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Literature summary for 1.2.1.105 extracted from

  • Baldi, N.; Dykstra, J.C.; Luttik, M.A.H.; Pabst, M.; Wu, L.; Benjamin, K.R.; Vente, A.; Pronk, J.T.; Mans, R.
    Functional expression of a bacterial alpha-ketoglutarate dehydrogenase in the cytosol of Saccharomyces cerevisiae (2019), Metab. Eng., 56, 190-197 .
    View publication on PubMed
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Application

Application Comment Organism
synthesis expression of the structural genes for all three subunits of the Escherichia coli 2-oxoglutarate dehydrogenase complex in Saccharomyces cerevisiae. The Escherichia coli lipoic-acid scavenging enzyme is coexpressed to enable cytosolic lipoylation of the complex, which is required for its enzymatic activity. In vivo cytosolic activity of the complex is tested byconstructing a reporter strain in which the essential metabolite 5-aminolevulinic acid can only be synthetized from cytosolic, and not mitochondrial, succinyl-CoA. In the resulting strain, complementation of 5-aminolevulinic acid auxotrophy depends on activation of the 2-oxoglutarate dehydrogenase complex by lipoic acid addition Escherichia coli

Organism

Organism UniProt Comment Textmining
Escherichia coli P0AFG3 and P0AFG6 and P0A9P0 i.e. SucA, component E1 of the 2-oxoglutarate dehydrogenase complex, cf. EC 1.2.4., P0AFG6 i.e. E2-component SucB, cf. EC 2.3.1.61, P0A9P0 i.e. E3-component Lpd, cf. 1.8.1.4
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