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Literature summary extracted from

  • Branchini, B.R.; Southworth, T.L.; Murtiashaw, M.H.; Wilkinson, S.R.; Khattak, N.F.; Rosenberg, J.C.; Zimmer, M.
    Mutagenesis evidence that the partial reactions of firefly bioluminescence are catalyzed by different conformations of the luciferase C-terminal domain (2005), Biochemistry, 44, 1385-1393.
    View publication on PubMed

Cloned(Commentary)

EC Number Cloned (Comment) Organism
1.13.12.7 wild-type and mutant enzymes expressed as glutathione-S-transferase-fusion proteins containing the additional N-terminal peptide Gly-Pro-Leu-Gly-SER, which remains after PreScission protease cleavage from GST, expression in Escherichia coli Photinus pyralis

Protein Variants

EC Number Protein Variants Comment Organism
1.13.12.7 G446I turnover number is 8.4fold lower compared to wild-type value, KM-value for D-luciferin is 1.5fold lower compared to wild-type value, KM-value for MgATP2- is 2.2fold lower compared to wild-type value, the bioluminescence emission maximum is 554 nm, compared to 558 nm for the wild-type value. The ratio of turnover-number to KM-value for D-luciferyl-O-adenosine monophosphate is 5.1fold lower compared to wild-type value Photinus pyralis
1.13.12.7 K443A turnover number is 2655 fold lower compared to wild-type value, KM-value for D-luciferin is 6.5fold lower compared to wild-type value, KM-value for MgATP2- is 3.3fold lower compared to wild-type value, the bioluminescence emission maximum is identical to the wild-type value. The ratio of turnover-number to KM-value for D-luciferyl-O-adenosine monophosphate is 181fold lower compared to wild-type value Photinus pyralis
1.13.12.7 K443A/K529A turnover number is 1063700fold lower compared to wild-type value, KM-value for D-luciferin is 4.5fold higher compared to wild-type value, KM-value for MgATP2- is 3.5fold higher compared to wild-type value, the bioluminescence emission maximum is 596 nm, compared to 558 nm for the wild-type value. The ratio of turnover-number to KM-value for D-luciferyl-O-adenosine monophosphate is 858fold lower compared to wild-type value Photinus pyralis
1.13.12.7 K445Q turnover number is 1.4fold higher compared to wild-type value, KM-value for D-luciferin is 1.7fold lower compared to wild-type value, KM-value for MgATP2- is 2.3fold lower compared to wild-type value, the bioluminescence emission maximum is 556 nm, compared to 558 nm for the wild-type value. The ratio of turnover-number to KM-value for D-luciferyl-O-adenosine monophosphate is 1.7fold higher compared to wild-type value Photinus pyralis
1.13.12.7 K529A turnover number is 668fold lower compared to wild-type value, KM-value for D-luciferin is 15.3fold higher compared to wild-type value, KM-value for MgATP2- is 7.5fold higher compared to wild-type value, the bioluminescence emission maximum is 562 nm, compared to 558 nm for the wild-type value. The ratio of turnover-number to KM-value for D-luciferyl-O-adenosine monophosphate is 3.5fold lower compared to wild-type value Photinus pyralis
1.13.12.7 Q448A turnover number is 1.9fold lower compared to wild-type value, KM-value for D-luciferin is 2.5fold lower compared to wild-type value, KM-value for MgATP2- is 2.1fold higher compared to wild-type value, the bioluminescence emission maximum is 557 nm, compared to 558 nm for the wild-type value. The ratio of turnover-number to KM-value for D-luciferyl-O-adenosine monophosphate is 1.1fold lower compared to wild-type value Photinus pyralis

KM Value [mM]

EC Number KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
1.13.12.7 0.00038
-
 D-luciferyl-O-adenosine monophosphate mutant enzyme K443A Photinus pyralis
1.13.12.7 0.00055
-
 D-luciferyl-O-adenosine monophosphate mutant enzyme K443A/K529A Photinus pyralis
1.13.12.7 0.0015
-
 D-luciferyl-O-adenosine monophosphate mutant enzyme G446I Photinus pyralis
1.13.12.7 0.0022
-
 D-luciferyl-O-adenosine monophosphate mutant enzyme Q448A Photinus pyralis
1.13.12.7 0.0023
-
 D-luciferin mutant enzyme K443A Photinus pyralis
1.13.12.7 0.0039
-
 D-luciferyl-O-adenosine monophosphate mutant enzyme K445Q Photinus pyralis
1.13.12.7 0.0047
-
 D-luciferyl-O-adenosine monophosphate wild-type enzyme Photinus pyralis
1.13.12.7 0.006
-
 D-luciferin mutant enzyme G446I Photinus pyralis
1.13.12.7 0.006
-
 D-luciferin mutant enzyme Q448A Photinus pyralis
1.13.12.7 0.0089
-
 D-luciferin mutant enzyme K445Q Photinus pyralis
1.13.12.7 0.0126
-
 D-luciferyl-O-adenosine monophosphate mutant enzyme K529A Photinus pyralis
1.13.12.7 0.015
-
 D-luciferin wild-type enzyme Photinus pyralis
1.13.12.7 0.0486
-
 MgATP2- mutant enzyme K443A Photinus pyralis
1.13.12.7 0.067
-
 D-luciferin mutant enzyme K443A/K529A Photinus pyralis
1.13.12.7 0.069
-
 MgATP2- mutant enzyme K445Q Photinus pyralis
1.13.12.7 0.073
-
 MgATP2- mutant enzyme G446I Photinus pyralis
1.13.12.7 0.16
-
 MgATP2- wild-type enzyme Photinus pyralis
1.13.12.7 0.23
-
 D-luciferin mutant enzyme K529A Photinus pyralis
1.13.12.7 0.341
-
 MgATP2- mutant enzyme Q448A Photinus pyralis
1.13.12.7 0.56
-
 MgATP2- mutant enzyme K443A/K529A Photinus pyralis
1.13.12.7 1.2
-
 MgATP2- mutant enzyme K529A Photinus pyralis

Organism

EC Number Organism UniProt Comment Textmining
1.13.12.7 Photinus pyralis P08659
-
-

Substrates and Products (Substrate)

EC Number Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
1.13.12.7 D-luciferin + O2 + ATP
-
 Photinus pyralis oxidized luciferin + CO2 + H2O + AMP + diphosphate + hv
-
 ?
1.13.12.7 D-luciferyl-O-adenosine monophosphate + ?
-
 Photinus pyralis ?
-
 ?
1.13.12.7 luciferin + MgATP2-
-
 Photinus pyralis AMP + diphosphate
-
 ?

Turnover Number [1/s]

EC Number Turnover Number Minimum [1/s] Turnover Number Maximum [1/s] Substrate Comment Organism Structure
1.13.12.7 0.000000157
-
 MgATP2- mutant enzyme K443A/K529A Photinus pyralis
1.13.12.7 0.000000157
-
 D-luciferin mutant enzyme K443A/K529A Photinus pyralis
1.13.12.7 0.0000311
-
 D-luciferyl-O-adenosine monophosphate mutant enzyme K443A/K529A Photinus pyralis
1.13.12.7 0.0000629
-
 MgATP2- mutant enzyme K443A Photinus pyralis
1.13.12.7 0.0000629
-
 D-luciferin mutant enzyme K443A Photinus pyralis
1.13.12.7 0.000101
-
 D-luciferyl-O-adenosine monophosphate mutant enzyme K443A Photinus pyralis
1.13.12.7 0.00025
-
 MgATP2- mutant enzyme K529A Photinus pyralis
1.13.12.7 0.00025
-
 D-luciferin mutant enzyme K529A Photinus pyralis
1.13.12.7 0.02
-
 MgATP2- mutant enzyme G446I Photinus pyralis
1.13.12.7 0.02
-
 D-luciferin mutant enzyme G446I Photinus pyralis
1.13.12.7 0.021
-
 D-luciferyl-O-adenosine monophosphate mutant enzyme G446I Photinus pyralis
1.13.12.7 0.0875
-
 MgATP2- mutant enzyme Q448A Photinus pyralis
1.13.12.7 0.0875
-
 D-luciferin mutant enzyme Q448A Photinus pyralis
1.13.12.7 0.095
-
 D-luciferyl-O-adenosine monophosphate mutant enzyme Q448A Photinus pyralis
1.13.12.7 0.167
-
 MgATP2- wild-type enzyme Photinus pyralis
1.13.12.7 0.167
-
 D-luciferin wild-type enzyme Photinus pyralis
1.13.12.7 0.175
-
 D-luciferyl-O-adenosine monophosphate mutant enzyme K529A Photinus pyralis
1.13.12.7 0.23
-
 D-luciferyl-O-adenosine monophosphate wild-type enzyme Photinus pyralis
1.13.12.7 0.24
-
 MgATP2- mutant enzyme K445Q Photinus pyralis
1.13.12.7 0.24
-
 D-luciferin mutant enzyme K445Q Photinus pyralis
1.13.12.7 0.32
-
 D-luciferyl-O-adenosine monophosphate mutant enzyme K445Q Photinus pyralis