Application of a metal switch to aqualysin I, a subtilisin-type bacterial serine protease, to the S3 site residues, Ser102 and Gly131

We applied 'metal switch' experiments to the S3 site residues, Ser102 and Gly131, of aqualysin I, a subtilisin-type serine protease. We showed that two histidines introduced at these positions did take part in histidine-metal-histidine bridge formation, and metal ions inhibited the proteas...

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Bibliographic Details
Published in:Bioscience, biotechnology, and biochemistry biotechnology, and biochemistry, 2000-09, Vol.64 (9), p.2008-2011
Main Authors: Tanaka, T. (Toyohashi Univ. of Technology, Aichi (Japan)), Kikuchi, Y, Matsuzawa, H, Ohta, T
Format: Article
Language:English
Subjects:
Amino Acid Substitution
Aqualysin I
BACTERIA
Biological and medical sciences
Biotechnology
Catalysis
Cations, Divalent - pharmacology
Copper - pharmacology
ENZYME INHIBITORS
Fundamental and applied biological sciences. Psychology
Glycine
HISTIDINE
IONS
Kinetics
metal-switch
METALS
Methods. Procedures. Technologies
Mutagenesis, Site-Directed
Nickel - pharmacology
PROTEASES
Protein engineering
Recombinant Proteins - chemistry
Recombinant Proteins - metabolism
S3 site
SERINE
Serine Endopeptidases - chemistry
Serine Endopeptidases - metabolism
serine proteinase
Substrate Specificity
subtilisin
THERMOPHILIC MICROORGANISMS
Thermus - enzymology
Thermus aquaticus YT-1
Zinc - pharmacology
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Summary:We applied 'metal switch' experiments to the S3 site residues, Ser102 and Gly131, of aqualysin I, a subtilisin-type serine protease. We showed that two histidines introduced at these positions did take part in histidine-metal-histidine bridge formation, and metal ions inhibited the protease activities. These results indicate that two histidines are near each other, and both side chains are metal-accessible. This is the first report on application of the metal-switch technique to a subtilisin-related enzyme.
ISSN:0916-8451
1347-6947
DOI:10.1271/bbb.64.2008