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Literature summary for 1.5.1.36 extracted from

  • De Silva, A.; Sehgal, R.; Kim, J.; Bellizzi, J.I.
    Steady-state kinetic analysis of halogenase-supporting flavin reductases BorF and AbeF reveals different kinetic mechanisms (2021), Arch. Biochem. Biophys., 704, 108874 .
    View publication on PubMed

Cloned(Commentary)

Cloned (Comment) Organism
gene abeF, recombinant overexpression in Escherichia coli uncultured bacterium AB1650
gene borF, recombinant overexpression in Escherichia coli uncultured bacterium AB1650

Protein Variants

Protein Variants Comment Organism
additional information site-directed mutagenesis of BorF implicates His160 and Arg38 as contributing to the catalytic activity and the pH dependence uncultured bacterium AB1650

Natural Substrates/ Products (Substrates)

Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
flavin + NADH + H+ uncultured bacterium AB1650
-
reduced flavin + NAD+
-
?

Organism

Organism UniProt Comment Textmining
uncultured bacterium AB1650
-
-
-
uncultured bacterium AB1650 F6LWA7
-
-

Purification (Commentary)

Purification (Comment) Organism
recombinant AbeF from Escherichia coli uncultured bacterium AB1650
recombinant BorF from Escherichia coli uncultured bacterium AB1650

Reaction

Reaction Comment Organism Reaction ID
reduced flavin + NAD+ = flavin + NADH + H+ AbeF follows a random-ordered sequence of substrate binding uncultured bacterium AB1650
reduced flavin + NAD+ = flavin + NADH + H+ BorF proceeds by a sequential ordered kinetic mechanism in which FAD binds first uncultured bacterium AB1650

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
FAD + NADH + H+ AbeF binds FAD with higher affinity than FADH2 uncultured bacterium AB1650 FADH2 + NAD+
-
?
FAD + NADH + H+ BorF binds FAD with higher affinity than FADH2 uncultured bacterium AB1650 FADH2 + NAD+
-
?
flavin + NADH + H+
-
uncultured bacterium AB1650 reduced flavin + NAD+
-
?
FMN + NADH + H+
-
uncultured bacterium AB1650 FMNH2 + NAD+
-
?
additional information AbeF can reduce FAD, FMN, and riboflavin in vitro and is selective for NADH over NADPH uncultured bacterium AB1650 ?
-
-
additional information AbeF can reduce FAD, FMN, and riboflavin in vitro and is selective for NADH over NADPH. BorF proceeds by a sequential ordered kinetic mechanism in which FAD binds first. NADH does not bind BorF in the absence of FAD uncultured bacterium AB1650 ?
-
-
riboflavin + NADH + H+
-
uncultured bacterium AB1650 reduced riboflavin + NAD+
-
?

Synonyms

Synonyms Comment Organism
AbeF
-
uncultured bacterium AB1650
BorF
-
uncultured bacterium AB1650

Cofactor

Cofactor Comment Organism Structure
additional information the enzyme is selectively for NADH over NADPH uncultured bacterium AB1650
NADH
-
uncultured bacterium AB1650

General Information

General Information Comment Organism
additional information His160 and Arg38 contribute to the catalytic activity and the pH dependence uncultured bacterium AB1650