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Volumn 39, Issue 32, 2000, Pages 9652-9661

Reversing the substrate specificities of phenylalanine and tyrosine hydroxylase: Aspartate 425 of tyrosine hydroxylase is essential for L-DOPA formation

(3) Daubner, S C a Melendez, J a Fitzpatrick, P F a

a TEXAS A AND M UNIVERSITY (United States)

Author keywords

[No Author keywords available]

Indexed keywords

LEVODOPA; PHENYLALANINE 4 MONOOXYGENASE; TYROSINE 3 MONOOXYGENASE;

AMINO ACID SEQUENCE; ARTICLE; DOPAMINE METABOLISM; ENZYME ACTIVITY; ENZYME SPECIFICITY; ENZYME SUBSTRATE COMPLEX; NONHUMAN; PRIORITY JOURNAL; STRUCTURE ACTIVITY RELATION;

ASPARTIC ACID; CATALYTIC DOMAIN; HYDROXYLATION; KINETICS; LEVODOPA; MODELS, MOLECULAR; MOLECULAR SEQUENCE DATA; MUTATION; PEPTIDE FRAGMENTS; PHENYLALANINE HYDROXYLASE; SEQUENCE ANALYSIS, PROTEIN; SEQUENCE DELETION; SEQUENCE HOMOLOGY, AMINO ACID; SUBSTRATE SPECIFICITY; TYROSINE 3-MONOOXYGENASE;

EID: 0034664038 PISSN: 00062960 EISSN: None Source Type: Journal
DOI: 10.1021/bi000493k Document Type: Article

Times cited : (44)

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