The mutation of two amino acid residues in the N-terminus of tyrosine hydroxylase (TH) dramatically enhances the catalytic activity in neuroendocrine atT-20 cells

Journal of Neurochemistry

Volumn 82, Issue 1, 2002, Pages 202-206

  Nakashima, Akira ^a   Kaneko, Yoko S ^a   Mori, Keiji ^a   Fujiwara, Kentaro ^a   Tsugu, Toshimitsu ^a   Suzuki, Takahiro ^b   Nagatsu, Toshiharu ^b   Ota, Akita ^a,c  

^a Fujita Health University   (Japan)

^b FUJITA HEALTH UNIVERSITY   (Japan)

^c FUJITA HEALTH UNIVERSITY SCHOOL OF MEDICINE   (Japan)

Author keywords

Dopamine; Feedback inhibition; Mutation; Parkinson's disease; Tyrosine hydroxylase

Indexed keywords

DOPA; DOPAMINE; TYROSINE 3 MONOOXYGENASE;

AMINO ACID SEQUENCE; AMINO ACID SUBSTITUTION; AMINO TERMINAL SEQUENCE; ANIMAL CELL; ARTICLE; DOPAMINE RELEASE; ENZYME MECHANISM; ENZYME PHOSPHORYLATION; GENE MUTATION; MOUSE; NEGATIVE FEEDBACK; NEUROSECRETORY CELL; NONHUMAN; PRIORITY JOURNAL; REGULATORY MECHANISM;

3,4-DIHYDROXYPHENYLACETIC ACID; AMINO ACID SUBSTITUTION; ANIMALS; CATALYSIS; CELL LINE; CELL-FREE SYSTEM; DOPAMINE; FEEDBACK, BIOCHEMICAL; HUMANS; MICE; MUTAGENESIS, SITE-DIRECTED; NEUROSECRETORY SYSTEMS; PHOSPHORYLATION; STRUCTURE-ACTIVITY RELATIONSHIP; TRANSFECTION; TYROSINE 3-MONOOXYGENASE;

ANIMALIA; MAMMALIA;

EID: 0036310290     PISSN: 00223042     EISSN: None     Source Type: Journal    
DOI: 10.1046/j.1471-4159.2002.00921.x     Document Type: Article

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