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Literature summary extracted from

  • Pagala, V.R.; Park, J.; Reed, D.W.; Hartzell, P.L.
    Cellular localization of D-lactate dehydrogenase and NADH oxidase from Archaeoglobus fulgidus (2002), Archaea, 1, 95-104.
    View publication on PubMedView publication on EuropePMC

Localization

EC Number Localization Comment Organism GeneOntology No. Textmining
1.1.99.6 membrane more than 85% of the enzyme is associated with the membrane, integral membrane protein, a significant portion including part of the FAD-binding pocket, is outside the membrane facing the S-layer. NADH oxidase (NoxA2) co-localized to the same sites in the membrane (NoxA2) may protect proteins involved in electron transfer by reducing O2 to H2O2 or H2O Archaeoglobus fulgidus 16020
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Natural Substrates/ Products (Substrates)

EC Number Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
1.1.99.6 additional information Archaeoglobus fulgidus the enzyme is expressed constitutively ?
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 ?

Organism

EC Number Organism UniProt Comment Textmining
1.1.99.6 Archaeoglobus fulgidus O29853
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Source Tissue

EC Number Source Tissue Comment Organism Textmining
1.1.99.6 culture condition:anaerobic and sulfate-thiosulfate-lactate-grown cell
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 Archaeoglobus fulgidus
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1.1.99.6 culture condition:pyruvate-grown cell
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 Archaeoglobus fulgidus
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Substrates and Products (Substrate)

EC Number Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
1.1.99.6 additional information the enzyme is expressed constitutively Archaeoglobus fulgidus ?
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 ?

Cofactor

EC Number Cofactor Comment Organism Structure
1.1.99.6 FAD
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 Archaeoglobus fulgidus