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Literature summary extracted from

  • Tyagi, T.K.; Ponnan, P.; Singh, P.; Bansal, S.; Batra, A.; Collin, F.; Guillonneau, F.; Jore, D.; Patkar, S.A.; Saxena, R.K.; Parmar, V.S.; Rastogi, R.C.; Raj, H.G.
    Moonlighting protein in Starkeyomyces koorchalomoides: characterization of dihydrolipoamide dehydrogenase as a protein acetyltransferase utilizing acetoxycoumarin as the acetyl group donor (2009), Biochimie, 91, 868-875.
    View publication on PubMed

Cloned(Commentary)

EC Number Cloned (Comment) Organism
1.8.1.4 expressed in Escherichia coli Starkeyomyces koorchalomoides

KM Value [mM]

EC Number KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
1.8.1.4 3.63
-
 alpha-lipoamide in 0.1 mM Tris-HCl (pH 7.0), 0.0005 mM EDTA, 0.01 mM beta2-mercaptoethanol, at 37°C Starkeyomyces koorchalomoides

Localization

EC Number Localization Comment Organism GeneOntology No. Textmining
1.8.1.4 mitochondrion mitochondrial matrix Starkeyomyces koorchalomoides 5739
-

Molecular Weight [Da]

EC Number Molecular Weight [Da] Molecular Weight Maximum [Da] Comment Organism
1.8.1.4 50000
-
 SDS-PAGE Starkeyomyces koorchalomoides

Organism

EC Number Organism UniProt Comment Textmining
1.8.1.4 Starkeyomyces koorchalomoides
-
-
-
1.8.1.4 Starkeyomyces koorchalomoides FDUS 0337
-
-
-

Purification (Commentary)

EC Number Purification (Comment) Organism
1.8.1.4 ammonium sulfate precipitation and Ni-NTA agarose column chromatography Starkeyomyces koorchalomoides

Source Tissue

EC Number Source Tissue Comment Organism Textmining
1.8.1.4 mycelium
-
 Starkeyomyces koorchalomoides
-

Substrates and Products (Substrate)

EC Number Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
1.8.1.4 alpha-lipoamide + NADH
-
 Starkeyomyces koorchalomoides dihydrolipoamide + NAD+
-
 ?
1.8.1.4 alpha-lipoamide + NADH
-
 Starkeyomyces koorchalomoides FDUS 0337 dihydrolipoamide + NAD+
-
 ?

Synonyms

EC Number Synonyms Comment Organism
1.8.1.4 dihydrolipoamide dehydrogenase
-
 Starkeyomyces koorchalomoides
1.8.1.4 LADH LADH is an E3 component of pyruvate dehydrogenase complex with significant protein acetyltransferase activity Starkeyomyces koorchalomoides
1.8.1.4 TAase Starkeyomyces koorchalomoides transacetylase (TAase) is a dihydrolipoamide dehydrogenase and also exhibits diaphorase activity Starkeyomyces koorchalomoides

Cofactor

EC Number Cofactor Comment Organism Structure
1.8.1.4 FAD
-
 Starkeyomyces koorchalomoides
1.8.1.4 NADH
-
 Starkeyomyces koorchalomoides

General Information

EC Number General Information Comment Organism
1.8.1.4 physiological function the protein acetyltransferase activity of LADH can be attributed as a moonlighting function of the enzyme Starkeyomyces koorchalomoides