EC Number | Cloned (Comment) | Organism |
---|---|---|
1.5.1.30 | expressed in Escherichia coli | Vibrio harveyi |
EC Number | Crystallization (Comment) | Organism |
---|---|---|
1.5.1.38 | the 1.8 A crystal structure of flavin reductase P from Vibrio harVeyi is solved by multiple isomorphous replacement and reveals that the enzyme is a unique dimer of interlocking subunits, with 9352 A(2) of surface area buried in the dimer interface. Each subunit comprises two domains | Vibrio harveyi |
EC Number | Organism | UniProt | Comment | Textmining |
---|---|---|---|---|
1.5.1.30 | Vibrio harveyi | - |
- |
- |
1.5.1.38 | Vibrio harveyi | Q56691 | - |
- |
EC Number | Reaction | Comment | Organism | Reaction ID |
---|---|---|---|---|
1.5.1.38 | FMNH2 + NADP+ = FMN + NADPH + H+ | the first step in catalysis, which is hydride transfer from C4 of NADPH to cofactor FMN, involves addition to the re face of the FMN, probably at the N5 position. The limited accessibility of the FMN binding pocket and the extensive FMN-protein hydrogen bond network are consistent with the observed ping-pong bisubstrate-biproduct reaction kinetics | Vibrio harveyi |
EC Number | Subunits | Comment | Organism |
---|---|---|---|
1.5.1.30 | homodimer | FMN binding pocket, crystallization, X-ray | Vibrio harveyi |
EC Number | Synonyms | Comment | Organism |
---|---|---|---|
1.5.1.30 | flavin reductase P | - |
Vibrio harveyi |
1.5.1.30 | NADPH:FMN oxidoreductase | - |
Vibrio harveyi |
1.5.1.38 | flavin reductase P | - |
Vibrio harveyi |
1.5.1.38 | NADPH:FMN oxidoreductase | - |
Vibrio harveyi |
EC Number | Cofactor | Comment | Organism | Structure |
---|---|---|---|---|
1.5.1.30 | FMN | - |
Vibrio harveyi | |
1.5.1.38 | FMN | the enzyme is specific for FMN as cofactor. FMN is recognized and tightly bound by a network of 16 hydrogen bonds, while steric considerations prevent the binding of FAD. A flexible loop containing a Lys and an Arg could account for the NADPH specificity | Vibrio harveyi |
EC Number | General Information | Comment | Organism |
---|---|---|---|
1.5.1.38 | physiological function | NADPH:FMN oxidoreductase is involved in bioluminescence by providing reduced FMN to luciferase | Vibrio harveyi |