2.0 Å resolution crystal structures of the ternary complexes of human phenylalanine hydroxylase catalytic domain with tetrahydrobiopterin and 3-(2-thienyl)-L-alanine or L-norleucine: Substrate specificity and molecular motions related to substrate binding

Journal of Molecular Biology

Volumn 333, Issue 4, 2003, Pages 747-757

  Andersen, Ole Andreas ^a   Stokka, Anne J ^b   Flatmark, Torgeir ^b   Hough, Edward ^a  

^a UNIVERSITY OF TROMSØ   (Norway)

^b Dept of Biochem/Molecular Biology ^*  (Norway)

Author keywords

Molecular motions; Phenylalanine hydroxylase; Protein crystallography; Substrate specificity; Tetrahydrobiopterin

Indexed keywords

ASPARAGINE; BETA (2 THIENYL)ALANINE; LEUCINE; NORLEUCINE; PHENYLALANINE 4 MONOOXYGENASE; TETRAHYDROBIOPTERIN; TYROSINE; 3-(2-THIENYL)ALANINE; 5,6,7,8-TETRAHYDROBIOPTERIN; ALANINE; BIOPTERIN; DRUG DERIVATIVE;

ARTICLE; BINDING AFFINITY; CARBOXY TERMINAL SEQUENCE; CATALYSIS; CONFORMATION; CRYSTAL STRUCTURE; ENZYME ACTIVE SITE; ENZYME BINDING; ENZYME SPECIFICITY; ENZYME SUBSTRATE; PRIORITY JOURNAL; PROTEIN DOMAIN; CHEMICAL STRUCTURE; CHEMISTRY; HUMAN; MACROMOLECULE; PROTEIN BINDING; PROTEIN TERTIARY STRUCTURE; X RAY CRYSTALLOGRAPHY;

ALANINE; BIOPTERIN; CATALYTIC DOMAIN; CRYSTALLOGRAPHY, X-RAY; HUMANS; MACROMOLECULAR SUBSTANCES; MODELS, MOLECULAR; NORLEUCINE; PHENYLALANINE HYDROXYLASE; PROTEIN BINDING; PROTEIN STRUCTURE, TERTIARY; SUBSTRATE SPECIFICITY;

EID: 0142106379     PISSN: 00222836     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.jmb.2003.09.004     Document Type: Article

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