Expression, purification and enzymatic characterization of the catalytic domains of human tryptophan hydroxylase isoforms
| Autor: | Pernille Efferbach Karlsen, Jane Boesen, Hans Erik Mølager Christensen, Michael Skovbo Windahl |
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| Rok vydání: | 2009 |
| Předmět: |
chemistry.chemical_classification
Gene isoform Tyrosine hydroxylase Organic Chemistry Tryptophan Gene Expression Bioengineering Tetrahydrobiopterin Tryptophan hydroxylase Tryptophan Hydroxylase Biochemistry Molecular biology Analytical Chemistry Kinetics Enzyme chemistry Catalytic Domain medicine Humans Protein Isoforms Enzyme kinetics Serotonin medicine.drug |
| Zdroj: | The protein journal. 28(9-10) |
| ISSN: | 1875-8355 |
| Popis: | 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. |
| Databáze: | OpenAIRE |
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