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Literature summary for 1.5.1.42 extracted from
- The transfer of reduced flavin mononucleotide from LuxG oxidoreductase to luciferase occurs via free diffusion (2013), Biochemistry, 52, 6834-6843 .
Cloned(Commentary)
| Cloned (Comment) | Organism |
|---|---|
| gene luxG encoding LuxG, the flavin reductase, is encoded in the same operon as its counterpart LuxAB | Photobacterium leiognathi |
KM Value [mM]
| KM Value [mM] | KM Value Maximum [mM] | Substrate | Comment | Organism | Structure |
|---|---|---|---|---|---|
| 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)
| Natural Substrates | Organism | Comment (Nat. Sub.) | Natural Products | Comment (Nat. Pro.) | Rev. | Reac. |
|---|---|---|---|---|---|---|
| FMN + NADH + H+ | Photobacterium leiognathi | - |
FMNH2 + NAD+ | - |
? |  |
| FMN + NADH + H+ | Photobacterium leiognathi TH1 | - |
FMNH2 + NAD+ | - |
? | |
| additional information | Photobacterium leiognathi | a transfer of reduced flavin mononucleotide from enzyme LuxG oxidoreductase to luciferase occurs via free diffusion | ? | - |
? | |
| additional information | Photobacterium leiognathi TH1 | a transfer of reduced flavin mononucleotide from enzyme LuxG oxidoreductase to luciferase occurs via free diffusion | ? | - |
? | |
Organism
| Organism | UniProt | Comment | Textmining |
|---|---|---|---|
| Photobacterium leiognathi | P29237 | - |
- |
| Photobacterium leiognathi TH1 | P29237 | - |
- |
Substrates and Products (Substrate)
| Substrates | Comment Substrates | Organism | Products | Comment (Products) | Rev. | Reac. |
|---|---|---|---|---|---|---|
| FMN + NADH + H+ | - |
Photobacterium leiognathi | FMNH2 + NAD+ | - |
? | |
| FMN + NADH + H+ | FMN is obtained by conversion of FAD to FMN using snake venom from Crotalus adamanteus | Photobacterium leiognathi | FMNH2 + NAD+ | - |
? | |
| FMN + NADH + H+ | - |
Photobacterium leiognathi TH1 | FMNH2 + NAD+ | - |
? | |
| FMN + NADH + H+ | FMN is obtained by conversion of FAD to FMN using snake venom from Crotalus adamanteus | Photobacterium leiognathi TH1 | FMNH2 + NAD+ | - |
? | |
| additional information | a transfer of reduced flavin mononucleotide from enzyme LuxG oxidoreductase to luciferase occurs via free diffusion | Photobacterium leiognathi | ? | - |
? | |
| 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 | ? | - |
? | |
| additional information | a transfer of reduced flavin mononucleotide from enzyme LuxG oxidoreductase to luciferase occurs via free diffusion | Photobacterium leiognathi TH1 | ? | - |
? | |
| 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
| Subunits | Comment | Organism |
|---|---|---|
| homodimer | - |
Photobacterium leiognathi |
Synonyms
| Synonyms | Comment | Organism |
|---|---|---|
| LuxG | - |
Photobacterium leiognathi |
| LuxG oxidoreductase | - |
Photobacterium leiognathi |
| NADH:FMN oxidoreductase | - |
Photobacterium leiognathi |
Temperature Optimum [°C]
| Temperature Optimum [°C] | Temperature Optimum Maximum [°C] | Comment | Organism |
|---|---|---|---|
| additional information | - |
stopped-flow kinetic experiments are performed at 4°C | Photobacterium leiognathi |
Turnover Number [1/s]
| Turnover Number Minimum [1/s] | Turnover Number Maximum [1/s] | Substrate | Comment | Organism | Structure |
|---|---|---|---|---|---|
| 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
| pH Optimum Minimum | pH Optimum Maximum | Comment | Organism |
|---|---|---|---|
| 7 | 8 | assay at | Photobacterium leiognathi |
Cofactor
| Cofactor | Comment | Organism | Structure |
|---|---|---|---|
| NADH | - |
Photobacterium leiognathi | |
General Information
| General Information | Comment | Organism |
|---|---|---|
| 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 |
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