The elastolytic properties of subtilisin GX from alkalophilic Bacillus sp. strain 6644 provides a means of differentiation from other subtilisins.
A serine protease exhibiting high activity in alkaline media was purified from alkalophilic Bacillus strain GX6644. The enzyme, subtilisin GX, has a molecular weight of 25,000 and a pI greater than 9.5. The protease exhibited high elastolytic activity, but unlike most elastin hydrolyzing enzymes, elastin hydrolysis and binding were not inhibited by 0.1 M NaCl. The elastolytic properties of subtilisin GX together with its specificity toward amino acid phenyl esters functionally distinguishes this protease from other subtilisins. However, comparisons of the available amino-terminal sequence of subtilisin GX with subtilisins from alkalophilic and neutrophilic Bacillus species revealed extensive homology.
Durham
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W. R. Grace & Co.-Conn., Washington Research Center, Biological Chemistry Research Department, Columbia, MD 21044.
D000595:Amino Acid Sequence; D001407:Bacillus / Q000201:enzymology*; D004549:Elastin / Q000378:metabolism*; D004952:Esters / Q000378:metabolism; D006863:Hydrogen-Ion Concentration; D007526:Isoelectric Point; D008969:Molecular Sequence Data; D008970:Molecular Weight; D010196:Pancreatic Elastase / Q000378:metabolism; D011480:Protease Inhibitors; D017386:Sequence Homology, Amino Acid; D012965:Sodium Chloride / Q000494:pharmacology; D013381:Subtilisins / Q000187:drug effects / Q000235:genetics / Q000378:metabolism*
D004952:Esters; D011480:Protease Inhibitors; D012965:Sodium Chloride; D004549:Elastin; D013381:Subtilisins; D010196:Pancreatic Elastase