Catalytic and structural insights into a stereospecific and thermostable Class II aldolase HpaI from Acinetobacter baumannii
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An enzyme produced by bacteria shows promise for catalysing the synthesis of industrially important chemicals.
The rapidly growing field of biocatalysis uses naturally occurring compounds such as enzymes to speed up the synthesis of industrially important chemicals, including fine chemicals and drugs.
Enzymes known as aldolases are promising for this purpose since they can catalyze the formation and severing of carbon−carbon bonds. In particular, they attractive for making chiral compounds that are widely used in pharmaceuticals.
Now, a team led by researchers from Vidyasirimedhi Institute of Science and Technology (VISTEC) in Thailand has investigated the catalytic and biophysical properties of a class II metal aldolase from the pathogenic bacterium Acinetobacter baumannii.
They found that this aldolase exhibits a high thermal stability, a good solvent tolerance and a broad aldehyde substrate specificity, making it attractive for biocatalytic applications.
- Journal of Biological Chemistry 297, 101280 (2021). doi: 10.1016/j.jbc.2021.101280