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metabolism
activity of genes iscU or hscB in the Isc iron-sulfur cluster biosynthesis pathway is required for formation of selenate reductase activity in vivo. Mutant strains JW2513 and JW2511 devoid of either the iscU or hscB gene in the Isc iron–sulfur cluster biosynthesis pathway lose the ability to reduce selenate, phenotypes, overview. Genetic complementation by the wildtype sequences restored selenate reductase activity. The Isc biosynthetic system plays a key role in selenate reductase Fe-S cofactor assembly and is essential for enzyme activity
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the signal peptide binding chaperone that interacts with the selenate reductase (YnfE) signal peptide is called DmsD and it is encoded within the ynfEFGH-dmsD operon. YnfE signal peptide residues L24 and A28 are important for assembly of an active selenate reductase, and DmsD V16 residue is important for signal peptide recognition and selenate reductase assembly, random mutational analysis. DmsD is a member of the TorD/DmsD/NarJ family of peptide binding proteins. Synthetic peptides containing the YnfE binding epitope can be chemically crosslinked to DmsD and signal peptide binding prevents DmsD dimerization in vitro, interaktion analysis, overview
physiological function
cell-free extracts of Alcaligenes sp. CKCr-6A catalyzes the NADH-dependent reduction of selenate and selenite to elemental selenium
physiological function
expression of the srdBCA operon with its own promoter, confers the phenotype of selenate reduction in Escherichia coli. Expression of subunits A, B and C is required for the selenate-reducing phenotype; expression of the srdBCA operon with its own promoter, confers the phenotype of selenate reduction in Escherichia coli. Expression of subunits A, B and C is required for the selenate-reducing phenotype; expression of the srdBCA operon with its own promoter, confers the phenotype of selenate reduction in Escherichia coli. Expression of subunits A, B and C is required for the selenate-reducing phenotype
Results 1 - 4 of 4