Kinetics of Inactivation of Phytase (phy A) During Modification of Histidine Residue by IAA and DEP

Title: Kinetics of Inactivation of Phytase (phy A) During Modification of Histidine Residue by IAA and DEP

Volume: 13 Issue: 6

Author(s): Xiao-Yun Wang, Ming-Lv Sun, Dong-Min Zhao and Min Wang

Affiliation:

Keywords: Phytase, inactivation, kinetics, iodoacetic acid, diethylpyrocarbonate

Abstract: Chemical probing of histidine residues using specific modifiers, iodoacetic acid (IAA) and diethylpyrocarbonate (DEP) resulted in the inactivation of phytase (phy A). The kinetic theory of the substrate reaction during the modification of enzyme activity was applied to a study of the kinetics of the course of inactivation of phytase by IAA and DEP. The results suggested that histidine residues are involved in the active site of the enzyme. They also indicated that inactivation of the enzyme by IAA was via a complexing type inhibition, while the inhibition by DEP reaction involved a conformational change step before inactivation. The dissociation constant of the enzyme-inhibitor complex of IAA, the constant of the conformational change of DEP and the microscopic rate constants of two inhibitors were obtained.

Cite this article as:

Wang Xiao-Yun, Sun Ming-Lv, Zhao Dong-Min and Wang Min, Kinetics of Inactivation of Phytase (phy A) During Modification of Histidine Residue by IAA and DEP, Protein & Peptide Letters 2006; 13 (6) . https://dx.doi.org/10.2174/092986606777145788