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Structure paper

TitleUnlocking Asymmetric Michael Additions in an Archetypical Class I Aldolase by Directed Evolution.
Journal, issue, pagesAcs Catalysis, Vol. 11, Page 13236-13243, Year 2021
Publish dateJul 19, 2021 (structure data deposition date)
AuthorsKunzendorf, A. / Xu, G. / van der Velde, J.J.H. / Rozeboom, H.J. / Thunnissen, A.W.H. / Poelarends, G.J.
External linksAcs Catalysis / PubMed:34765282
MethodsX-ray diffraction
Resolution1.23 - 1.9 Å
Structure data

PDB-7p75:
Re-engineered 2-deoxy-D-ribose-5-phosphate aldolase catalysing asymmetric Michael addition reactions in substrate-free state
Method: X-RAY DIFFRACTION / Resolution: 1.23 Å

PDB-7p76:
Re-engineered 2-deoxy-D-ribose-5-phosphate aldolase catalysing asymmetric Michael addition reactions, Schiff base complex with cinnamaldehyde
Method: X-RAY DIFFRACTION / Resolution: 1.9 Å

Chemicals

ChemComp-HOH:
WATER

ChemComp-9Y6:
(2E)-3-phenylprop-2-enal

ChemComp-GOL:
GLYCEROL

Source
  • escherichia coli (strain atcc 8739 / dsm 1576 / nbrc 3972 / ncimb 8545 / wdcm 00012 / crooks) (bacteria)
  • escherichia coli 909945-2 (bacteria)
KeywordsLYASE / Protein engineering / directed evolution / DERA / aldolase / carboligase / Michael addition / carbon-carbon lyase / Schiff base / cinnamaldehyde

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