Primary structure of tyrosinase from Streptomyces glaucescens
Details
Serval ID
serval:BIB_627EC1ED9958
Type
Article: article from journal or magazin.
Collection
Publications
Institution
Title
Primary structure of tyrosinase from Streptomyces glaucescens
Journal
Biochemistry
ISSN
0006-2960 (Print)
Publication state
Published
Issued date
10/1985
Volume
24
Number
22
Pages
6038-44
Notes
Journal Article
Research Support, Non-U.S. Gov't --- Old month value: Oct 22
Research Support, Non-U.S. Gov't --- Old month value: Oct 22
Abstract
The complete amino acid sequence of Streptomyces glaucescens tyrosinase is reported. The molecule consists of 273 amino acids and has a Mr of 30 900 including two copper atoms. The primary structure was determined by a combination of amino acid and DNA sequence analysis. Peptide sequence information was derived from the cyanogen bromide, tryptic, and thermolytic fragments of apotyrosinase by automated Edman degradation and aminopeptidase M and carboxypeptidase C digestions. The nucleotide sequence of the tyrosinase gene cloned into the PvuII site of pBR322 was determined. The enzyme contains no apparent leader peptide despite the fact that it is secreted into the culture medium. As observed for a number of different Streptomyces genes, the tyrosinase gene shows a strong preference (97%) for codons ending in G or C. A comparison of the amino acid sequence of Streptomyces glaucescens tyrosinase with that of Neurospora crassa tyrosinase reveals an overall sequence homology of only 24.2%. However, the sequence homology is much higher in those regions thought to be involved in metal binding of the binuclear active site copper of this monooxygenase.
Keywords
Amino Acid Sequence
Base Sequence
Catechol Oxidase/*isolation & purification
Chromatography, High Pressure Liquid
Cyanogen Bromide
DNA Restriction Enzymes
Monophenol Monooxygenase/genetics/*isolation & purification
Peptide Fragments/analysis
Plasmids
Streptomyces/*enzymology
Trypsin
Pubmed
Web of science
Create date
25/01/2008 16:39
Last modification date
20/08/2019 14:19