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EC Number Substrates Commentary Substrates Organism Products Commentary (Products) Reversibility
Display the word mapDisplay the reaction diagram Show all sequences 1.5.1.37FAD + NADH + H+ involved in pyrrolnitrin biosynthesis. PrnF is the flavin:NADH reductase component of the two-component arylamine oxygenase system in Pseudomonas fluorescens Pf-5. PrnF reduces FAD to FADH2, which is then directly transferred to PrnD, where it is used by PrnD to catalyze the oxygenation of aminopyrrolnitrin. The PrnD oxygenase component requires a direct interaction with the PrnF reductase component to oxygenate arylamine Pseudomonas protegens Pf-5 FADH2 + NAD+ - ?
Display the word mapDisplay the reaction diagram Show all sequences 1.5.1.37FAD + NADH + H+ no activity with NADPH. PrnF reduces FAD to FADH2, which is then directly transferred to aminopyrrolnitrin oxygenase (PrnD), where it is used by PrnD to catalyze the oxygenation of aminopyrrolnitrin. The PrnD oxygenase component requires a direct interaction with the PrnF reductase component to oxygenate arylamine. Other flavin reductases present in the host cell would not supplant the role of PrnF. The turnover rate of PrnD in the presence of PrnF is almost two times higher than that in the presence of the Escherichia coli flavin SsuE reductase (EC 1.5.1.29) Pseudomonas protegens Pf-5 FADH2 + NAD+ - ?
Display the word mapDisplay the reaction diagram Show all sequences 1.5.1.37FAD + NADH + H+ the reductase catalyzes the reduction of FAD by NADH and releases the FADH- product into solution, but unlike the reductase from Actinetobacter baumannii, this catalysis is not influenced by p-hydroxyphenylacetate Pseudomonas aeruginosa FADH2 + NAD+ - ?
Display the word mapDisplay the reaction diagram Show all sequences 1.5.1.37FAD + NADH + H+ FAD is a better substrate than FMN. The enzyme does not use NADPH or riboflavin as substrate Paraburkholderia phenoliruptrix FADH2 + NAD+ - ?
Display the word mapDisplay the reaction diagram Show all sequences 1.5.1.37FAD + NADH + H+ the enzyme can adequately supply reduced flavin under saturating substrate conditions to support catalysis of flavin-dependent halogenase SgcC3 and monooxygenase SgcC during biosynthesis of C-1027 Streptomyces globisporus FADH2 + NAD+ - ?
Display the word mapDisplay the reaction diagram Show all sequences 1.5.1.37FAD + NADH + H+ strictly NADH- and FAD-specific enzyme: No activity with NADPH or FMN Streptomyces globisporus FADH2 + NAD+ - ?
Display the word mapDisplay the reaction diagram Show all sequences 1.5.1.37FAD + NADH + H+ FMN and FAD are both substrates for the reductase. FMN is the favored substrate with a 2fold-higher rate constant and affinity that is about 5 times higher compared to that of FAD. With regard to electron donors, only NADH is effective whereas NADPH at a similar concentration acts as a very poor cosubstrate Pseudomonas putida FADH2 + NAD+ - ?
Display the word mapDisplay the reaction diagram Show all sequences 1.5.1.37FAD + NADH + H+ FMN and FAD are both substrates for the reductase. FMN is the favored substrate with a 2fold-higher rate constant and affinity that is about 5 times higher compared to that of FAD. With regard to electron donors, only NADH is effective whereas NADPH at a similar concentration acts as a very poor cosubstrate Pseudomonas putida ATCC 17453 FADH2 + NAD+ - ?
Display the word mapDisplay the reaction diagram Show all sequences 1.5.1.37FADH2 + NAD+ - Parageobacillus thermoglucosidasius FAD + NADH + H+ - r
Display the word mapDisplay the reaction diagram Show all sequences 1.5.1.37FADH2 + NAD+ - Parageobacillus thermoglucosidasius NCIMB 11955 FAD + NADH + H+ - r
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