EC Number   |
General Information |
Reference |
|---|
   1.5.1.42 | 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 |
-, 765526 |
| 1.5.1.42 | malfunction |
mutation of the critical residue Thr62, T62N and T62A, show a 5 and 7fold increase in catalytic rate, respectively |
764492 |
| 1.5.1.42 | metabolism |
the enzyme is involved in the degradation of (-)-camphor |
-, 746821 |
| 1.5.1.42 | more |
critical role of the residue in position 62 (threonine) of the DszD sequence in the enzymatic activity. This residue is located near the N5 atom of the isoalloxazine ring of FMN. Structure modelling of wild-type and mutants using quantum mechanics/molecular mechanics (QM/MM) method, and active site as well as substrate binding structure analysis, overview |
764492 |
| 1.5.1.42 | more |
the enzyme structure of DszD enzyme from Rhodococcus erythropolis strain IGTS8 complexed with both NADH and FMN is modeled using the crystal structure of the homologous enzyme 4-hydroxyphenylacetate hydroxylase component C of Sulfolobus tokodaii strain 7, HpaCst, PDB ID 2D37, with a resolution of 1.7 A |
-, 743144 |
| 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 |
-, 741888 |
| 1.5.1.42 | physiological function |
DszD from Rhodococcus erythropolis is a NADH-FMN oxidoreductase responsible for supplying FMNH2 to DszA and DszC in the biodesulfurization process of crude oil, the 4S pathway. The rate-limiting step of the reduction of FMN to FMNH2 is a process catalysed by DszD and known to play an important role in the reaction energy profile |
764492 |
| 1.5.1.42 | physiological function |
LuxG supplies reduced flavin mononucleotide (FMN) for bacterial luminescence by catalyzing the oxidation of nicotinamide adenine dinucleotide hydrogen (NADH) |
-, 765526 |
| 1.5.1.42 | physiological function |
NADH:FMN-oxidoreductase-luciferase is the coupled enzyme system of luminous bacteria used for bioluminescence |
741589 |
| 1.5.1.42 | physiological function |
Nocardioides sp. PD653 genes hcbA1, hcbA2, and hcbA3 encode enzymes that catalyze the oxidative dehalogenation of hexachlorobenzene (HCB), which is one of the most recalcitrant persistent organic pollutants (POPs). HcbA3 shows the highest affinity for FMN. HcbA3 may be the partner reductase component for HcbA1 in Nocardioides sp. PD653 |
765260 |
