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BKMS-react is an integrated and non-redundant biochemical reaction database containing known enzyme-catalyzed and spontaneous reactions. Biochemical reactions collected from BRENDA, KEGG, MetaCyc and SABIO-RK were matched and integrated by aligning substrates and products.
 

:= BRENDA, := KEGG, := MetaCyc, := SABIO-RK
:= amino acid sequences := show the reaction diagram
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EC Number
Reaction
Pathways
Reaction IDs
Stoichiometry Check  
Commentary
dihydrolipoyl dehydrogenase
protein N6-(dihydrolipoyl)lysine + NAD+ = protein N6-(lipoyl)lysine + NADH + H+
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: a part step of glycine cleavage system (see R01221, R03425+R04125+R03815); Oxo-acid dehydrogenase complexes, dihydrolipoyl dehydrogenase; general reaction (see R03815 and R07618)
: A flavoprotein (FAD). A component of the multienzyme 2-oxo-acid dehydrogenase complexes. In the pyruvate dehydrogenase complex, it binds to the core of EC 2.3.1.12, dihydrolipoyllysine-residue acetyltransferase, and catalyses oxidation of its dihydrolipoyl groups. It plays a similar role in the oxoglutarate and 3-methyl-2-oxobutanoate dehydrogenase complexes. Another substrate is the dihydrolipoyl group in the H-protein of the glycine-cleavage system (click here for diagram), in which it acts, together with EC 1.4.4.2, glycine dehydrogenase (decarboxylating), and EC 2.1.2.10, aminomethyltransferase, to break down glycine. It can also use free dihydrolipoate, dihydrolipoamide or dihydrolipoyllysine as substrate. This enzyme was first shown to catalyse the oxidation of NADH by methylene blue; this activity was called diaphorase. The glycine cleavage system is composed of four components that only loosely associate: the P protein (EC 1.4.4.2), the T protein (EC 2.1.2.10), the L protein (EC 1.8.1.4) and the lipoyl-bearing H protein [15642479].