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Literature summary for 1.5.1.38 extracted from

  • Tanner, J.J.; Lei, B.; Tu, S.C.; Krause, K.L.
    Flavin reductase P: structure of a dimeric enzyme that reduces flavin (1996), Biochemistry, 35, 13531-13539.
    View publication on PubMed

Crystallization (Commentary)

Crystallization (Comment) Organism
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

Organism

Organism UniProt Comment Textmining
Vibrio harveyi Q56691
-
-

Reaction

Reaction Comment Organism Reaction ID
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

Synonyms

Synonyms Comment Organism
flavin reductase P
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Vibrio harveyi
NADPH:FMN oxidoreductase
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Vibrio harveyi

Cofactor

Cofactor Comment Organism Structure
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

General Information

General Information Comment Organism
physiological function NADPH:FMN oxidoreductase is involved in bioluminescence by providing reduced FMN to luciferase Vibrio harveyi