Expression, purification and enzymatic characterization of the catalytic domains of human tryptophan hydroxylase isoforms

Michael Skovbo Windahl, Jane Boesen, Pernille Efferbach Karlsen, Hans Erik Mølager Christensen

Research output: Contribution to journalJournal articleResearchpeer-review

Abstract

Tryptophan hydroxylase exists in two isoforms: Isoform 1 catalyses the first and rate-limiting step in the synthesis of serotonin in the peripheral parts of the body while isoform 2 catalyses this step in the brain. The catalytic domains of human tryptophan hydroxylase 1 and 2 have been expressed, purified and the kinetic properties have been studied and are compared. Substrate inhibition by tryptophan is observed for isoform 1 but not for isoform 2. Large differences are observed in the K m,tetrahydrobiopterin values for the two isoforms, being >10 times larger for isoform 1 compared to isoform 2.
Original languageEnglish
JournalProtein Journal
Volume28
Issue number9-10
Pages (from-to)400-406
ISSN1572-3887
DOIs
Publication statusPublished - 2009

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