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Literature summary extracted from

  • Fukamichi, T.; Nishimoto, E.
    Conformational change near the redox center of dihydrolipoamide dehydrogenase induced by NAD+ to regulate the enzyme activity (2015), J. Fluoresc., 25, 577-583 .
    View publication on PubMed

Crystallization (Commentary)

EC Number Crystallization (Comment) Organism
1.8.1.4 X-ray diffraction structure determination and analysis Geobacillus stearothermophilus

Natural Substrates/ Products (Substrates)

EC Number Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
1.8.1.4 dihydrolipoamide + NAD+ Geobacillus stearothermophilus
-
 lipoamide + NADH + H+
-
 r

Organism

EC Number Organism UniProt Comment Textmining
1.8.1.4 Geobacillus stearothermophilus P11959 i.e. Geobacillus stearothermophilus
-

Substrates and Products (Substrate)

EC Number Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
1.8.1.4 dihydrolipoamide + NAD+
-
 Geobacillus stearothermophilus lipoamide + NADH + H+
-
 r
1.8.1.4 dihydrolipoamide + NAD+ dihydrolipoamide dehydrogenase (LipDH) transfers two electrons from dihydrolipoamide to NAD+ mediated by FAD Geobacillus stearothermophilus lipoamide + NADH + H+
-
 r

Subunits

EC Number Subunits Comment Organism
1.8.1.4 dimer
-
 Geobacillus stearothermophilus

Synonyms

EC Number Synonyms Comment Organism
1.8.1.4 dihydrolipoamide dehydrogenase
-
 Geobacillus stearothermophilus
1.8.1.4 LipDH
-
 Geobacillus stearothermophilus
1.8.1.4 pdhD
-
 Geobacillus stearothermophilus

Cofactor

EC Number Cofactor Comment Organism Structure
1.8.1.4 FAD a single FAD is non-covalently arranged in each subunit Geobacillus stearothermophilus
1.8.1.4 NAD+
-
 Geobacillus stearothermophilus
1.8.1.4 NADH
-
 Geobacillus stearothermophilus

General Information

EC Number General Information Comment Organism
1.8.1.4 additional information conformational change near the redox center of dihydrolipoamide dehydrogenase induced by NAD+ to regulate the enzyme activity Geobacillus stearothermophilus
1.8.1.4 physiological function dihydrolipoamide dehydrogenase (LipDH) transfers two electrons from dihydrolipoamide to NAD+ mediated by FAD. Since this reaction is the final step of a series of catalytic reaction of pyruvate dehydrogenase multi-enzyme complex (PDC), LipDH is a key enzyme to maintain the fluent metabolic flow Geobacillus stearothermophilus