[Effect of pH on the kinetics of the reaction catalyzed by beta-D-hexosaminidase from Halocynthia roretzi].
The analysis of the pH-dependence of Michaelis constant and maximal velocity for the reaction catalyzed by beta-D-hexosaminidase from Halocynthia roretzi revealed two essential ionazable groups of the enzyme. One of them controls substrate binding and has a pKa of 5.5 in free enzyme. The other group (pKa=5.6) is necessary for the occurrence of the catalytic step and appears not to change its pKa on substrate binding.
D000818:Animals; D006596:Hexosaminidases / Q000378:metabolism*; D006863:Hydrogen-Ion Concentration; D007700:Kinetics; D011485:Protein Binding; D014561:Urochordata / Q000201:enzymology*
D006596:Hexosaminidases
Vliianie pN na kinetiku reaktsii, kataliziruemoĭ beta-D-gekoszaminidazoĭ iz Halocynthia roretzi