Effects of dopamine on N-terminus-deleted human tyrosine hydroxylase type 1 expressed in Escherichia coli

Akira Ota, Akira Nakashima, Keiji Mori, Toshiharu Nagatsu

Research output: Contribution to journalArticle

13 Citations (Scopus)

Abstract

N-Terminus deleted mutants and wild-type human tyrosine hydroxylase type I were expressed in Escherichia coli (E. coli) and utilized to investigate the dopamine-induced decrease in the enzyme catalytic activity and also to identify the specific portion in the N-terminus that affects the efficiency of the inhibitory action of dopamine. Supernatants of bacterial lysates were used as enzyme samples. The pH profiles of the enzyme catalytic activity were affected according to the degree of the deletion. The deletion up to 39 amino acid residues was enough to abolish the inhibitory effect of dopamine in the basic pH range. These results suggest that the inhibition by dopamine of tyrosine hydroxylase activity is closely related to the amino acid sequence in the N-terminus of the enzyme.

Original languageEnglish
Pages (from-to)57-60
Number of pages4
JournalNeuroscience Letters
Volume229
Issue number1
DOIs
Publication statusPublished - 20-06-1997

All Science Journal Classification (ASJC) codes

  • Neuroscience(all)

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