrahydrofolate

Tatsuo Mori, Seymour Kaufmant, Thomas Lloyd

Research output: Contribution to journalArticle

21 Scopus citations

Abstract

A purification of freshly reduced tetrahydrofolate by column chromatography has resulted in the separation of the moee active hydroxylase cofactor fraction from authentic tetrahydrofolate. In the present study, the purification of the two fractions is described and their roles as phenylalanine and tyrosine hydroxylase cofactors in previously used mixtures are compared. The moee active fraction has been characterized by physical, chemical, and enzymatic methods as 2-amino-4-hydroxy-6-methyltetrahydropterin. This very active unconjugated reduced pterin is produced in small amounts by the degradation of tetrahydrofolate during catalytic reduction.

Original languageEnglish (US)
Pages (from-to)2330-2336
Number of pages7
JournalBiochemistry
Volume10
Issue number12
DOIs
StatePublished - Jun 1 1971

All Science Journal Classification (ASJC) codes

  • Biochemistry

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