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Literature summary for 1.13.12.7 extracted from

  • Jazayeri, F.S.; Amininasab, M.; Hosseinkhani, S.
    Structural and dynamical insight into thermally induced functional inactivation of firefly luciferase (2017), PLoS ONE, 12, e0180667 .
    View publication on PubMedView publication on EuropePMC

Application

Application Comment Organism
biotechnology extensive and advantageous application of this enzyme in biotechnology is restricted due to its low thermal stability Photinus pyralis

Natural Substrates/ Products (Substrates)

Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
D-firefly luciferin + O2 + ATP Photinus pyralis
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firefly oxyluciferin + CO2 + AMP + diphosphate + hv
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?

Organism

Organism UniProt Comment Textmining
Photinus pyralis P08659
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-

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
D-firefly luciferin + O2 + ATP
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Photinus pyralis firefly oxyluciferin + CO2 + AMP + diphosphate + hv
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?
D-firefly luciferin + O2 + ATP molecular dynamic is utilized to simulate free luciferase in explicit solvent at normal and at temperature above its Tm. The results of simulations are analyzed in order to evaluate the structural and dynamical properties of the enzyme Photinus pyralis firefly oxyluciferin + CO2 + AMP + diphosphate + hv
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?

General Information

General Information Comment Organism
physiological function luciferase is the key component of light production in bioluminescence process Photinus pyralis