Modeled ligand-protein complexes elucidate the origin of substrate specificity and provide insight into catalytic mechanisms of phenylalanine hydroxylase and tyrosine hydroxylase

European Journal of Biochemistry

Volumn 270, Issue 6, 2003, Pages 1065-1075

  Maaß, Astrid ^a   Scholz, Joachim ^b,c   Moser, Andreas ^b  

^a FRAUNHOFER INSTITUTE FOR ALGORITHMS AND SCIENTIFIC COMPUTING SCAI   (Germany)

^b UNIVERSITY OF LÜBECK   (Germany)

^c MASSACHUSETTS GENERAL HOSPITAL   (United States)

Author keywords

Catecholamines; Feedback inhibition; Phenylalanine hydroxylase; Substrate specificity; Tyrosine hydroxylase

Indexed keywords

AMINO ACID; DOPAMINE; LEVODOPA; LIGAND; PHENYLALANINE 4 MONOOXYGENASE; TETRAHYDROBIOPTERIN; TYROSINE; TYROSINE 3 MONOOXYGENASE;

ARTICLE; CATALYSIS; CRYSTAL STRUCTURE; ENZYME ACTIVITY; ENZYME SPECIFICITY; ENZYME SUBSTRATE; LIGAND BINDING; MODEL; NEGATIVE FEEDBACK; NUCLEAR MAGNETIC RESONANCE SPECTROSCOPY; PRIORITY JOURNAL; PROTEIN BINDING; X RAY CRYSTALLOGRAPHY;

AMINO ACID SEQUENCE; ANIMALS; BIOPTERIN; CATALYTIC DOMAIN; DOPAMINE; HUMANS; LEVODOPA; LIGANDS; MODELS, MOLECULAR; MOLECULAR SEQUENCE DATA; MOLECULAR STRUCTURE; PHENYLALANINE; PHENYLALANINE HYDROXYLASE; PROTEIN BINDING; RATS; SEQUENCE ALIGNMENT; SUBSTRATE SPECIFICITY; TYROSINE; TYROSINE 3-MONOOXYGENASE;

EID: 0037351143     PISSN: 00142956     EISSN: None     Source Type: Journal    
DOI: 10.1046/j.1432-1033.2003.03429.x     Document Type: Article

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