EzCatDB: M00009

DB codeM00009
CATH domainDomain 13.40.50.980
Domain 23.40.50.980Catalytic domain
Domain 32.30.38.10
Domain 43.30.300.30Catalytic domain
Domain 54.10.8.10
E.C.1.13.12.7
CSA1lci
MACiEM0128

CATH domainRelated DB codes (homologues)
2.30.38.10M00170,M00347
3.30.300.30M00170,M00347
3.40.50.980M00170,M00347

Enzyme Name
Swiss-protKEGG

P08659
Protein nameLuciferin 4-monooxygenasePhotinus-luciferin 4-monooxygenase (ATP-hydrolysing)
firefly luciferase
luciferase (firefly luciferin)
Photinus luciferin 4-monooxygenase (adenosinetriphosphate-hydrolyzing)
firefly luciferin luciferase
Photinus pyralis luciferase
SynonymsLuciferase
EC 1.13.12.7


Swiss-prot:Accession NumberP08659
Entry nameLUCI_PHOPY
ActivityPhotinus luciferin + O(2) + ATP = oxidized Photinus luciferin + CO(2) + AMP + diphosphate + light.
Subunit
Subcellular locationPeroxisome.
CofactorMagnesium.


CofactorsSubstratesProducts
KEGG-idC00305C02740C00007C00002C03797C00011C00020C00013C00205
CompoundMagnesiumPhotinus luciferinO2ATPOxidized Photinus luciferinCO2AMPPyrophosphatehn(light)
Typedivalent metal (Ca2+, Mg2+)amine group,aromatic ring (only carbon atom),carboxyl group,aromatic ring (with hetero atoms other than nitrogen atoms),sulfide groupothersamine group,nucleotideamine group,aromatic ring (only carbon atom),aromatic ring (with hetero atoms other than nitrogen atoms),sulfide groupothersamine group,nucleotidephosphate group/phosphate ionothers
1ba3A01UnboundUnboundUnboundUnboundUnboundUnboundUnboundUnboundUnbound
1lciA01UnboundUnboundUnboundUnboundUnboundUnboundUnboundUnboundUnbound
1ba3A02UnboundUnboundUnboundUnboundUnboundUnboundUnboundUnboundUnbound
1lciA02UnboundUnboundUnboundUnboundUnboundUnboundUnboundUnboundUnbound
1ba3A03UnboundUnboundUnboundUnboundUnboundUnboundUnboundUnboundUnbound
1lciA03UnboundUnboundUnboundUnboundUnboundUnboundUnboundUnboundUnbound
1ba3A04UnboundUnboundUnboundUnboundUnboundUnboundUnboundUnboundUnbound
1lciA04UnboundUnboundUnboundUnboundUnboundUnboundUnboundUnboundUnbound
1ba3A05UnboundUnboundUnboundUnboundUnboundUnboundUnboundUnboundUnbound
1lciA05UnboundUnboundUnboundUnboundUnboundUnboundUnboundUnboundUnbound

Active-site residues
resource
literature [4], [7], [11], [14]
pdbCatalytic residues
1ba3A01
1lciA01
1ba3A02ARG 218;HIS 245;THR 343
1lciA02ARG 218;HIS 245;THR 343
1ba3A03
1lciA03
1ba3A04LYS 529
1lciA04LYS 529
1ba3A05
1lciA05

References for Catalytic Mechanism
ReferencesSectionsNo. of steps in catalysis
[2]Fig.3, p.224-225
[3]p.292-295
[4]Fig.1, Fig.5, p.15316-15318
[7]Fig.1, Fig.5, p.132270-13228
[11]Fig.1, Fig.2, p.5439
[14]Fig.1, p.2416-2417
[16]Fig.3, Fig.7, p.1837-1838
[18]Fig.1, p.10434

references
[1]
PubMed ID8547353
JournalBiochim Biophys Acta
Year1996
Volume1292
Pages89-98
AuthorsWaud JP, Sala-Newby GB, Matthews SB, Campbell AK
TitleEngineering the C-terminus of firefly luciferase as an indicator of covalent modification of proteins.
[2]
PubMed ID8805542
JournalStructure
Year1996
Volume4
Pages223-8
AuthorsBaldwin TO
TitleFirefly luciferase: the structure is known, but the mystery remains.
[3]
CommentsX-RAY CRYSTALLOGRAPHY (2.0 ANGSTROMS)
Medline ID96398615
PubMed ID8805533
JournalStructure
Year1996
Volume4
Pages287-98
AuthorsConti E, Franks NP, Brick P
TitleCrystal structure of firefly luciferase throws light on a superfamily of adenylate-forming enzymes.
Related PDB1lci
Related Swiss-protP08659
[4]
PubMed ID9799491
JournalBiochemistry
Year1998
Volume37
Pages15311-9
AuthorsBranchini BR, Magyar RA, Murtiashaw MH, Anderson SM, Zimmer M
TitleSite-directed mutagenesis of histidine 245 in firefly luciferase: a proposed model of the active site.
[5]
CommentsX-RAY CRYSTALLOGRAPHY (2.2 ANGSTROMS)
Medline ID99007339
PubMed ID9788915
JournalBiophys J
Year1998
Volume75
Pages2205-11
AuthorsFranks NP, Jenkins A, Conti E, Lieb WR, Brick P
TitleStructural basis for the inhibition of firefly luciferase by a general anesthetic.
Related PDB1ba3
Related Swiss-protP08659
[6]
PubMed ID9825705
JournalPhotochem Photobiol
Year1998
Volume68
Pages749-53
AuthorsSung D, Kang H
TitleThe N-terminal amino acid sequences of the firefly luciferase are important for the stability of the enzyme.
[7]
PubMed ID10529195
JournalBiochemistry
Year1999
Volume38
Pages13223-30
AuthorsBranchini BR, Magyar RA, Murtiashaw MH, Anderson SM, Helgerson LC, Zimmer M
TitleSite-directed mutagenesis of firefly luciferase active site amino acids: a proposed model for bioluminescence color.
[8]
PubMed ID10498816
JournalBiochemistry (Mosc)
Year1999
Volume64
Pages962-7
AuthorsSandalova TP, Ugarova NN
TitleModel of the active site of firefly luciferase.
[9]
PubMed ID10404229
JournalNat Struct Biol
Year1999
Volume6
Pages697-705
AuthorsFrydman J, Erdjument-Bromage H, Tempst P, Hartl FU
TitleCo-translational domain folding as the structural basis for the rapid de novo folding of firefly luciferase.
[10]
PubMed ID10623630
JournalBiochem Biophys Res Commun
Year2000
Volume267
Pages394-7
AuthorsKumita JR, Jain L, Safroneeva E, Woolley GA
TitleA cysteine-free firefly luciferase retains luminescence activity.
[11]
PubMed ID10820015
JournalBiochemistry
Year2000
Volume39
Pages5433-40
AuthorsBranchini BR, Murtiashaw MH, Magyar RA, Anderson SM
TitleThe role of lysine 529, a conserved residue of the acyl-adenylate-forming enzyme superfamily, in firefly luciferase.
[12]
PubMed ID11225787
JournalFresenius J Anal Chem
Year2000
Volume366
Pages760-8
AuthorsLewis JC, Daunert S
TitlePhotoproteins as luminescent labels in binding assays.
[13]
PubMed ID11263966
JournalBiochem Biophys Res Commun
Year2001
Volume282
Pages28-33
AuthorsWang WQ, Xu Q, Shan YF, Xu GJ
TitleProbing local conformational changes during equilibrium unfolding of firefly luciferase: fluorescence and circular dichroism studies of single tryptophan mutants.
[14]
PubMed ID11327861
JournalBiochemistry
Year2001
Volume40
Pages2410-8
AuthorsBranchini BR, Magyar RA, Murtiashaw MH, Portier NC
TitleThe role of active site residue arginine 218 in firefly luciferase bioluminescence.
[15]
PubMed ID11180660
JournalLuminescence
Year2001
Volume16
Pages57-63
AuthorsEu J, Andrade J
TitleProperties of firefly luciferase immobilized through a biotin carboxyl carrier protein domain.
[18]
PubMed ID12530517
JournalCell Mol Life Sci
Year2002
Volume59
Pages1833-50
AuthorsViviani VR
TitleThe origin, diversity, and structure function relationships of insect luciferases.
[19]
PubMed ID12007636
JournalInt J Biochem Cell Biol
Year2002
Volume34
Pages983-91
AuthorsWang XC, Yang J, Huang W, He L, Yu JT, Lin QS, Li W, Zhou HM
TitleEffects of removal of the N-terminal amino acid residues on the activity and conformation of firefly luciferase.
[20]
PubMed ID12950169
JournalBiochemistry
Year2003
Volume42
Pages10429-36
AuthorsBranchini BR, Southworth TL, Murtiashaw MH, Boije H, Fleet SE
TitleA mutagenesis study of the putative luciferin binding site residues of firefly luciferase.

comments
This enzyme catalyzes three reactions (see [2]):
(1) Transfer of AMP to the carboxyl group of luciferin compound.
(2) Oxygenation of the compound, resulting in the release of AMP.
(3) Elimination of CO2, leading to formation of an additional double-bond.

createdupdated
2004-10-252009-02-26
Copyright: Nozomi Nagano, JST & CBRC-AIST
Funded by PRESTO/Japan Science and Technology Corporation (JST) (December 2001 - November 2004)
Funded by Grant-in-Aid for Publication of Scientific Research Results/Japan Society for the Promotion of Science (JSPS) (April 2005 - March 2006)
Funded by Grant-in-Aid for Scientific Research (B)/Japan Society for the Promotion of Science (JSPS) (April 2005 - March 2008)
Funded by BIRD/Japan Science and Technology Corporation (JST) (September 2005 - September 2010)
Funded by BIRD/Japan Science and Technology Corporation (JST) (October 2007 - September 2010)
Funded by Grant-in-Aid for Publication of Scientific Research Results/Japan Society for the Promotion of Science (JSPS) (April 2011 - March 2012)

© Computational Biology Research Center, AIST, 2004 All Rights Reserved.