Stabilization of the oxy form of tyrosinase by a single conservative amino acid substitution.
- Jackman MP Biochemisches Institut der Universität Zürich, Switzerland.
- Huber M
- Hajnal A
- Lerch K
- 1992-03-15
Published in:
- The Biochemical journal. - 1992
Amino Acid Sequence
Animals
Arthropods
Aspartic Acid
Base Sequence
Copper
Enzyme Stability
Glutamates
Glutamic Acid
Kinetics
Molecular Sequence Data
Monophenol Monooxygenase
Mutagenesis, Site-Directed
Oxidation-Reduction
Protein Conformation
Sequence Homology, Nucleic Acid
Spectrophotometry
Streptomyces
English
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.
- Language
-
- English
- Open access status
- green
- Identifiers
-
- DOI 10.1042/bj2820915
- PMID 1348173
- Persistent URL
- https://folia.unifr.ch/global/documents/30891
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