Inactivation of Escherichia coli L-threonine dehydrogenase by 2,3-butanedione

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Inactivation of Escherichia coli L-threonine dehydrogenase by 2,3-butanedione. Evidence for a catalytically essential arginine residue.

Incubation of homogeneous preparations of L-threonine dehydrogenase from Escherichia coli with 2,3-butanedione, 2,3-pentanedione, phenylglyoxal, or 1,2-cyclohexanedione causes a time- and concentration-dependent loss of enzymatic activity; plots of log percent activity remaining versus time are linear to greater than 90% inactivation, indicative of pseudo-first order inactivation kinetics. The ...

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Inactivation of Escherichia coli elongation factor Tu by the arginine-specific reagent butanedione.

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Inactivation of Escherichia coli Elongation Factor T, by the Arginine- specific Reagent Butanedione*

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ژورنال

عنوان ژورنال: Journal of Biological Chemistry

سال: 1989

ISSN: 0021-9258

DOI: 10.1016/s0021-9258(18)51462-9