Alcohol oxidase of methylotrophic thermo- and acidotolerant yeast Hansenula sp.
Electrophoretic analysis of alcohol oxidase purified from the methylotrophic thermo- and acidotolerant yeast Hansenula sp. revealed the presence of two active forms of the enzyme with molar mass 440 kg/mol (major component) and 724 kg/mol (minor component). A subunit M of the enzyme was found to be 72 kg/mol. Two active forms of the enzyme found by electrophoresis seem to be caused by dissociation of the octameric form to the tetramer under alkaline conditions. Studies of alcohol oxidase showed a kinetic variability of the enzyme with respect to its Km. It is proposed that the variability of Km is caused by enzyme binding to formaldehyde.
Bystrykh
L V
LV
Institute of Biochemistry and Physiology of Microorganism, Academy of Sciences, Pushchino, Moscow region, USSR.
Dvoráková
J
J
Volfová
O
O
D000429:Alcohol Oxidoreductases / Q000302:isolation & purification / Q000378:metabolism*; D002851:Chromatography, High Pressure Liquid; D004591:Electrophoresis, Polyacrylamide Gel; D006863:Hydrogen-Ion Concentration; D007700:Kinetics; D046911:Macromolecular Substances; D010843:Pichia / Q000201:enzymology*; D004718:Saccharomycetales / Q000201:enzymology*
D046911:Macromolecular Substances; D000429:Alcohol Oxidoreductases