Myoglobin with peroxidase activity
AssigneeThe University of British Columbia
InventorsGary D. Brayer, Hung Lee, A. Grant Mauk, Michael Smith, Harry Tong, Lianglu Wan
Life of this patent
Estimating the term…
Abstract
Myoglobin is shown to have Manganese (Mn.sup.2') binding and peroxidase capacity. Mn binding and peroxidase activity is enhanced by modification of the amino acid sequence of myoglobin to provide a Mn binding site on the surface of the protein near the heme group. Peroxidase activity of myoglobin not specific to Mn is enhanced by substituting amino acids at residues 39, 45, 46, 97 and 107 of myolglobin.
Claims8
A method of catalysing a reaction with myoglobin in which a substrate is oxidized with a peroxide wherein, a reaction mixture is provided comprising substrate, peroxide and myoglobin, characterized in that the myoglobin has peroxidase activity greater than wild-type and a modified amino acid sequence in which one or more of the following amino acids are substituted:
- Thr 39, Lys/Arg 45, Phe 46, His 97 and He 107.
A method of catalysing oxidation of Mn(II) by hydrogen peroxide with myoglobin comprising:
- (a) mixing Mn(II) substrate, hydrogen peroxide and myoglobin to provide a reaction mixture, and
- (b) maintaining the reaction mixture under conditions appropriate for oxidation of Mn(II) to be catalysed by myoglobin.
Dependencies are inferred from the claim text.