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Threonine deaminase from extremely halophilic bacteria - Cooperative substrate kinetics and salt dependence.The effect of salt on the activity, stability, and allosteric properties of catabolic threonine deaminase from Halobacterium cutirubrum was studied. The enzyme exhibits sigmoidal kinetics with the substrate, threonine. The Hill slope is 1.55 at pH 10. The enzyme is activated by ADP at low substrate concentrations. In the presence of this effector, sigmoidal kinetics are no longer observed. At pH 10, in the absence of ADP, enzyme activity increases with increasing NaCl concentration from 0 to 4 M.
Document ID
19720038869
Document Type
Reprint (Version printed in journal)
Authors
Lieberman, M. M. (Cutter Laboratories Berkeley, Calif., United States)
Lanyi, J. K. (NASA Ames Research Center Exobiology Div., Moffett Field, Calif., United States)
Date Acquired
August 6, 2013
Publication Date
January 1, 1972
Publication Information
Publication: Biochemistry
Volume: 11
Issue: 2, 19
Subject Category
CHEMISTRY
Distribution Limits
Public
Copyright
Other