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Literature summary for 1.13.12.7 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)

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

Protein Variants

Protein Variants Comment Organism
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
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
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
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]

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

Organism

Organism UniProt Comment Textmining
Photinus pyralis
-
-
-
Pyrophorus plagiophthalamus
-
-
-

Purification (Commentary)

Purification (Comment) Organism
-
Photinus pyralis

Storage Stability

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

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
5,5-dimethyl-luciferyl-O-adenosine monophosphate + ?
-
Photinus pyralis 5,5-dimethyloxyluciferin + hv
-
?
5,5-dimethyl-luciferyl-O-adenosine monophosphate + ?
-
Pyrophorus plagiophthalamus 5,5-dimethyloxyluciferin + hv
-
?
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 ?
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 ?
luciferyl-O-adenosine monophosphate + ?
-
Photinus pyralis ?
-
?
luciferyl-O-adenosine monophosphate + ?
-
Pyrophorus plagiophthalamus ?
-
?

pH Optimum

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