Doi, Yuko <br/><br/>
Thermal stabilization of penicillolysin, a thermolabile 19 kDa Zn2+-protease, obtained by site-directed mutagenesis.  [electronic resource] 

 -  Protein engineering, design & selection : PEDS  Mar 2004 
 - 261-6 p.  digital 
<br/><br/> Publication Type: Comparative Study; Journal Article 
<br/><br/><label>ISSN: </label>1741-0126 
<br/><br/><label>Standard No.: </label>10.1093/protein/gzh034  doi 
<br/><br/><label>Subjects--Topical Terms: </label><br/>Amino Acid Sequence<br/>Aspergillus--enzymology<br/>Base Sequence<br/>Catalysis<br/>Circular Dichroism<br/>Disulfides<br/>Enzyme Stability<br/>Escherichia coli--genetics<br/>Fungal Proteins--chemistry<br/>Hot Temperature<br/>Isoelectric Point<br/>Kinetics<br/>Metalloendopeptidases--chemistry<br/>Models, Molecular<br/>Molecular Sequence Data<br/>Molecular Weight<br/>Mutagenesis, Site-Directed<br/>Penicillium--chemistry<br/>Protein Structure, Secondary<br/>Recombinant Proteins--chemistry<br/>Sequence Homology, Amino Acid<br/>Spectrophotometry, Atomic<br/>Spectrophotometry, Ultraviolet<br/>Substrate Specificity<br/>Zinc--metabolism