KEGG ENZYME: 1.13.12.7

ENZYME: 1.13.12.7

Entry

EC 1.13.12.7                Enzyme

Name

firefly luciferase;
Photinus-luciferin 4-monooxygenase (ATP-hydrolysing);
luciferase (firefly luciferin);
Photinus luciferin 4-monooxygenase (adenosine triphosphate-hydrolyzing);
firefly luciferin luciferase;
Photinus pyralis luciferase;
Photinus-luciferin:oxygen 4-oxidoreductase (decarboxylating, ATP-hydrolysing)

Class

Oxidoreductases;
Acting on single donors with incorporation of molecular oxygen (oxygenases);
With incorporation of one atom of oxygen (internal monooxygenases or internal mixed-function oxidases)

Sysname

D-firefly luciferin:oxygen 4-oxidoreductase (decarboxylating, ATP-hydrolysing)

Reaction(IUBMB)

D-firefly luciferin + O2 + ATP = firefly oxyluciferin + CO2 + AMP + diphosphate + hnu [RN:R04036]

Reaction(KEGG)

R04036

Substrate

D-firefly luciferin [CPD:C02740];
O2 [CPD:C00007];
ATP [CPD:C00002]

Product

firefly oxyluciferin [CPD:C03797];
CO2 [CPD:C00011];
AMP [CPD:C00020];
diphosphate [CPD:C00013];
hnu [CPD:C00205]

Comment

The enzyme, which is found in fireflies (Lampyridae), is responsible for their biolouminescence. The reaction begins with the formation of an acid anhydride between the carboxylic group of D-firefly luciferin and AMP, with the release of diphosphate. An oxygenation follows, with release of the AMP group and formation of a very short-lived peroxide that cyclizes into a dioxetanone structure, which collapses, releasing a CO2 molecule. The spontaneous breakdown of the dioxetanone (rather than the hydrolysis of the adenylate) releases the energy (about 50 kcal/mole) that is necessary to generate the excited state of oxyluciferin. The excited luciferin then emits a photon, returning to its ground state. The enzyme has a secondary acyl-CoA ligase activity when acting on L-firefly luciferin (see EC 6.2.1.52).

History

EC 1.13.12.7 created 1976, modified 1981, modified 1982, modified 2017

Orthology

K05914

photinus-luciferin 4-monooxygenase (ATP-hydrolysing)

Reference

1 [PMID:13315363]

Authors

GREEN AA, MCELROY WD

Title

Crystalline firefly luciferase.

Journal

Biochim Biophys Acta 20:170-6 (1956)
DOI:10.1016/0006-3002(56)90275-X

Reference

Authors

White EH, McCapra F, Field GF, McElroy WD.

Title

The structure and synthesis of firefly luciferin.

Journal

J Am Chem Soc 83:2402-2403 (1961)

Reference

3 [PMID:6064360]

Authors

Hopkins TA, Seliger HH, White EH, Cass MH.

Title

The chemiluminescence of firefly luciferin. A model for the bioluminescent reaction and identification of the product excited state.

Journal

J Am Chem Soc 89:7148-50 (1967)
DOI:10.1021/ja01002a076

Reference

4 [PMID:5784183]

Authors

White EH, Rapaport E, Hopkins TA, Seliger HH.

Title

Chemi- and bioluminescence of firefly luciferin.

Journal

J Am Chem Soc 91:2178-80 (1969)
DOI:10.1021/ja01036a093

Reference

5 [PMID:272645]

Authors

Koo JA, Schmidt SP, Schuster GB

Title

Bioluminescence of the firefly: key steps in the formation of the electronically excited state for model systems.

Journal

Proc Natl Acad Sci U S A 75:30-3 (1978)
DOI:10.1073/pnas.75.1.30

Reference

6 [PMID:3906652]

Authors

de Wet JR, Wood KV, Helinski DR, DeLuca M

Title

Cloning of firefly luciferase cDNA and the expression of active luciferase in Escherichia coli.

Journal

Proc Natl Acad Sci U S A 82:7870-3 (1985)
DOI:10.1073/pnas.82.23.7870

Reference

7 [PMID:15850783]

Authors

Nakamura M, Maki S, Amano Y, Ohkita Y, Niwa K, Hirano T, Ohmiya Y, Niwa H

Title

Firefly luciferase exhibits bimodal action depending on the luciferin chirality.

Journal

Biochem Biophys Res Commun 331:471-5 (2005)
DOI:10.1016/j.bbrc.2005.03.202

Reference

8 [PMID:22852753]

Authors

Sundlov JA, Fontaine DM, Southworth TL, Branchini BR, Gulick AM

Title

Crystal structure of firefly luciferase in a second catalytic conformation supports a domain alternation mechanism.

Journal

Biochemistry 51:6493-5 (2012)
DOI:10.1021/bi300934s

Other DBs

ExplorEnz - The Enzyme Database:

1.13.12.7

IUBMB Enzyme Nomenclature:

1.13.12.7

ExPASy - ENZYME nomenclature database:

1.13.12.7

BRENDA, the Enzyme Database:

1.13.12.7

CAS:	61970-00-1

DBGET integrated database retrieval system