Deuteration of Escherichia coli Enzyme INtr alters its stability
نویسندگان
چکیده
منابع مشابه
Malic Enzyme of Escherichia coli
The TPN+-specitk malic enzyme from Escherichia coli has been purified from malate-grown cells. An approximately loo-fold purified preparation is activated by NH4+ and K+ ions. The enzyme is inhibited by acetyl coenzyme A, oxalacetate, TPNH, and DPNH in an allosteric manner. Glycine at concentration ranges above 0.5 M has been shown to activate the enzyme as well as to desensitize it reversibly ...
متن کاملEnzyme Biosynthesis in Escherichia Coli
Escherichia coli B synthesized beta-galactosidase and an enzyme system for D-xylose when exposed to lactose and xylose respectively in nitrogen-free media. The amount of beta-galactosidase formed in the absence of external nitrogen depended upon the nature of the medium in which the cells had originally been grown. Half as much of this enzyme was synthesized without exogenous nitrogen by cells ...
متن کاملCloning and optimization of phytase enzyme gene expression in Escherichia coli
Introduction Phytase is an enzyme that has the ability to break down phytic acid into myoinositol and mineral phosphate, and widely uses as an additive in animal foods. The aim of this study was to achieve a high level of bacterial phytase expression in PET26b expression host. Materials and Methods To generate the recombinant phytase enzyme, the target gene was introduced into the expression ...
متن کاملThermoregulation of Escherichia coli hchA transcript stability.
The conserved chaperone Hsp31 of Escherichia coli is transcribed at low temperatures by sigma(S) and repressed by H-NS, whereas at high temperature, transcription is by sigma70 independently of both sigma(S) and H-NS. Here we present evidence for an additional, novel, temperature-dependent control of Hsp31 expression by increased transcript stability.
متن کاملS-ribosylhomocysteine cleavage enzyme from Escherichia coli.
Cell-free extracts from Escherichia coli cleave the thioether linkage of S-ribosylhomocysteine and generate free homocysteine. Homocysteine was quantitatively recovered from reaction mixtures by ion exchange chromatography on Amberlite CG-120 resin. Free ribose was not a product of this cleavage; however, a compound initially derived from the ribose moiety of S-ribosylhomocysteine has been isol...
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ژورنال
عنوان ژورنال: Archives of Biochemistry and Biophysics
سال: 2011
ISSN: 0003-9861
DOI: 10.1016/j.abb.2010.12.022