[Identification of catalytically active groups in inulinase from Bacillus polymyxa 722].
Inulinase from Bacillus polymyxa 722 hydrolyzing a polyfructosan inulin was studied. The dependence of inulinase activity on pH, measurements of pK value, calculation of ionization heat, photoinactivation with methylene blue, and inhibition with p-chloromercuribenzoate suggest that the active center of this enzyme contains imidazole and sulfhydryl groups. A possible mechanism underlying cleavage of beta-2,1-fructoside bonds in the inulin molecule with inulinase is considered.
Zherebtsov
N A
NA
Voronezh State Technological Academy, Voronezh, 394017 Russia.
Abramova
I N
IN
Shelamova
S A
SA
Popova
T N
TN
D001407:Bacillus / Q000201:enzymology*; D001665:Binding Sites; D002729:Chloromercuribenzoates / Q000494:pharmacology; D004791:Enzyme Inhibitors / Q000494:pharmacology; D006026:Glycoside Hydrolases / Q000737:chemistry / Q000378:metabolism*; D006863:Hydrogen-Ion Concentration; D007093:Imidazoles / Q000737:chemistry; D007444:Inulin / Q000378:metabolism; D007700:Kinetics; D008751:Methylene Blue / Q000494:pharmacology
D002729:Chloromercuribenzoates; D004791:Enzyme Inhibitors; D007093:Imidazoles; C029899:imidazole; D007444:Inulin; D006026:Glycoside Hydrolases; C023086:inulinase; D008751:Methylene Blue