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Literature summary for 1.5.1.42 extracted from

  • Xuan, G.; Xiao, Q.; Wang, J.; Lin, H.
    Cloning and expression of the flavin reductase LuxG from Photobacterium leiognathi YL and its improvement for NADH detection (2020), Photochem. Photobiol. Sci., 19, 274-280 .
    View publication on PubMed
Search for more literature for 1.5.1.42

Application

Application Comment Organism
analysis Photobacterium leiognathi Lux G might contribute to the development of a NADH detection kit Photobacterium leiognathi

Cloned(Commentary)

Cloned (Comment) Organism
gene luxG, phylogenetic analysis, cloning and recombinant overexpression of His-tagged enzyme in Escherichia coli strain BL21(DE3) Photobacterium leiognathi

Protein Variants

Protein Variants Comment Organism
additional information establishment of a coupled pure enzyme bioluminescent system and usage for NADH detection 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 YL
-
 FMNH2 + NAD+
-
 ?

Organism

Organism UniProt Comment Textmining
Photobacterium leiognathi P29237
-
-
Photobacterium leiognathi YL P29237
-
-

Purification (Commentary)

Purification (Comment) Organism
recombinant His-tagged enzyme from Escherichia coli strain BL21(DE3) by nickel affinity chromatography Photobacterium leiognathi

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
FMN + NADH + H+
-
 Photobacterium leiognathi FMNH2 + NAD+
-
 ?
FMN + NADH + H+
-
 Photobacterium leiognathi YL FMNH2 + NAD+
-
 ?
additional information establishment of a coupled pure enzyme bioluminescent system and usage for quantitative detection, method evaluation Photobacterium leiognathi ?
-
-
additional information establishment of a coupled pure enzyme bioluminescent system and usage for quantitative detection, method evaluation Photobacterium leiognathi YL ?
-
-

Subunits

Subunits Comment Organism
? x * 26000, recombinant His-tagged enzyme, SDS-PAGE Photobacterium leiognathi

Synonyms

Synonyms Comment Organism
flavin reductase
-
 Photobacterium leiognathi
LuxG
-
 Photobacterium leiognathi
NADH:flavin oxidoreductase
-
 Photobacterium leiognathi

Temperature Optimum [°C]

Temperature Optimum [°C] Temperature Optimum Maximum [°C] Comment Organism
40
-
 recombinant His-tagged enzyme Photobacterium leiognathi

pH Optimum

pH Optimum Minimum pH Optimum Maximum Comment Organism
8
-
 recombinant His-tagged enzyme Photobacterium leiognathi

Cofactor

Cofactor Comment Organism Structure
NADH
-
 Photobacterium leiognathi

pI Value

Organism Comment pI Value Maximum pI Value
Photobacterium leiognathi recombinant His-tagged enzyme, isoelectric focusing
-
 6

General Information

General Information Comment Organism
evolution phylogenetic analysis demonstrats that Photobacterium leiognathi strain YL LuxG has a rather distant evolutionary relationship with Frase I of Aliivibrio fischeri and Frp of Vibrio harveyi, but a close evolutionary relationship with Fre from Escherichia coli, which are all enzymes related to oxidoreductases. Changes in the functionally conserved sites contribute to the functional divergence of LuxG and Fre. Bioinformatics analysis of LuxG sequences in bacteria, overview. Structure comparisons Photobacterium leiognathi
physiological function LuxG supplies reduced flavin mononucleotide (FMN) for bacterial luminescence by catalyzing the oxidation of nicotinamide adenine dinucleotide hydrogen (NADH) Photobacterium leiognathi