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Literature summary extracted from

  • Klink, M.; Brzezinska, M.; Szulc, I.; Brzostek, A.; Kielbik, M.; Sulowska, Z.; Dziadek, J.
    Cholesterol oxidase is indispensable in the pathogenesis of Mycobacterium tuberculosis (2013), PLoS ONE, 8, e73333 .
    View publication on PubMedView publication on EuropePMC

Localization

EC Number Localization Comment Organism GeneOntology No. Textmining
1.1.3.6 extracellular
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 Mycobacterium tuberculosis
-
-

Natural Substrates/ Products (Substrates)

EC Number Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
1.1.3.6 cholesterol + O2 Mycobacterium tuberculosis
-
 cholest-4-en-3-one + H2O2
-
 ?

Organism

EC Number Organism UniProt Comment Textmining
1.1.3.6 Mycobacterium tuberculosis
-
-
-

Substrates and Products (Substrate)

EC Number Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
1.1.3.6 cholesterol + O2
-
 Mycobacterium tuberculosis cholest-4-en-3-one + H2O2
-
 ?

Synonyms

EC Number Synonyms Comment Organism
1.1.3.6 CHOD
-
 Mycobacterium tuberculosis

Cofactor

EC Number Cofactor Comment Organism Structure
1.1.3.6 FAD
-
 Mycobacterium tuberculosis

General Information

EC Number General Information Comment Organism
1.1.3.6 malfunction intracellular replication of an Mycobacterium tuberculosis mutant lacking a functional choD gene (DELTAchoD) is less efficient in macrophages than that of the wild-type strain. In contrast to wild-type tb, the DELTA strain inducesnitric oxide production in macrophages, an action that depends on the TLR2, but not the CR3, signaling pathway. Both wild-type and mutant strains inhibit the production of reactive oxygen species, but the DELTAchoD strain does so to a significantly lesser extent. Blocking TLR2-mediated signaling abolishes the inhibitory effect of wild-type Mycobacterium tuberculosis on reactive oxygen species production by macrophages. The mutant DELTAchoD strain, does not decrease phorbol myristate acetate-induced phosphorylation of extracellular signal-regulated kinases 1 and 2 (ERK1/2) ib contrast to the wild-type. The production of interleukin 10 by macrophages is significantly lower in DELTAchoD-infected macrophages than in wild-type Mtb-infected macrophages Mycobacterium tuberculosis
1.1.3.6 physiological function cholesterol oxidase ChoD is capable of modifying the bactericidal and pro-inflammatory activity of human macrophages. and is indispensable in the pathogenesis of Mycobacterium tuberculosis. The enzyme is enzyme capable of converting cholesterol to its 3-keto-4-ene derivative, cholestenone. The wild-type strain inhibits the production of reactive oxygen species. Wild-type Mycobacterium tuberculosis, but not the DELTAchoD strain, decreases phorbol myristate acetate-induced phosphorylation of extracellular signal-regulated kinases 1 and 2 (ERK1/2), which are involved in both TLR2-and CR3-mediated signaling pathways Mycobacterium tuberculosis