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 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.
Tanaka
T
T
Department of Ecological Engineering, Toyohashi University of Technology, Aichi, Japan. tanakat@eco.tut.ac.jp
Kikuchi
Y
Y
Matsuzawa
H
H
Ohta
T
T
D019943:Amino Acid Substitution; D002384:Catalysis; D002413:Cations, Divalent / Q000494:pharmacology*; D003300:Copper / Q000494:pharmacology; D005998:Glycine; D006639:Histidine; D007700:Kinetics; D016297:Mutagenesis, Site-Directed; D009532:Nickel / Q000494:pharmacology; D011994:Recombinant Proteins / Q000737:chemistry / Q000378:metabolism; D012694:Serine; D012697:Serine Endopeptidases / Q000737:chemistry* / Q000378:metabolism*; D013379:Substrate Specificity; D013824:Thermus / Q000201:enzymology; D015032:Zinc / Q000494:pharmacology
D002413:Cations, Divalent; D011994:Recombinant Proteins; D012694:Serine; D006639:Histidine; D003300:Copper; D009532:Nickel; D012697:Serine Endopeptidases; C055102:aqualysin I; D015032:Zinc; D005998:Glycine