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Literature summary for 1.13.12.7 extracted from

  • Branchini, B.R.; Southworth, T.L.; Fontaine, D.M.; Kohrt, D.; Talukder, M.; Michelini, E.; Cevenini, L.; Roda, A.; Grossel, M.J.
    An enhanced chimeric firefly luciferase-inspired enzyme for ATP detection and bioluminescence reporter and imaging applications (2015), Anal. Biochem., 484, 148-153 .
    View publication on PubMedView publication on EuropePMC
Search for more literature for 1.13.12.7

Cloned(Commentary)

Cloned (Comment) Organism
recombinant expression of the chimeric mutant luc2 that contains the N-domain of Photinus pyralis luciferase joined to the C-domain of Luciola italica luciferase in HEK-293 cells and in Escherichia coli strain BL21(DE3)pLysS Photinus pyralis
recombinant expression of the chimeric mutant luc2 that contains the N-domain of Photinus pyralis luciferase joined to the C-domain of Luciola italica luciferase in HEK-293 cells and in Escherichia coli strain BL21(DE3)pLysS Luciola italica

Protein Variants

Protein Variants Comment Organism
additional information construction of a chimeric enzyme luc2 that contains the N-domain of Photinus pyralis luciferase joined to the C-domain of Luciola italica luciferase, the recombinant chimeric enzyme shows 2fold enhanced activity and 1.4fold greater bioluminescence quantum yield compared to the wild-type Photinus pyralis luciferase. Further engineering to enhance thermal and pH stability produces a different luciferase called PLG2, that shows 4.4fold enhanced activity and 2.2fold greater bioluminescence quantum yield compared to the wild-type. Five amino acid changes based on Luciola italica are the main determinants of the improved bioluminescence properties Luciola italica
additional information construction of a chimeric enzyme luc2 that contains the N-domain of Photinus pyralis luciferase joined to the C-domain of Luciola italica luciferase, the recombinant chimeric enzyme shows 2fold enhanced activity and 1.4fold greater bioluminescence quantum yield compared to the wild-type Photinus pyralis luciferase. Further engineering to enhance thermal and pH stability produces a different luciferase called PLG2, that shows 4.4fold enhanced activity and 2.2fold greater bioluminescence quantum yield compared to the wild-type. Five amino acid changes based on Luciola italica are the main determinants of the improved bioluminescence properties, comparison to the Photinus pyralis luciferase wild-type, overview 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
-
 firefly oxyluciferin + CO2 + AMP + diphosphate + hv
-
 ?
D-firefly luciferin + O2 + ATP Luciola italica
-
 firefly oxyluciferin + CO2 + AMP + diphosphate + hv
-
 ?

Organism

Organism UniProt Comment Textmining
Luciola italica Q1AG35
-
-
Photinus pyralis P08659
-
-

Substrates and Products (Substrate)

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

Synonyms

Synonyms Comment Organism
firefly luciferase
-
 Photinus pyralis
Luciola italica luciferase
-
 Luciola italica
PpyWT
-
 Photinus pyralis

Temperature Optimum [°C]

Temperature Optimum [°C] Temperature Optimum Maximum [°C] Comment Organism
37
-
 assay at Photinus pyralis
37
-
 assay at, mutants luc2 and PLG2 Luciola italica

pH Optimum

pH Optimum Minimum pH Optimum Maximum Comment Organism
8
-
 assay at Photinus pyralis
8
-
 assay at, mutants luc2 and PLG2 Luciola italica

Cofactor

Cofactor Comment Organism Structure
ATP
-
 Photinus pyralis
ATP
-
 Luciola italica