| Description | L-Lactate dehydrogenase (L-LDH) Fcb2 from Saccharomyces cerevisiae and L-mandelate dehydrogenase (L-MDH) from Rhodotorula graminis are both flavocytochromes b2. L-LDH is a respiratory enzyme located in the intermembrane space of fungal mitochondria which catalyzes the oxidation of L-lactate to pyruvate. It is composed of 2 domains: a C-terminal flavin-binding domain, which includes the active site for lactate oxidation, and an N-terminal b2-cytochrome domain, required for efficient cytochrome c reduction. Despite their similarities these enzymes have distinct substrate specificities; L-LDH is unable to oxidize mandelate, whereas L-MDH is unable to oxidize lactate [ , ].Fcb2 is composed of 2 domains: a C-terminal FMN-binding domain, which includes the active site for lacate oxidation, and an N-terminal b2-cytochrome domain, required for efficient cytochrome c reduction. Fcb2 is a homotetramer and contains two noncovalently bound cofactors, FMN and heme per subunit. This entry represents the FMN-binding domain [ ]. | Name | L-mandelate/L-lactate dehydrogenase, FMN-binding domain |
| Short Name | L-MDH/L-LDH_FMN-bd | Type | Domain |
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