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Comparative study of horseradish mutant forms by radioenzymology
Authors:Orlova  M A  Chubar"  T A  Ignatenko  O V  Korzhuev  A V  Gazaryan  I G
Institution:(1) Department of Chemistry, M. V. Lomonosov Moscow State University, Leninskie Gory, 119899 Moscow, Russian Federation
Abstract:Radioenzymology was used to study the recombinant and mutant forms of horseradish peroxidase, namely, F221W, Q176E, Q176A, S35K, E64P, E64S, S35A, and S35KQ176E. Both removal of the Trp residue and introduction of an additional one result in a simpler dose response; the insertion of polar residues stabilizes the enzyme molecule through realization of a more closed conformation. The greatest oscillation changes were found for the replacement by Ala. It was assumed that the binding site of guaiacol as a substrate is located near the residue 64, which is structurally related to the residue 176 and the heme. A scheme of formation of the intermediate through rotation of the Trp aromatic ring was proposed.
Keywords:horseradish peroxidase  recombinant horseradish peroxidase  mutant forms of horseradish peroxidase  F221W  Q176A  Q176E  S35A  S35K  E64P  E64S  S35KQ176E
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