Expression, purification and enzymatic characterization of the catalytic domains of human tryptophan hydroxylase
Michael S Windahl1, Jane Boesen, Pernille E Karlsen
1Department of Basic Sciences and Environment, Faculty of Life Sciences, University of Copenhagen, Thorvaldsensvej 40, 1871, Frederiksberg C, Denmark.
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.
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