title: Deletion mutagenesis of human tyrosine hydroxylase type 1 regulatory domain.
abstract: A series of N-terminal deletion mutants of human tyrosine hydroxylase type 1 has been expressed in Escherichia coli to characterize the N-terminal regulatory domain. The mutants lacking the first 74 to 117 amino acids led to the precipitation into aggregates probably due to improper folding. All of the deletion mutants are active in the lysate supernatant and/or the pellet. The Michaelis constants of pterins are similar among all the mutants examined and the wild-type.
authors.affiliation: Joint Research Division for Therapies against Intractable Diseases, School of Medicine, Fujita Health University, Aichi, Japan.
authors.forename: A
authors.initials: A
authors.lastname: Ota
authors.forename: S
authors.initials: S
authors.lastname: Yoshida
authors.forename: T
authors.initials: T
authors.lastname: Nagatsu
mesh_terms: D000595:Amino Acid Sequence; D001483:Base Sequence; D001665:Binding Sites; D003001:Cloning, Molecular; D018076:DNA, Complementary; D004926:Escherichia coli / Q000235:genetics; D006801:Humans; D007700:Kinetics; D008969:Molecular Sequence Data; D017384:Sequence Deletion; D017386:Sequence Homology, Amino Acid; D014446:Tyrosine 3-Monooxygenase / Q000737:chemistry / Q000235:genetics*
chemical_list: D018076:DNA, Complementary; D014446:Tyrosine 3-Monooxygenase