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Showing 1 to 6 of 6 for “"Bilin lyase"”.

  1. Characterization of Slr1098, a Protein with Similarity to the Bilin Lyase Subunit CpcE from the Cyanobacterium Synechocystis sp. PCC 6803

    … which encodes a subunit of an enzyme involved in bilin attachment to phycocyanin. This protein is hypothesized to be involved in oligomerization of phycocyanin due to previous results showing the mutant made shorter phycocyanin rods. The recombinant Slr1098 protein was produced and purified from …

    uno Repository record for Characterization of Slr1098, a Protein with Similarity to the Bilin Lyase Subunit CpcE from the Cyanobacterium Synechocystis sp. PCC 6803 (opens in a new tab)

  2. Identification and characterization of enzymes involved in the biosynthesis of different phycobiliproteins in cyanobacteria

    … in soluble form and shown to have intrinsic bilin lyase activity. In addition, this system was used to chromophorylated CpcA from <em><em>Synechococystis sp. </em></em>PCC 6803 with a non-cognate bilin; PEB with the aid of CpcEF type bilin lyase. However, the CpcSU type lyase displays much …

    uno Repository record for Identification and characterization of enzymes involved in the biosynthesis of different phycobiliproteins in cyanobacteria (opens in a new tab)

  3. Development of a novel electron-transfer secondary reaction matrix, characterization of the site–specificity of novel bilin-lyase, and Fundulus grandis protein expression investigation using mass spectrometry

    … the site specificity of a newly developed bilin-lyase enzyme, a new approach was developed to distinguish between A-ring and D-ring attachment of bilins, and <em>F.</em> <em>grandis </em>protein expression pattern was investigated in several tissues. All obtained results were acquired using …

    uno Repository record for Development of a novel electron-transfer secondary reaction matrix, characterization of the site–specificity of novel bilin-lyase, and Fundulus grandis protein expression investigation using mass spectrometry (opens in a new tab)

  4. Characterization of cpeY and cpeZ mutants in Fremyella diplosiphon strain UTEX 481

    … contains covalently attached phycoerythrobilin (PEB) chromophores for efficient photosynthetic light capture. Chromophore ligation on phycobiliprotein subunits occurs through bilin lyase catalyzed reactions. The <em>cpeY </em>and <em>cpeZ</em> genes in <em>F. diplosiphon</em> were shown to …

    uno Repository record for Characterization of cpeY and cpeZ mutants in Fremyella diplosiphon strain UTEX 481 (opens in a new tab)

  5. Novel Design Strategies For Engineering Biliverdin-Binding Fluorescent Proteins

    … Chapter 4, we developed a new NIR-FP based off a bilin lyase protein, a novel scaffold that we hypothesized would have high chromophorylation due to its role as a chaperone protein responsible for bilin attachment in cyanobacteria. Our engineered bilin lyase binds biliverdin and fluoresces in …

    penn Repository record for Novel Design Strategies For Engineering Biliverdin-Binding Fluorescent Proteins (opens in a new tab)

  6. Characterization of Enzymes Involved in Bilin Attachment to Allophycocyanin in the Cyanobacterium Synechococcus sp. PCC 7002

    … to identify and characterize enzymes involved in bilin attachment to the phycobiliprotein allophycocyanin in the cyanobacterium Synechococcus sp. PCC 7002. Candidates for lyases responsible for attachment of phycocyanobilin to allophycocyanin are two cpeS-like genes termed cpcS and cpcU, and one …

    uno Repository record for Characterization of Enzymes Involved in Bilin Attachment to Allophycocyanin in the Cyanobacterium Synechococcus sp. PCC 7002 (opens in a new tab)