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Literature summary for 2.3.1.190 extracted from

  • Lorenzl, H.; Oppermann, F.; Schmidt, B.; Steinbuchel, A.
    Purification and characterization of the E1 component of the Clostridium magnum acetoin dehydrogenase enzyme system (1993), Antonie van Leeuwenhoek, 64, 9-15.
    View publication on PubMed

Molecular Weight [Da]

Molecular Weight [Da] Molecular Weight Maximum [Da] Comment Organism
138000
-
gel filtration, component E1, i.e. acetoin:2,6-dichlorophenolindophenol oxidoreductase Clostridium magnum

Organism

Organism UniProt Comment Textmining
Clostridium magnum
-
-
-

Purification (Commentary)

Purification (Comment) Organism
component E1, i.e. acetoin:2,6-dichlorophenolindophenol oxidoreductase Clostridium magnum

Source Tissue

Source Tissue Comment Organism Textmining

Subunits

Subunits Comment Organism
More component E1, i.e. acetoin:2,6-dichlorophenolindophenol oxidoreductase, exhibits tetrameric alpha2beta2 structure, with alpha, 38500 and beta, 34000 Da, SDS-PAGE Clostridium magnum

Expression

Organism Comment Expression
Clostridium magnum formation of the enzyme components of the acetoin dehydrogenase enzyme system E1, i.e. acetoin:2,6-dichlorophenolindophenol oxidoreductase Ao:DCPIP OR,, E2, i.e. dihydrolipoamide acetyltransferase DHLTA, and E3, i.e. dihydrolipoamide dehydrogenase DHLDH, are induced during growth on acetoin up