Journal
PROTEIN JOURNAL
Volume 28, Issue 9-10, Pages 400-406Publisher
SPRINGER
DOI: 10.1007/s10930-009-9207-y
Keywords
Tryptophan hydroxylase; Aromatic amino acid hydroxylases; Enzyme kinetics; Enzymatic properties; Iron-containing enzymes; Tetrahydrobiopterin
Categories
Funding
- Novo Nordisk Foundation [1689]
- The Danish Medical Research Council [271-05-0318]
- The Graduate School on Metal Ions in Biological Systems
- Technical University of Denmark
Ask authors/readers for more resources
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.
Authors
I am an author on this paper
Click your name to claim this paper and add it to your profile.
Reviews
Recommended
No Data Available
Share Paper
