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Literature summary for 1.8.1.4 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)

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

Organism

Organism UniProt Comment Textmining
Bombyx mori Q8MUB0
-
-

Purification (Commentary)

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

Source Tissue

Source Tissue Comment Organism Textmining
larva
-
Bombyx mori
-

Specific Activity [micromol/min/mg]

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

Substrates and Products (Substrate)

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

Synonyms

Synonyms Comment Organism
dihydrolipoamide dehydrogenase
-
Bombyx mori
DLDH
-
Bombyx mori

Cofactor

Cofactor Comment Organism Structure
FAD
-
Bombyx mori
NAD+
-
Bombyx mori