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Information on EC 1.5.1.30 - flavin reductase (NADPH)
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1.5.1.30 flavin reductase (NADPH)IUBMB Comments
The enzyme reduces riboflavin, and, less efficiently, FMN and FAD. NADH is oxidized less efficiently than NADPH.
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Word Map
- 1.5.1.30
- monooxygenase
- mononucleotide
- harveyi
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flavin-dependent
- fmnh2
- fischeri
- dibenzothiophene
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desulfurization
- halogenases
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oxygen-insensitive
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nadh:flavin
- nitroreductases
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biodesulfurization
-
leiognathi
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fadh2-dependent
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single-enzyme
- 2-hydroxybiphenyl
The expected taxonomic range for this enzyme is: Bacteria, Eukaryota, Archaea
Synonyms
alkanesulfonate FMN reductase, ArsH, azoreductase, AZRü, Biliverdin-IX beta-reductase, CysJ, flavin oxidoreductase, flavin reductase, flavin reductase 1, flavin reductase Nr1, 
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topREACTION 
REACTION DIAGRAM
COMMENTARY 
ORGANISM
UNIPROT
LITERATURE
reduced riboflavin + NADP+ = riboflavin + NADPH + H+
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reduced riboflavin + NADP+ = riboflavin + NADPH + H+
ping-pong mechanism
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reduced riboflavin + NADP+ = riboflavin + NADPH + H+
bi-bi ternary mechanism, i.e. both FMN and NADPH must bind to the active site before catalysis can occur
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reduced riboflavin + NADP+ = riboflavin + NADPH + H+
binding of FMN by apoenzyme is noncooperative, exothermic and primarily enthalpy driven with significant conformational changes in enzyme upon binding. The kinetically deduced ping-pong mechanism is supported by measurement of binding affinities of the oxidized and reduced FMN cofoactors
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reduced riboflavin + NADP+ = riboflavin + NADPH + H+
FRP:luciferase coupled reaction can utilize reduced flavin by both free diffusion and direct transfer
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reduced riboflavin + NADP+ = riboflavin + NADPH + H+
single-enzyme kinetic assay, SsuE follows ordered sequential mechanism with NADPH as the first substrate to bind and NADP+ as the last product to leave. In presence of monooxygenase SsuD and octanesulfonate mechanism is altered to rapid equilibrium ordered mechanism, and Km-value for FMN increases 10fold
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reduced riboflavin + NADP+ = riboflavin + NADPH + H+
the nicotinamide of NAD+ stacks the isoalloxazine ring of FMN so that NADH can directly transfer hydride. The bound NADP+ also has a compact conformation but is bound in a reverse direction, which is not suitable for hydride transfer
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reduced riboflavin + NADP+ = riboflavin + NADPH + H+
the enzyme catalysis obeys the ping-pong Bi-Bi kinetic mechanism with substrate FMN as well as substrate nitrofurazone, but upon coupling with the bioluminescent reaction of luciferase, it changes to the sequential mechanism
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reduced riboflavin + NADP+ = riboflavin + NADPH + H+
the nicotinamide of NAD+ stacks the isoalloxazine ring of FMN so that NADH can directly transfer hydride. The bound NADP+ also has a compact conformation but is bound in a reverse direction, which is not suitable for hydride transfer
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reduced riboflavin + NADP+ = riboflavin + NADPH + H+
the enzyme catalysis obeys the ping-pong Bi-Bi kinetic mechanism with substrate FMN as well as substrate nitrofurazone, but upon coupling with the bioluminescent reaction of luciferase, it changes to the sequential mechanism
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