|Gene:||fadD19||Accession Number: G-14719 (MetaCyc)|
Species: Rhodococcus rhodochrous
An ATP-dependent steroid-CoA ligase (65 kDa) from Mycobacterium sp. strain NRRL B3805 was purified to near homogeneity and shown to be highly specific toward C26 carboxylic sterols [Chen85]. However, the gene encoding the enzyme has not been identified at the time.
Deletion of the fadD19 gene of Rhodococcus rhodochrous strain RG32 completely blocked side chain degradation of C-24 branched sterols. Heterologously expressed enzyme was also active toward steroid-C26-oic acid substrates, identifying FadD19 as a steroid-coenzyme A ligase with an essential in vivo role in the degradation of the side chains of C-24 branched-chain sterols [Wilbrink11].
Molecular Weight of Polypeptide: 60.602 kD (from nucleotide sequence)
Relationship Links: Entrez-Nucleotide:PART-OF:HM588719 , InterPro:IN-FAMILY:IPR000873 , InterPro:IN-FAMILY:IPR020845 , InterPro:IN-FAMILY:IPR025110 , Pfam:IN-FAMILY:PF00501 , Pfam:IN-FAMILY:PF13193 , Prosite:IN-FAMILY:PS00455
Enzymatic reaction of: 3-oxocholest-4-en-26-oate–CoA ligase
Synonyms: cholest-4-en-3-one-27-oate-CoA ligase
EC Number: 6.2.1.f
The reaction direction shown, that is, A + B ↔ C + D versus C + D ↔ A + B, is in accordance with the Enzyme Commission system.
The reaction is physiologically favored in the direction shown.
Wilbrink11: Wilbrink MH, Petrusma M, Dijkhuizen L, van der Geize R (2011). "FadD19 of Rhodococcus rhodochrous DSM43269, a steroid-coenzyme A ligase essential for degradation of C-24 branched sterol side chains." Appl Environ Microbiol 77(13);4455-64. PMID: 21602385
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