Journal
BIOCHEMISTRY
Volume 41, Issue 42, Pages 12569-12574Publisher
AMER CHEMICAL SOC
DOI: 10.1021/bi026561f
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- NICHD NIH HHS [HD38718] Funding Source: Medline
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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 Angstrom) 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 family-tyrosine hydroxylase, phenylalanine hydroxylase, and tryptophan hydroxylase-reveals important differences at the active sites.
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