Any feedback?
Please rate this page
(literature.php)
(0/150)

BRENDA support

Literature summary extracted from

  • Branchini, B.R.; Southworth, T.L.; Murtiashaw, M.H.; Magyar, R.A.; Gonzalez, S.A.; Ruggiero, M.C.; Stroh, J.G.
    An alternative mechanism of bioluminescence color determination in firefly luciferase (2004), Biochemistry, 43, 7255-7262.
    View publication on PubMed

Cloned(Commentary)

EC Number Cloned (Comment) Organism
1.13.12.7 wild-type and mutant enzymes are expressed as GST-fusion proteins Photinus pyralis
1.13.12.7 wild-type and mutant enzymes are expressed as GST-fusion proteins Pyrophorus plagiophthalamus

Protein Variants

EC Number Protein Variants Comment Organism
1.13.12.7 A243G bioluminescence emission maximum with luciferyl-O-adenosine monophosphate is 599 nm compared to 549 nm for the wild-type enzyme, bioluminescence emission maxima with 5,5-dimethyl-luciferyl-O-adenosine monophosphate are 610 nm and 557 nm compared to 624 nm for the wild-type enzyme Pyrophorus plagiophthalamus
1.13.12.7 F250S bioluminescence emission maximum with luciferyl-O-adenosine monophosphate is 546 nm compared to 552 nm for the wild-type enzyme, bioluminescence emission maxima with 5,5-dimethyl-luciferyl-O-adenosine monophosphate are 631 nm and 552 nm compared to 560 nm for the wild-type enzyme Photinus pyralis
1.13.12.7 G246A bioluminescence emission maximum with luciferyl-O-adenosine monophosphate is 548 nm compared to 552 nm for the wild-type enzyme, bioluminescence emission maximum with 5,5-dimethyl-luciferyl-O-adenosine monophosphate is 578 nm compared to 560 nm for the wild-type enzyme Photinus pyralis
1.13.12.7 S247F bioluminescence emission maximum with luciferyl-O-adenosine monophosphate is 597 nm compared to 549 nm for the wild-type enzyme, bioluminescence emission maximum with 5,5-dimethyl-luciferyl-O-adenosine monophosphate is 612 nm compared to 624 nm for the wild-type enzyme Pyrophorus plagiophthalamus

KM Value [mM]

EC Number KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
1.13.12.7 0.00025
-
 5,5-dimethyl-luciferyl-O-adenosine monophosphate pH 8.6, wild-type enzyme Photinus pyralis
1.13.12.7 0.0003
-
 5,5-dimethyl-luciferyl-O-adenosine monophosphate pH 8.6, mutant enzyme F250S Photinus pyralis
1.13.12.7 0.0003
-
 5,5-dimethyl-luciferyl-O-adenosine monophosphate pH 8.6, mutant enzyme G246A Photinus pyralis
1.13.12.7 0.0003
-
 5,5-dimethyl-luciferyl-O-adenosine monophosphate pH 8.6, wild-type enzyme Pyrophorus plagiophthalamus
1.13.12.7 0.0004
-
 5,5-dimethyl-luciferyl-O-adenosine monophosphate pH 8.6, mutant enzyme A243G Pyrophorus plagiophthalamus
1.13.12.7 0.0006
-
 luciferyl-O-adenosine monophosphate pH 8.6, mutant enzyme A243G Pyrophorus plagiophthalamus
1.13.12.7 0.0008
-
 5,5-dimethyl-luciferyl-O-adenosine monophosphate pH 8.6, mutant enzyme S247F Pyrophorus plagiophthalamus
1.13.12.7 0.0008
-
 luciferyl-O-adenosine monophosphate pH 8.6, wild-type enzyme Pyrophorus plagiophthalamus
1.13.12.7 0.0046
-
 luciferyl-O-adenosine monophosphate pH 8.6, mutant enzyme S247F Pyrophorus plagiophthalamus
1.13.12.7 0.0077
-
 luciferyl-O-adenosine monophosphate pH 8.6, wild-type enzyme Photinus pyralis
1.13.12.7 0.0114
-
 luciferyl-O-adenosine monophosphate pH 8.6, mutant enzyme F250S Photinus pyralis
1.13.12.7 0.0127
-
 luciferyl-O-adenosine monophosphate pH 8.6, mutant enzyme G246A Photinus pyralis

Organism

EC Number Organism UniProt Comment Textmining
1.13.12.7 Photinus pyralis
-
-
-
1.13.12.7 Pyrophorus plagiophthalamus
-
-
-

Purification (Commentary)

EC Number Purification (Comment) Organism
1.13.12.7
-
 Photinus pyralis

Storage Stability

EC Number Storage Stability Organism
1.13.12.7 4°C, 20% loss of activity after 2 weeks Pyrophorus plagiophthalamus
1.13.12.7 4°C, wild-type and mutant enzymes remain fully active for up to 6 months Photinus pyralis

Substrates and Products (Substrate)

EC Number Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
1.13.12.7 5,5-dimethyl-luciferyl-O-adenosine monophosphate + ?
-
 Photinus pyralis 5,5-dimethyloxyluciferin + hv
-
 ?
1.13.12.7 5,5-dimethyl-luciferyl-O-adenosine monophosphate + ?
-
 Pyrophorus plagiophthalamus 5,5-dimethyloxyluciferin + hv
-
 ?
1.13.12.7 luciferin + O2 + ATP
-
 Photinus pyralis oxidized luciferin + CO2 + H2O + AMP + diphosphate + hv luciferase modulates emission color by controlling the resonance-based delocalization of the anionic keto form of the oxyluciferin excited state ?
1.13.12.7 luciferin + O2 + ATP
-
 Pyrophorus plagiophthalamus oxidized luciferin + CO2 + H2O + AMP + diphosphate + hv luciferase modulates emission color by controlling the resonance-based deloclization of the anionic keto form of the oxyluciferin excited state ?
1.13.12.7 luciferyl-O-adenosine monophosphate + ?
-
 Photinus pyralis ?
-
 ?
1.13.12.7 luciferyl-O-adenosine monophosphate + ?
-
 Pyrophorus plagiophthalamus ?
-
 ?

pH Optimum

EC Number pH Optimum Minimum pH Optimum Maximum Comment Organism
1.13.12.7 8.6
-
 reaction with 5,5-dimethyl-luciferyl-O-adenosine monophosphate Photinus pyralis