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TitleBiocatalytic and structural properties of a highly engineered halohydrin dehalogenase.
Journal, issue, pagesChembiochem, Vol. 14, Page 870-881, Year 2013
Publish dateJan 28, 2013 (structure data deposition date)
AuthorsSchallmey, M. / Floor, R.J. / Hauer, B. / Breuer, M. / Jekel, P.A. / Wijma, H.J. / Dijkstra, B.W. / Janssen, D.B.
External linksChembiochem / PubMed:23585096
MethodsX-ray diffraction
Resolution2.1 - 2.49 Å
Structure data

PDB-4ixt:
Structure of a 37-fold mutant of halohydrin dehalogenase (HheC) bound to ethyl (R)-4-cyano-3-hydroxybutyrate
Method: X-RAY DIFFRACTION / Resolution: 2.49 Å

PDB-4ixw:
Halohydrin dehalogenase (HheC) bound to ethyl (2S)-oxiran-2-ylacetate
Method: X-RAY DIFFRACTION / Resolution: 2.47 Å

PDB-4iy1:
Structure of a 37-fold mutant of halohydrin dehalogenase (HheC) with chloride bound
Method: X-RAY DIFFRACTION / Resolution: 2.1 Å

Chemicals

ChemComp-1H1:
ethyl (3R)-4-cyano-3-hydroxybutanoate

ChemComp-CL:
Unknown entry

ChemComp-HOH:
WATER

ChemComp-IXW:
ethyl (2S)-oxiran-2-ylacetate

Source
  • rhizobium radiobacter (Agrobacterium genomosp. 4)
KeywordsLYASE / thermostability / synergistic mutations / coupled mutations / proline-induced / backbone changes / enantioselectivity changes / directed evolution / protein engineering / short-chain dehydrogenase/reductase enzyme superfamily / Cyanolysis / dehalogenase / Atorvastatin synthesis

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