Crystal structure of tyrosine hydroxylase with bound cofactor analogue and iron at 2.3 Å resolution: Self-hydroxylation of Phe300 and the pterin- binding site

Biochemistry

Volumn 37, Issue 39, 1998, Pages 13437-13445

  Goodwill, Kenneth E ^a,b   Sabatier, Christelle ^a   Stevens, Raymond C ^a  

^a UNIVERSITY OF CALIFORNIA   (United States)

^b UNIVERSITY OF CALIFORNIA   (United States)

Author keywords

[No Author keywords available]

Indexed keywords

CARBONYL DERIVATIVE; GLUTAMIC ACID; GLUTAMINE; HYDROXYL GROUP; IRON; LEUCINE; LEVODOPA; PHENYLALANINE; PTERIN; TETRAHYDROBIOPTERIN; TETRAMER; TYROSINE 3 MONOOXYGENASE;

ARTICLE; CATECHOLAMINE SYNTHESIS; CRYSTAL STRUCTURE; ENZYME ACTIVE SITE; ENZYME BINDING; ENZYME STRUCTURE; HYDROGEN BOND; HYDROXYLATION; POLYMERIZATION; PRIORITY JOURNAL; PROTEIN DOMAIN;

ANIMALS; BINDING SITES; BIOPTERIN; COENZYMES; CRYSTALLIZATION; CRYSTALLOGRAPHY, X-RAY; HUMANS; HYDROXYLATION; IRON; MODELS, MOLECULAR; MUTAGENESIS, SITE-DIRECTED; PHENYLALANINE; RATS; SPECTROSCOPY, MOSSBAUER; SUBSTRATE SPECIFICITY; TYROSINE 3-MONOOXYGENASE; X-RAYS;

EID: 0032578427     PISSN: 00062960     EISSN: None     Source Type: Journal    
DOI: 10.1021/bi981462g     Document Type: Article

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