Article
Modulation of the multisubstrate specificity of Thermus maltogenic amylase by truncation of the N-terminal domain and by a salt-induced shift of the monomer/dimer equilibrium.
Biochemistry - 27 Nov 2001
Kim T J, Nguyen V D, Lee H S, Kim M J, Cho H Y, Kim Y W, Moon T W, Park C S, Kim J W, Oh B H, Lee S B, Svensson B, Park K H
Abstract excerpt
The relation between the quaternary structure and the substrate specificity of Thermus maltogenic amylase (ThMA) has been investigated. Sedimentation diffusion equilibrium ultracentrifugation and gel filtration analyses, in combination with the crystal structure determined recently, have demonstrated that ThMA existed in a monomer/dimer equilibrium. The truncation of ThMA by removing the N-terminal domain, which...
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