NAD-Linked l(+)-Lactate Dehydrogenase from the Strict Aerobe Alcaligenes eutrophus. 1. Purification and Properties
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منابع مشابه
+)-Lactate Dehydrogenase from the Strict Aerobe Alcaligenes eutrophus
The L( +)-lactate dehydrogenase (EC 1.1.1.27) of Alcaligenes eutrophus catalyzes the NADH-dependent reduction of pyruvate and a few other 2-oxoacids. The K,,, values for NADH, NAD, pyruvate and L( +)-lactate are 0.075 mM, 0.130 mM, 0.820 mM and 7.10 mM, respectively. The reaction follows a rapid equilibrium ordered bi-bi mechanism and involves the formation of a dead-end EBQ complex. The compet...
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Crude soluble extracts of Methylococcus capsulatus strain Bath, grown on methane, were found to contain NAD(P)+-linked formaldehyde dehydrogenase activity. Activity in the extract was lost on dialysis against phosphate buffer, but could be restored by supplementing with inactive, heat-treated extract (70 degrees C for 12 min). The non-dialysable, heat-sensitive component was isolated and purifi...
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The membrane-bound hydrogenase of Alcaligenes eutrophus was solubilized from washed membranes of autotrophically grown cells. The enzyme consists of two types of subunits and is an iron-sulfur protein. A flavin compound was not detected. The enzyme reacts only with few artificial electron acceptors.
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Mutants of Alcaligenes eutrophus which are altered with respect to the utilization of 2,3-butanediol and acetoin were isolated after transposon mutagenesis. The suicide vehicle pSUP5011 was used to introduce the drug resistance transposable element Tn5 into A. eutrophus. Kanamycin-resistant transconjugants of the 2,3-butanediol-utilizing parent strains CF10141 and AS141 were screened for mutant...
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BACKGROUND Various Pseudomonas strains can use L-lactate as their sole carbon source for growth. However, the L-lactate-utilizing enzymes in Pseudomonas have never been identified and further studied. METHODOLOGY/PRINCIPAL FINDINGS An NAD-independent L-lactate dehydrogenase (L-iLDH) was purified from the membrane fraction of Pseudomonas stutzeri SDM. The enzyme catalyzes the oxidation of L-la...
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ژورنال
عنوان ژورنال: European Journal of Biochemistry
سال: 1983
ISSN: 0014-2956,1432-1033
DOI: 10.1111/j.1432-1033.1983.tb07155.x