spacer

Overview for MACiE Entry M0128

Version history

General Information

EC Number: 1.13.12.7 (A member of the Oxidoreductases, Acting on single donors with O2 as oxidant and incorporation of oxygen into the substrate (oxygenases). The oxygen incorporated need not be derived from O2, With incorporation of one atom of oxygen (internal monooxygenases or internal mixed-function oxidases))

Enzyme Name: photinus-luciferin 4-monooxygenase

Biological Species: Photinus pyralis (North american firefly)

Catalytic Chain UniprotKB Accession Codes:

  • P08659 - Luciferin 4-monooxygenase

Representative PDB Code: 1ba3 - FIREFLY LUCIFERASE IN COMPLEX WITH BROMOFORM (Resolution = 2.20 Å).

Catalytic CATH Codes:

"Other" CATH Codes:

Display structure information

Overall Reaction:

Image of oxygen

Image of ATP

Image of photinus luciferin

right arrow

Image of carbon dioxide

Image of AMP

Image of photon

Image of diphosphate

Image of oxidised photinus luciferin

oxygen
C00007
CHEBI:15379
ATP
C00002
CHEBI:30616
photinus luciferin
C02740
CHEBI:17165
carbon dioxide
C00011
CHEBI:16526
AMP
C00020
CHEBI:456215
photon
C00205
CHEBI:30212
diphosphate
C00013
CHEBI:33019
oxidised photinus luciferin
C03797
CHEBI:16792

Overall Comment: Partial reactions are catalysed by two different conformations of the enzyme. Adenylation in the PheA closed conformation and thioester formation in the bAcs rotated form. Lys443 and Lys529 are located on opposite sides of the C-terminal domain of the enzyme and are each essential for only one of the partial reactions of firefly bioluminescence supporting the proposal of two different conformations catalysing the two half-reactions [1]. The multistep oxidation of firefly luciferin results in the production of excited oxyluciferin. Luciferase modulates emission colour by controlling the resonance-based charge delocalisation of the anionic keto form of the oxyluciferin excited state. The key residues Arg218 His245 Phe247 Thr343 Ala348 and Asp422 are absolutely conserved among luciferases and have major roles in the modulation of emission colour [4]. While CoA is not required for bioluminescence the cofactor does have a stimulatory effect on light production [1]. ATP is also an allosteric modulator of luciferase, with two putative allosteric sites [3].


View similar reactions


Stepwise Description of the Reaction

Step 1The carboxylate oxygen of photinus luciferin attacks the alpha-phosphate of ATP in a nucleophilic substitution reaction, producing the pyrophosphate product.
Step 2Water deprotonates the luciferin intermediate at the C4 atom resulting in a carbanionic intermediate
Step 3The carbanion attacks dioxygen in a nucleophilic addition.
Step 4The peroxide anion attacks the carbonyl carbon in an intramolecular nucleophilic substitution, resulting in the formation of the AMP product and a 4-membered peroxo ring intermediate.
Step 5Carbon dioxide is eliminated from the intermediate with concomitant production of a photon.

View similar reactions (composite manual annotation)


Catalytic Residues Involved

Type Number Chain Location of Function
Thr 343 A Side Chain
Main Chain Amide
Lys 443 A Side Chain
Lys 529 A Side Chain

Metal Cofactors for M0128

Type Het group Number Chain
magnesium MG(not in PDB) 1 x Overview

References

  1. B. R. Branchini et al. (2005), Biochemistry, 44, 1385-1393. Mutagenesis evidence that the partial reactions of firefly bioluminescence are catalyzed by different conformations of the luciferase C-terminal domain.
    Medline: 15683224
  2. B. R. Branchini et al. (1998), Biochemistry, 37, 15311-15319. Site-directed mutagenesis of histidine 245 in firefly luciferase: a proposed model of the active site.
    Medline: 9799491
  3. V. R. Viviani (2002), Cell. Mol. Life Sci., 59, 1833-1850. The origin, diversity, and structure function relationships of insect luciferases.
    Medline: 12530517
  4. B. R. Branchini et al. (2004), Biochemistry, 43, 7255-7262. An alternative mechanism of bioluminescence color determination in firefly luciferase.
    Medline: 15182171
  5. B. R. Branchini et al. (2000), Biochemistry, 39, 5433-5440. The role of lysine 529, a conserved residue of the acyl-adenylate-forming enzyme superfamily, in firefly luciferase.
    Medline: 10820015
  6. J.-Y. Koo et al. (1978), Proc. Natl Acad. Sci. USA, 75, 30-33. Bioluminescence of the firefly: key steps in the formation of the electronically excited state for model systems.
    Medline: 272645
  7. T. Nakatsu et al. (2006), Nature, 440, 372-376. Structural basis for the spectral difference in luciferase bioluminescence.
    Medline: 16541080

Homologue information for M0128 (1ba3)

CSA Homologues

MACiE Homologues (within the PDB)

MACiE Homologues (within UniprotKB/SwissProt)


Links to this entry in other databases

Link to EC-PDB-SUM Link to PDB-SUM Link to RCSB PDB Link to PDBe Link to CSA
Link to MetaCyc Link to KEGG Link to BRENDA Link to ExplorENZ
Link to EzCatDB

GOA logo
nucleotide binding (molecular function)
catalytic activity (molecular function)
monooxygenase activity (molecular function)
ATP binding (molecular function)
peroxisome (cellular component)
metabolic process (biological process)
bioluminescence (biological process)
oxidoreductase activity (molecular function)
metal ion binding (molecular function)
Photinus-luciferin 4-monooxygenase (ATP-hydrolyzing) activity (molecular function)
oxidation-reduction process (biological process)
spacer
spacer