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TitleEnzyme engineering enables inversion of substrate stereopreference of the halogenase WelO5*
Journal, issue, pagesChemcatchem, Year 2022
Publish dateJul 7, 2022 (structure data deposition date)
AuthorsVoss, M. / Huppi, S. / Schaub, D. / Hayashi, T. / Ligibel, M. / Sager, E. / Schroer, K. / Snajdrova, R. / Buller, R.M.U.
External linksChemcatchem / Search PubMed
MethodsX-ray diffraction
Resolution2.26 - 2.685 Å
Structure data

PDB-8acv:
WelO5* bound to Zn(II), Cl, and 2-oxoglutarate
Method: X-RAY DIFFRACTION / Resolution: 2.26 Å

PDB-8aut:
WelO5* L221A bound to Zn(II), Cl, 2-oxoglutarate, and 12-epi-hapalindole C
Method: X-RAY DIFFRACTION / Resolution: 2.685 Å

Chemicals

ChemComp-AKG:
2-OXOGLUTARIC ACID

ChemComp-CL:
Unknown entry

ChemComp-ZN:
Unknown entry

ChemComp-GOL:
GLYCEROL

ChemComp-ACT:
ACETATE ION

ChemComp-HOH:
WATER

ChemComp-OAU:
3-[(1~{S},2~{R},3~{S},6~{S})-3-ethenyl-2-isocyano-3-methyl-6-prop-1-en-2-yl-cyclohexyl]-1~{H}-indole

ChemComp-SO4:
SULFATE ION

Source
  • hapalosiphon welwitschii uh ic-52-3 (bacteria)
KeywordsOXIDOREDUCTASE / WelO5* 2-oxoglutarate-dependent halogenase / 12-epi-hapalindole C

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