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Literature summary for 1.5.1.42 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)

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