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Showing 1 to 5 of 5 for “"Cysteine Desulfurases"”.

  1. Cysteine Desulfurases Mediating Sulfur Trafficking for the Biosynthesis of Fe-S Clusters

    … to date include the participation of at least a cysteine desulfurase and an Fe-S cluster scaffold. The first step in sulfur mobilization for the assembly of Fe-S clusters as well as other thiocofactors within the cell involves a PLP-dependent enzymatic mechanism, catalyzed by cysteine

    wfu Repository record for Cysteine Desulfurases Mediating Sulfur Trafficking for the Biosynthesis of Fe-S Clusters (opens in a new tab)

  2. Protein Specificity Dictates Proper Sulfur Transfer in the Biosynthesis of Thio-cofactors in Bacteria

    … molecules is predominantly originated from L-cysteine through activation by cysteine desulfurases and is relayed to specific pathways involving the synthesis of thio-cofactors. In this dissertation, we reviewed recent methods for detection and quantification of bacterial thio-nucleosides used …

    wfu Repository record for Protein Specificity Dictates Proper Sulfur Transfer in the Biosynthesis of Thio-cofactors in Bacteria (opens in a new tab)

  3. Biosynthesis and Functions of tRNA 2-Thiouridine in Bacillus subtilis

    Cysteine desulfurases are PLP-dependent enzymes that catalyze the abstraction of sulfur from the free amino acid cysteine in a majority of organisms. Together with their sulfur acceptor proteins, these enzymes are required for the mobilization of sulfur for its incorporation into a wide variety of …

    wfu Repository record for Biosynthesis and Functions of tRNA 2-Thiouridine in Bacillus subtilis (opens in a new tab)

  4. Investigations of conserved structure-function relationships and enzymatic evolution

    … stress and iron starvation. SufS is the cysteine desulfurase enzyme responsible for the acquisition of sulfur and subsequent transfer to transpersulfurase SufE. Recent studies have provided several crystal structures of SufS including two variants displaying stalled intermediates of the …

    alabama Repository record for Investigations of conserved structure-function relationships and enzymatic evolution (opens in a new tab)