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Journal article

A simple two step procedure for purification of the catalytic domain of chicken tryptophan hydroxylase 1 in a form suitable for crystallization

By Windahl, Michael Skovbo1; Petersen, Charlotte R.; Munch, Astrid1,2; Vendelboe, Trine Vammen1,2; Boesen, Jane1,2; Harris, Pernille1,3; Christensen, Hans Erik Mølager1,2

From

Department of Chemistry, Technical University of Denmark1

Metalloprotein Chemistry and Engineering, Department of Chemistry, Technical University of Denmark2

X-ray Crystallography, Department of Chemistry, Technical University of Denmark3

Tryptophan hydroxylase (TPH) [EC 1.14.16.4] catalyzes the conversion of tryptophan to 5-hydroxytryptophan, which is the first and rate-determining step in the biosynthesis of the neurotransmitter serotonin. We have expressed the catalytic domain of chicken (Gallus gallus) TPH isoform 1 in Escherichia coli in high yield.

The enzyme was highly purified using only one anion exchange and one gel filtration, with a yield of 11 mg/L culture and a specific activity of 0.60 μmol/min/mg. The Km values were determined to Km,tryptophan = 7.7 ± 0.7 μM, Km,BH4=324±10 μM and Km,O2=39±2 μM. Substrate inhibition by tryptophan was observed at concentrations above 15 μM.

Furthermore, the purified enzyme has been crystallized without 7,8-dihydro-l-biopterin and a data set to 3 Å resolution has been collected.

Language: English
Year: 2008
Pages: 116-126
ISSN: 10960279 and 10465928
Types: Journal article
DOI: 10.1016/j.pep.2007.10.016
ORCIDs: Harris, Pernille and Christensen, Hans Erik Mølager
Keywords

Amino Acid Sequence Animals Biotechnology Catalytic Domain Chickens Chromatography, Gel Chromatography, Ion Exchange Crystallography, X-Ray Electrophoresis, Polyacrylamide Gel Humans Kinetics Molecular Sequence Data Sequence Alignment Tryptophan Hydroxylase

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