Mutational analysis of catecholamine binding in tyrosine hydroxylase

Biochemistry

Volumn 50, Issue 9, 2011, Pages 1545-1555

  Briggs, Gabrielle D ^a   Gordon, Sarah L ^a,b   Dickson, Phillip W ^a  

^a HUNTER MEDICAL RESEARCH INSTITUTE   (Australia)

^b UNIVERSITY OF EDINBURGH   (United Kingdom)

Author keywords

[No Author keywords available]

Indexed keywords

ACTIVE SITE; ACTIVE SITE RESIDUES; ACTIVE SITE STRUCTURE; COFACTORS; HIGH AFFINITY BINDING; HIGH-AFFINITY SITES; MUTATIONAL ANALYSIS; RATE-LIMITING STEPS; TETRAHYDROBIOPTERIN; TETRAMERS; TYROSINE HYDROXYLASE; WILD TYPES;

AMINO ACIDS; BIOCHEMISTRY; COENZYMES; OLIGOMERS; PHOSPHORYLATION;

BINDING SITES;

CATECHOLAMINE; DOPAMINE; TETRAHYDROBIOPTERIN; TYROSINE 3 MONOOXYGENASE;

ARTICLE; BINDING AFFINITY; BINDING COMPETITION; BIOCATALYSIS; CATECHOLAMINE SYNTHESIS; CONTROLLED STUDY; DISSOCIATION; ENZYME ACTIVE SITE; ENZYME ACTIVITY; ENZYME BINDING; ENZYME INHIBITION; ENZYME PHOSPHORYLATION; ENZYME STRUCTURE; FEEDBACK SYSTEM; MUTATIONAL ANALYSIS; NONHUMAN; PRIORITY JOURNAL; REGULATORY MECHANISM; WILD TYPE;

CATALYTIC DOMAIN; CATECHOLAMINES; DNA MUTATIONAL ANALYSIS; ESCHERICHIA COLI; GENE EXPRESSION REGULATION, ENZYMOLOGIC; PROTEIN BINDING; TYROSINE 3-MONOOXYGENASE;

EID: 79952122319     PISSN: 00062960     EISSN: 15204995     Source Type: Journal    
DOI: 10.1021/bi101455b     Document Type: Article

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