Journal article
Expression, purification and enzymatic characterization of the catalytic domains of human tryptophan hydroxylase isoforms
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.
| Language: | English |
|---|---|
| Publisher: | Springer US |
| Year: | 2009 |
| Pages: | 400-406 |
| ISSN: | 18758355 , 15723887 , 15734943 and 02778033 |
| Types: | Journal article |
| DOI: | 10.1007/s10930-009-9207-y |
| ORCIDs: | Christensen, Hans Erik Mølager |
Animal Anatomy / Morphology / Histology Aromatic amino acid hydroxylases Biochemistry, general Bioorganic Chemistry Catalytic Domain Chemistry Enzymatic properties Enzyme kinetics Gene Expression Humans Iron-containing enzymes Kinetics Organic Chemistry Protein Isoforms TPH1 protein, human TPH2 protein, human Tetrahydrobiopterin Tryptophan Hydroxylase Tryptophan hydroxylase
