1.14.14.3	metabolism	during the reaction, the first observed flavin C4a intermediate at pH below 8.5 is the protonated flavin C4a-hydroperoxide, which loses a proton to become an active flavin C4a-peroxide. Residue His44 plays an essential role in deprotonating the flavin C4a-hydroperoxide and initiating chemical catalysis. Residue His45 has a role in binding reduced FMN	764657	
1.14.14.3	metabolism	the enzyme controls the formation of the FMNH-C4a-OO- intermediate via the conserved His44 residue, the steps are: H+ reacts with O2 to generate +OOH. +OOH attacks C4a of FMNH- to generate FMNH-C4a-OOH. H+ is transferred from FMNH-C4a?OOH to His44 to generate FMNH-C4a-OO- while His44 stabilizes FMNH-C4a-OO- by forming a hydrogen bond to an oxygen atom	765135	
1.14.14.3	physiological function	bacterial luciferase requires an exogenous source of reduced flavin mononucleotide for bioluminescence activity. There is no stable complex formation between luciferase and oxidoreductases Fre/NfsA from Escherichia coli or Frp from Vibrio harveyi, which are believed to provide reduced flavin for luciferase activity. No difference in the levels of luciferase expression in either the DELTAfre or DELTANsfA strains	698992	
1.14.14.3	physiological function	expression in Staphylococcus aureus Xen29. In the absence of antibiotics, staphylococcal bioluminescence increases over time until a maximum after ca. 6 h of growth, and subsequently decreases to the detection threshold after 24 h of growth. Up to minimal inhibitory concentrations of the antibiotics vancomycin, ciprofloxacin, erythromycin or chloramphenicol, bioluminescence increases according to a similar pattern up to 6 h of growth, but after 24 h, bioluminescence is higher than in the absence of antibiotics. Antibiotic pressure impacts the relation between bioluminescence per organism and bioluminescence. Under antibiotic pressure, bioluminescence is not controlled by luxA expression but by cofactors impacting the bacterial metabolic activity	745081	
1.14.14.3	physiological function	isolated dimeric LuxF binds four molecules of the derivatized flavin, 6-(3'-(R)-myristyl)-FMN. LuxF binds myrFMN tightly with a dissociation constant of 80 nM	-, 744404	
1.14.14.3	physiological function	luciferase is the enzyme responsible for light emission in bioluminescent bacteria, it catalyzes the reaction of reduced flavin mononucleotide FMNH2, O2, and an aliphatic aldehyde to yield FMN, the corresponding carboxylic acid, and blue-green light	711486	
1.14.14.3	physiological function	the luxCDABE encoded protein products synergistically generate bioluminescent light signals exclusive of supplementary substrate additions or exogenous manipulations	713371	
1.14.14.3	physiological function	transient and stable transfection of human kidney, breast cancer, and colorectal cancer cell lines by a codon optimized lux expression cassette using viral 2A elements as linker regions. The expression product produces autobioluminescent phenotypes in all cell lines tested without the induction of cytotoxicity and allows for repeated interrogation of populations and self-directed control of bioluminescent activation with detection limits and EC50 values similar to traditional reporter systems	746267