Conserved supersecondary structural motif in NAD-dependent dehydrogenases
نویسندگان
چکیده
منابع مشابه
Inhibition studies of dehydrogenases by structural analogues of NAD.
The coenzyme anologues [3-(2-acetylpyridinio) propyl]-adenosine pyrophosphate and [3-(2-bromoacetylpyridinio) -propyl] -adenosine pyrophoshate were synthesized and used for inhibition studies. While the first compound reacts as competitive inhi bitor against NAD+, the latter is able to form co valently bound derivatives of several NAD+-dependent dehydrogenases, giving informations about amino...
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In the Gram-positive methylotroph Bacillus methanolicus, methanol oxidation is catalyzed by an NAD-dependent methanol dehydrogenase (Mdh) that belongs to the type III alcohol dehydrogenase (Adh) family. It was previously shown that the in vitro activity of B. methanolicus Mdh is increased by the endogenous activator protein Act, a Nudix hydrolase. Here we show that this feature is not unique, b...
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The electrochemical detection of dehydrogenase activity in crude cell lysates is performed simultaneously using 96 carbon electrodes modified with electrografted phenazines. The method is applied to the screening of a library of formate dehydrogenase mutants obtained by directed evolution.
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Mycobacterium vaccae 10 growing in methanol medium synthesizes two inducible alternative NAD(+)-dependent formate dehydrogenases (FDH). In the presence of molybdenum, the dominating form of the enzyme is FDHI with Mr 440 kDa and Km 0.32 mM for sodium formate. FDHI reduced ferricyanide as well as NAD+, and it was reversibly inactivated by formate. NAD+ stabilized FDHI against this inactivation. ...
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In Aspergillus nidulans three alcohol dehydrogenases (ADHs) have been described. ADHI is induced by ethanol and is the physiological enzyme of ethanol utilization, ADHII has not been attributed a function but is repressed by ethanol. The ALCR regulatory protein acts positively to induce ADHI, and negatively in its control of ADHII. ADHIII is specifically induced by anaerobic stress. We have cha...
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ژورنال
عنوان ژورنال: FEBS Letters
سال: 1998
ISSN: 0014-5793
DOI: 10.1016/s0014-5793(98)00074-x