Stabilization of the oxy form of tyrosinase by a single conservative amino acid substitution.
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.
Biochemisches Institut der Universität Zürich, Switzerland.
M P
MP
Jackman
M
M
Huber
A
A
Hajnal
K
K
Lerch
D000595:Amino Acid Sequence; D000818:Animals; D001181:Arthropods / Q000201:enzymology / Q000235:genetics; D001224:Aspartic Acid / Q000737:chemistry* / Q000235:genetics / Q000378:metabolism; D001483:Base Sequence; D003300:Copper / Q000737:chemistry; D004795:Enzyme Stability; D005971:Glutamates / Q000737:chemistry* / Q000235:genetics / Q000378:metabolism; D018698:Glutamic Acid; D007700:Kinetics; D008969:Molecular Sequence Data; D014442:Monophenol Monooxygenase / Q000737:chemistry* / Q000235:genetics / Q000378:metabolism; D016297:Mutagenesis, Site-Directed; D010084:Oxidation-Reduction; D011487:Protein Conformation; D012689:Sequence Homology, Nucleic Acid; D013053:Spectrophotometry; D013302:Streptomyces / Q000201:enzymology / Q000235:genetics
D005971:Glutamates; D001224:Aspartic Acid; D018698:Glutamic Acid; D003300:Copper; D014442:Monophenol Monooxygenase