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Literature summary for 1.13.12.18 extracted from

  • Li, L.; Liu, L.; Hong, R.; Robertson, D.; Hastings, J.W.
    N-terminal intramolecularly conserved histidines of three domains in Gonyaulax luciferase are responsible for loss of activity in the alkaline region (2001), Biochemistry, 40, 1844-1849.
    View publication on PubMed

Cloned(Commentary)

Cloned (Comment) Organism
the three intramolecularly homologous domains are separately cloned and expressed in Escherichia coli JM109 cells as fusion proteins Lingulodinium polyedra

Protein Variants

Protein Variants Comment Organism
additional information for each luciferase domain (D1, D2, D3) the removal of approximately 50 N-terminal amino acids results in an increase in the ratio of luciferase activity at pH 8.0 relative to that at pH 6.3. At pH 8.0, peptides D1167-486, D2535-897, and D3927-1241, lacking the first 55, 47, and 62 amino acids of their N-termini retain about 40%, 50%, and 70% of the pH 6.3 luciferase activity, respectively Lingulodinium polyedra

Organism

Organism UniProt Comment Textmining
Lingulodinium polyedra
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formerly Gonyaulax polyedra
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Purification (Commentary)

Purification (Comment) Organism
glutathione-Sepharose column chromatography Lingulodinium polyedra

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
dinoflagellate luciferin + O2
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Lingulodinium polyedra oxidized dinoflagellate luciferin + H2O + hv
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?

pH Optimum

pH Optimum Minimum pH Optimum Maximum Comment Organism
6.3
-
full-length native enzyme Lingulodinium polyedra

pH Stability

pH Stability pH Stability Maximum Comment Organism
8
-
the activity of the full-length native enzyme drops to near zero at pH 8.0, the activity of domain fragments also peaks at pH 6.3 but remains high at 8.0 Lingulodinium polyedra