5T79 : X-Ray Crystal Structure of a Novel Aldo-keto Reductases for the Biocatalytic Conversion of 3-hydroxybutanal to 1,3-butanediol

  • Joseph Brunzelle (Contributor)
  • Elena Evdokimova (Contributor)
  • Wayne F Anderson (Contributor)
  • Alexei Savchenko (Contributor)
  • Alexander F. Yakunin (Contributor)



Experimental Technique/Method:X-RAY DIFFRACTION
Release Date:2017-02-15
Deposition Date:2016-09-02
Revision Date:
Molecular Weight:38403.54
Macromolecule Type:Protein
Residue Count:332
Atom Site Count:2660

The nonnatural alcohol 1,3-butanediol (1,3-BDO) is a valuable building block for the synthesis of various polymers. One of the potential pathways for the biosynthesis of 1,3-BDO includes the biotransformation of acetaldehyde to 1,3-BDO via 3-hydroxybutanal (3-HB) using aldolases and aldo-keto reductases (AKRs). This pathway requires an AKR selective for 3-HB, but inactive toward acetaldehyde, so it can be used for one-pot synthesis. In this work, we screened more than 20 purified uncharacterized AKRs for 3-HB reduction and identified 10 enzymes with significant activity and nine proteins with detectable activity. PA1127 from
Date made available2017

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