Article: article from journal or magazin.
Stabilization of the oxy form of tyrosinase by a single conservative amino acid substitution
Comparative Study Journal Article Research Support, Non-U.S. Gov't --- Old month value: Mar 15
Asp-208 of Streptomyces glaucescens tyrosinase (an invariant residue in the CuB-binding region of tyrosinases and haemocyanins) was conservatively substituted by glutamic acid. Although having little effect on spectroscopic or kinetic properties of the enzyme, the mutation greatly decreased the lability of Cu-bound O2. A rationalization for these results is given, based on the crystal structure of Panuliris interruptus haemocyanin in the conserved CuB-binding region.
Amino Acid Sequence Animals Arthropods/enzymology/genetics Aspartic Acid/*chemistry/genetics/metabolism Base Sequence Copper/chemistry Enzyme Stability Glutamates/*chemistry/genetics/metabolism Glutamic Acid Kinetics Molecular Sequence Data Monophenol Monooxygenase/*chemistry/genetics/metabolism Mutagenesis, Site-Directed Oxidation-Reduction Protein Conformation Sequence Homology, Nucleic Acid Spectrophotometry Streptomyces/enzymology/genetics
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