The dissociated tryptophanase subunit is inactive.
作者： O Raibaud , M E Goldberg
DOI: 10.1016/S0021-9258(17)33562-7
关键词: Molecule 、 Dissociation (chemistry) 、 Dimer 、 Tryptophanase 、 Hofmeister series 、 Kinetics 、 Cofactor 、 Stereochemistry 、 Chemistry 、 Reaction rate constant 、 Cell biology 、 Biochemistry 、 Molecular biology
摘要: The dissociation into dimers of apotryptophanase has been studied from two points view: the nature interactions which govern dimer-tetramer equilibrium and effect on functional properties enzyme. It is shown that order in different anions are able to shift Hofmeister series, thus showing main contribution interaction between hydrophobic nature. also that, when dimeric incubated presence its cofactor substrate, kinetics appearance active molecules second enzyme independent pyridoxal-P concentration; rate constant determined (5-10(4) M-1 S-1). These results indicate reassociation tetramers rate-limiting step enzymatic activity, tryptophanase dimer not functional.
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