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ENZYME entry: EC 18.104.22.168
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|a 3beta-hydroxy-4,4-dimethylsteroid + 2 H(+) + 3 NADH + 3 O2 <=> a 3beta-hydroxy-4alpha-methylsteroid-4beta-carboxylate + 4 H2O + 3 NAD(+)|
- Contains a Rieske [2Fe-2S] iron-sulfur cluster.
- This bacterial enzyme (SdmA) participates in the biosynthesis of
- Together with SdmB it forms an enzyme system that removes one methyl
group from the C-4 position of 4,4-dimethylated steroid molecules.
- SdmA catalyzes three successive oxidations of the C-4beta methyl
group, turning it into a carboxylate group; the second enzyme, SdmB,
is a bifunctional enzyme that catalyzes two different activities.
- As EC 22.214.171.1247 it catalyzes an oxidative decarboxylation that
results in reduction of the 3beta-hydroxy group at the C-3 carbon to
an oxo group.
- As EC 126.96.36.1990 it reduces the 3-oxo group back to a 3beta-hydroxyl.
- Unlike the animal/fungal enzyme EC 188.8.131.52 and the plant enzymes
EC 184.108.40.206 and EC 220.127.116.11, this enzyme acts preferentially on
the 4beta-methyl group.
- Since no epimerization of the remaining C-4alpha methyl group occurs,
the enzyme can only remove one methyl group, leaving a 4alpha-
|PRIAM enzyme-specific profiles||18.104.22.168|
|KEGG Ligand Database for Enzyme Nomenclature||22.214.171.124|
|IUBMB Enzyme Nomenclature||126.96.36.199|
|MEDLINE||Find literature relating to 188.8.131.52|
|Rhea expert-curated reactions||184.108.40.206|
entries corresponding to 1.14.13.-
All ENZYME / UniProtKB/Swiss-Prot entries corresponding to 1.14.-.-
All ENZYME / UniProtKB/Swiss-Prot entries corresponding to 1.-.-.-