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Literature summary extracted from

  • Tinikul, R.; Pitsawong, W.; Sucharitakul, J.; Nijvipakul, S.; Ballou, D.P.; Chaiyen, P.
    The transfer of reduced flavin mononucleotide from LuxG oxidoreductase to luciferase occurs via free diffusion (2013), Biochemistry, 52, 6834-6843 .
    View publication on PubMed

Cloned(Commentary)

EC Number Cloned (Comment) Organism
1.5.1.42 gene luxG encoding LuxG, the flavin reductase, is encoded in the same operon as its counterpart LuxAB Photobacterium leiognathi

KM Value [mM]

EC Number KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
1.5.1.42 additional information
-
 additional information the kinetics of binding of FMNH- to PlLuxAB and VcLuxAB and the subsequent reactions with oxygen are the same with either free FMNH- or FMNH- generated in situ by LuxG. No complexes between LuxG and the various species are necessary to transfer FMNH- to the acceptors. Single-mixing and double-mixing stopped-flow spectrophotometry. Anaerobic transient reaction kinetic analysis, overview Photobacterium leiognathi

Natural Substrates/ Products (Substrates)

EC Number Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
1.5.1.42 FMN + NADH + H+ Photobacterium leiognathi
-
 FMNH2 + NAD+
-
 ?
1.5.1.42 FMN + NADH + H+ Photobacterium leiognathi TH1
-
 FMNH2 + NAD+
-
 ?
1.5.1.42 additional information Photobacterium leiognathi a transfer of reduced flavin mononucleotide from enzyme LuxG oxidoreductase to luciferase occurs via free diffusion ?
-
 ?
1.5.1.42 additional information Photobacterium leiognathi TH1 a transfer of reduced flavin mononucleotide from enzyme LuxG oxidoreductase to luciferase occurs via free diffusion ?
-
 ?

Organism

EC Number Organism UniProt Comment Textmining
1.5.1.42 Photobacterium leiognathi P29237
-
-
1.5.1.42 Photobacterium leiognathi TH1 P29237
-
-

Substrates and Products (Substrate)

EC Number Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
1.5.1.42 FMN + NADH + H+
-
 Photobacterium leiognathi FMNH2 + NAD+
-
 ?
1.5.1.42 FMN + NADH + H+ FMN is obtained by conversion of FAD to FMN using snake venom from Crotalus adamanteus Photobacterium leiognathi FMNH2 + NAD+
-
 ?
1.5.1.42 FMN + NADH + H+
-
 Photobacterium leiognathi TH1 FMNH2 + NAD+
-
 ?
1.5.1.42 FMN + NADH + H+ FMN is obtained by conversion of FAD to FMN using snake venom from Crotalus adamanteus Photobacterium leiognathi TH1 FMNH2 + NAD+
-
 ?
1.5.1.42 additional information a transfer of reduced flavin mononucleotide from enzyme LuxG oxidoreductase to luciferase occurs via free diffusion Photobacterium leiognathi ?
-
 ?
1.5.1.42 additional information analysis of mode of transfer of FMNH- between enzyme LuxG from Photobacterium leiognathi TH1 and enzyme complexes LuxAB from both Photobacterium leiognathi TH1 and Vibrio campbellii, PlLuxAB and VcLuxAB, respectively, using single-mixing and double-mixing stopped-flow spectrophotometry. The oxygenase component of p-hydroxyphenylacetate hydroxylase (C2) from Acinetobacter baumannii, which has no structural similarity to LuxAB, is used to measure the kinetics of release of FMNH- from LuxG. With all FMNH- acceptors used (C2, PlLuxAB, and VcLuxAB), the kinetics of FMN reduction on LuxG are the same. The kinetics of the overall reactions and the individual rate constants correlate well with a free diffusion model for the transfer of FMNH- from LuxG to either LuxAB Photobacterium leiognathi ?
-
 ?
1.5.1.42 additional information a transfer of reduced flavin mononucleotide from enzyme LuxG oxidoreductase to luciferase occurs via free diffusion Photobacterium leiognathi TH1 ?
-
 ?
1.5.1.42 additional information analysis of mode of transfer of FMNH- between enzyme LuxG from Photobacterium leiognathi TH1 and enzyme complexes LuxAB from both Photobacterium leiognathi TH1 and Vibrio campbellii, PlLuxAB and VcLuxAB, respectively, using single-mixing and double-mixing stopped-flow spectrophotometry. The oxygenase component of p-hydroxyphenylacetate hydroxylase (C2) from Acinetobacter baumannii, which has no structural similarity to LuxAB, is used to measure the kinetics of release of FMNH- from LuxG. With all FMNH- acceptors used (C2, PlLuxAB, and VcLuxAB), the kinetics of FMN reduction on LuxG are the same. The kinetics of the overall reactions and the individual rate constants correlate well with a free diffusion model for the transfer of FMNH- from LuxG to either LuxAB Photobacterium leiognathi TH1 ?
-
 ?

Subunits

EC Number Subunits Comment Organism
1.5.1.42 homodimer
-
 Photobacterium leiognathi

Synonyms

EC Number Synonyms Comment Organism
1.5.1.42 LuxG
-
 Photobacterium leiognathi
1.5.1.42 LuxG oxidoreductase
-
 Photobacterium leiognathi
1.5.1.42 NADH:FMN oxidoreductase
-
 Photobacterium leiognathi

Temperature Optimum [°C]

EC Number Temperature Optimum [°C] Temperature Optimum Maximum [°C] Comment Organism
1.5.1.42 additional information
-
 stopped-flow kinetic experiments are performed at 4°C Photobacterium leiognathi

Turnover Number [1/s]

EC Number Turnover Number Minimum [1/s] Turnover Number Maximum [1/s] Substrate Comment Organism Structure
1.5.1.42 additional information
-
 additional information LuxG releases FMNH- with a rate constant of 4.5-6/s. The anaerobic reaction of LuxG with NADH involves half-sites reactivity, with the first flavin being reduced at a rate of 68/s and the second at a rate of 2.8/s Photobacterium leiognathi

pH Optimum

EC Number pH Optimum Minimum pH Optimum Maximum Comment Organism
1.5.1.42 7 8 assay at Photobacterium leiognathi

Cofactor

EC Number Cofactor Comment Organism Structure
1.5.1.42 NADH
-
 Photobacterium leiognathi

General Information

EC Number General Information Comment Organism
1.5.1.42 physiological function bacterial luciferase (LuxAB) is a two-component flavin mononucleotide (FMN)-dependent monooxygenase that catalyzes the oxidation of reduced FMN (FMNH-) and a long-chain aliphatic aldehyde by molecular oxygen to generate oxidized FMN, the corresponding aliphatic carboxylic acid, and concomitant emission of light. The LuxAB reaction requires a flavin reductase to generate FMNH- to serve as a luciferin in its reaction. FMNH- is unstable and can react with oxygen to generate H2O2. Enzyme LuxG, as a NADH:FMN oxidoreductase, supplies FMNH2 to luciferase in vivo. No complexes between LuxG and the various species are necessary to transfer FMNH- to the acceptors. Functional role of LuxG as an in vivo reductase in the luminous bacteria, overview Photobacterium leiognathi