EC Number   |
General Information |
Reference |
|---|
   1.1.3.6 | drug target |
cholesterol oxidase can alter the structure of the cell membrane in pathogenic bacteria and is thus a potential antimicrobial drug target |
762731 |
| 1.1.3.6 | evolution |
CgChoA belongs to the non-covalent FAD-dependent enzymes belonging to the class I family |
-, 742195 |
| 1.1.3.6 | evolution |
the type I CO from Streptomyces sp. SA-COO is a member of the glucosemethanolcholine (GMC) oxidoreductase family and contains a single molecule of flavin adenine dinucleotide (FAD) noncovalently but tightly bound to the protein |
741512 |
| 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 |
743637 |
| 1.1.3.6 | malfunction |
the deletion mutant of choM1 completely lose the ability to form colonies on the cholesterol agar, the catabolism of sterols is greatly blocked, phenotype, overview |
725869 |
| 1.1.3.6 | malfunction |
the disruption of the choG gene does not alter the ability of strain CECT3014 cells to grow on cholesterol, but it abolishes the production of extracellular cholesterol oxidase |
-, 712958 |
| 1.1.3.6 | metabolism |
cholesterol oxidase ChoM1 is involved in the oxidation of sterols to sterones, a rate-limiting step in the catabolic pathway of sterols in Mycobacterium neoaurum. The bacterium exhibits definite preference for steroidal substrates possessing the 3-keto-4-ene moiety rather than the 3beta-ol-5-ene moiety |
725869 |
| 1.1.3.6 | metabolism |
cholesterol oxidase ChoM2 is involved in the oxidation of sterols to sterones, a rate-limiting step in the catabolic pathway of sterols in Mycobacterium neoaurum |
725869 |
| 1.1.3.6 | metabolism |
PimE is a key enzyme in the biosynthesis of the polyene macrolide pimaricin |
710959 |
| 1.1.3.6 | metabolism |
the enzyme catalyzes the first step in the biodegradation of cholesterol |
763254 |
