Three-Dimensional Structure of Human Tryptophan Hydroxylase and Its Implications for the Biosynthesis of the Neurotransmitters Serotonin and Melatonin,
- 26 September 2002
- journal article
- research article
- Published by American Chemical Society (ACS) in Biochemistry
- Vol. 41 (42) , 12569-12574
- https://doi.org/10.1021/bi026561f
Abstract
Tryptophan hydroxylase oxidizes l-tryptophan to 5-hydroxy-l-tryptophan in the rate-determining step of serotonin biosynthesis. We have determined the X-ray crystal structure (1.7 Å) of a truncated functional form of human tryptophan hydroxylase with the bound cofactor analogue 7,8-dihydro-l-biopterin, providing the first atomic-resolution information for the catalytic domain of this important enzyme. Comparison of the three-dimensional structures of all three members of the aromatic amino acid hydroxylase familytyrosine hydroxylase, phenylalanine hydroxylase, and tryptophan hydroxylasereveals important differences at the active sites.Keywords
This publication has 1 reference indexed in Scilit:
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