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Literature summary extracted from

  • Huo, J.; Shi, H.; Yao, Q.; Chen, H.; Wang, L.; Chen, K.
    Cloning and purification of recombinant silkworm dihydrolipoamide dehydrogenase expressed in Escherichia coli (2010), Protein Expr. Purif., 72, 95-100.
    View publication on PubMed

Cloned(Commentary)

EC Number Cloned (Comment) Organism
1.8.1.4 expressed in Escherichia coli BL21(DE3) cells Bombyx mori

Organism

EC Number Organism UniProt Comment Textmining
1.8.1.4 Bombyx mori Q8MUB0
-
-

Purification (Commentary)

EC Number Purification (Comment) Organism
1.8.1.4 Ni-NTA column chromatography Bombyx mori

Source Tissue

EC Number Source Tissue Comment Organism Textmining
1.8.1.4 larva
-
 Bombyx mori
-

Specific Activity [micromol/min/mg]

EC Number Specific Activity Minimum [µmol/min/mg] Specific Activity Maximum [µmol/min/mg] Comment Organism
1.8.1.4 0.344
-
 cell lysate, in 50 mM potassium phosphate buffer, pH 6.7, at 37°C Bombyx mori
1.8.1.4 6.65
-
 19.3fold purified enzyme, in 50 mM potassium phosphate buffer, pH 6.7, at 37°C Bombyx mori

Substrates and Products (Substrate)

EC Number Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
1.8.1.4 dihydrolipoamide + NAD+
-
 Bombyx mori lipoamide + NADH
-
 r
1.8.1.4 lipoamide + NADH
-
 Bombyx mori dihydrolipoamide + NAD+
-
 r

Synonyms

EC Number Synonyms Comment Organism
1.8.1.4 dihydrolipoamide dehydrogenase
-
 Bombyx mori
1.8.1.4 DLDH
-
 Bombyx mori

Cofactor

EC Number Cofactor Comment Organism Structure
1.8.1.4 FAD
-
 Bombyx mori
1.8.1.4 NAD+
-
 Bombyx mori