Purification and characterization of 5-aminolevulinic acid dehydratase from Methanosarcina barken
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منابع مشابه
-Aminolevulinic Acid Dehydratase from Plasmodium falciparum
The heme biosynthetic pathway of the malaria parasite is a drug target and the import of host -aminolevulinate dehydratase (ALAD), the second enzyme of the pathway, from the red cell cytoplasm by the intra erythrocytic malaria parasite has been demonstrated earlier in this laboratory. In this study, ALAD encoded by the Plasmodium falciparum genome (PfALAD) has been cloned, the protein overexpre...
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A hemB mutant of Escherichia coli was used to clone the gene encoding 5-aminolevulinic acid dehydratase from Rhodobacter sphaeroides after physiological complementation of the mutation. A 2.9-kb DNA fragment was obtained and cloned in both orientations into the unique PstI restriction site of pUC19. This recombinant plasmid encodes a protein (Mr 39,000) that is immunoreactive with antibodies ra...
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Purification and Characterization of Glycerol Dehydratase from Lactobacillus reuterit
A coenzyme B12-dependent glycerol dehydratase from Lactobacillus reuteri has been purified and characterized. The dehydratase has a molecular weight of approximately 200,000, and sodium dodecyl sulfatepolyacrylamide gel electrophoresis yielded a single major band with a molecular weight of 52,000. Km values for substrates and coenzyme B12 were in the millimolar and the submicromolar range, resp...
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The activity of S-aminolevulinic acid (ALA) dehydratase. an enzyme involved in heme biosynthesis. has been shown to increase in Friend virus-transformed murine erythroleukemia (MEL) cells during erythroid differentiation. In this study. the nature of the increase in ALA dehydratase activity in MEL cells was examined using a monospecific antibody directed to the enzyme. A sevenfold increase in A...
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ژورنال
عنوان ژورنال: FEMS Microbiology Letters
سال: 1995
ISSN: 0378-1097
DOI: 10.1016/0378-1097(95)00057-c