Stabilization of the oxy form of tyrosinase by a single conservative amino acid substitution

Details

Serval ID
serval:BIB_D2BFF3214953
Type
Article: article from journal or magazin.
Collection
Publications
Institution
Title
Stabilization of the oxy form of tyrosinase by a single conservative amino acid substitution
Journal
Biochemical Journal
Author(s)
Jackman  M. P., Huber  M., Hajnal  A., Lerch  K.
ISSN
0264-6021 (Print)
Publication state
Published
Issued date
03/1992
Volume
282
Number
3
Pages
915-918
Notes
Comparative Study Journal Article Research Support, Non-U.S. Gov't --- Old month value: Mar 15
Abstract
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.
Keywords
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
Pubmed
Web of science
Create date
25/01/2008 16:39
Last modification date
20/08/2019 15:52
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