Description
Experimental Technique/Method:X-RAY DIFFRACTION
Resolution:1.86
Classification:TRANSLATION
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
DOI:10.2210/pdb5t79/pdb
Abstract:
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
Resolution:1.86
Classification:TRANSLATION
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
DOI:10.2210/pdb5t79/pdb
Abstract:
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 available | 2017 |
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Publisher | RCSB-PDB |