Glu434 is an important amino acid residue for the activity, structure and stability of tyrosine hydroxylase of the silkworm, Bombyx mori

Author:

Li Chao,Chen Yu-hua,Zhang Zhen-wang,Gong Cheng-liang,Han Hong-yan,Xu Wei-an

Publisher

Elsevier BV

Subject

Applied Microbiology and Biotechnology,Biochemistry,Bioengineering

Reference41 articles.

1. Tyrosine hydroxylase: the initial step in norepinephrine biosynthesis;Nagatsu;J Biol Chem,1964

2. Steady-state kinetic mechanism of rat tyrosine hydroxylase;Fitzpatrick;Biochemistry,1991

3. Studies of the rate-limiting step in the tyrosine hydroxylase reaction: alternate substrates, solvent isotope effects, and transition-state analogs;Fitzpatrick;Biochemistry,1991

4. Identification of iron ligands in tyrosine hydroxylase by mutagenesis of conserved histidinyl residues;Daubner;Protein Sci,1995

5. The metal requirement of rat tyrosine hydroxylase;Fitzpatrick;Biochem Biophys Res Commun,1989

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