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Literature summary extracted from

  • Schwinde, J.W.; Hertz, P.F.; Sahm, H.; Eikmanns, B.J.; Guyonvarch, A.
    Lipoamide dehydrogenase from Corynebacterium glutamicum: molecular and physiological analysis of the lpd gene and characterization of the enzyme (2001), Microbiology, 147, 2223-2231.
    View publication on PubMed

Cloned(Commentary)

EC Number Cloned (Comment) Organism
1.8.1.4 expression in Escherichia coli or in Corynebacterium glutamicum, the cloned gene is expressed in Corynebacterium glutamicum cells harbouring the gene on a plasmid shows 12fold higher specific LPD activity when compared to the wild-type strain Corynebacterium glutamicum

General Stability

EC Number General Stability Organism
1.8.1.4 no loss of activity when the enzyme is frozen at -20°C, and thawed three times Corynebacterium glutamicum

Natural Substrates/ Products (Substrates)

EC Number Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
1.8.1.4 additional information Corynebacterium glutamicum the enzyme is an essential component of the pyruvate dehydrogenase and 2-oxoglutarate dehydrogenase complexes ?
-
 ?
1.8.1.4 additional information Corynebacterium glutamicum DSM 20300 the enzyme is an essential component of the pyruvate dehydrogenase and 2-oxoglutarate dehydrogenase complexes ?
-
 ?

Organism

EC Number Organism UniProt Comment Textmining
1.8.1.4 Corynebacterium glutamicum Q8NTE1
-
-
1.8.1.4 Corynebacterium glutamicum DSM 20300 Q8NTE1
-
-

Purification (Commentary)

EC Number Purification (Comment) Organism
1.8.1.4
-
 Corynebacterium glutamicum

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 3.651
-
-
 Corynebacterium glutamicum

Storage Stability

EC Number Storage Stability Organism
1.8.1.4 4°C or -20°C, stable for at least 1 month Corynebacterium glutamicum

Substrates and Products (Substrate)

EC Number Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
1.8.1.4 2-(p-iodophenyl)-3-p-nitrophenyl-5-phenyltetrazolium chloride + NADH
-
 Corynebacterium glutamicum ? + NAD+
-
 ?
1.8.1.4 2-(p-iodophenyl)-3-p-nitrophenyl-5-phenyltetrazolium chloride + NADH
-
 Corynebacterium glutamicum DSM 20300 ? + NAD+
-
 ?
1.8.1.4 dihydrolipoamide + NAD+
-
 Corynebacterium glutamicum lipoamide + NADH
-
 ?
1.8.1.4 dihydrolipoamide + NAD+
-
 Corynebacterium glutamicum DSM 20300 lipoamide + NADH
-
 ?
1.8.1.4 additional information the enzyme is an essential component of the pyruvate dehydrogenase and 2-oxoglutarate dehydrogenase complexes Corynebacterium glutamicum ?
-
 ?
1.8.1.4 additional information the enzyme is an essential component of the pyruvate dehydrogenase and 2-oxoglutarate dehydrogenase complexes Corynebacterium glutamicum DSM 20300 ?
-
 ?
1.8.1.4 oxidized 2,6-dichlorophenolindophenol + NADH
-
 Corynebacterium glutamicum ? + NAD+
-
 ?
1.8.1.4 oxidized 2,6-dichlorophenolindophenol + NADH
-
 Corynebacterium glutamicum DSM 20300 ? + NAD+
-
 ?

Temperature Optimum [°C]

EC Number Temperature Optimum [°C] Temperature Optimum Maximum [°C] Comment Organism
1.8.1.4 50
-
-
 Corynebacterium glutamicum

pH Optimum

EC Number pH Optimum Minimum pH Optimum Maximum Comment Organism
1.8.1.4 7 7.5 50 mM phosphate buffer Corynebacterium glutamicum

Cofactor

EC Number Cofactor Comment Organism Structure
1.8.1.4 NAD+
-
 Corynebacterium glutamicum
1.8.1.4 NADH
-
 Corynebacterium glutamicum