Structural highlights
6ok1 is a 4 chain structure with sequence from Thermomonospora curvata DSM 43183. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
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| Method: | X-ray diffraction, Resolution 1.7Å |
| Ligands: | , , , , |
| Resources: | FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT |
Function
LTP2_THECD Probably involved in bile acid degradation (Probable). In vitro, when associated with the ChsH1/ChsH2 hydratase, catalyzes the retroaldol cleavage of 17-hydroxy-3-oxo-4-pregnene-20-carboxyl-CoA (17-HOPC-CoA), forming androst-4-ene-3,17-dione and propionyl-CoA (PubMed:31209106). The in vivo substrate is probably a closely analogous bile acid degradation metabolite (Probable).[1] [2]
References
- ↑ Aggett R, Mallette E, Gilbert SE, Vachon MA, Schroeter KL, Kimber MS, Seah SYK. The steroid side chain-cleaving aldolase Ltp2-ChsH2DUF35 is a thiolase superfamily member with a radically repurposed active site. J Biol Chem. 2019 Jun 16. pii: RA119.008889. doi: 10.1074/jbc.RA119.008889. PMID:31209106 doi:http://dx.doi.org/10.1074/jbc.RA119.008889
- ↑ Aggett R, Mallette E, Gilbert SE, Vachon MA, Schroeter KL, Kimber MS, Seah SYK. The steroid side chain-cleaving aldolase Ltp2-ChsH2DUF35 is a thiolase superfamily member with a radically repurposed active site. J Biol Chem. 2019 Jun 16. pii: RA119.008889. doi: 10.1074/jbc.RA119.008889. PMID:31209106 doi:http://dx.doi.org/10.1074/jbc.RA119.008889