A team from Cape Town has recently printed the first high-res cryo-electron microscopy (EM) paper to stem from Africa. As described in Nature Communications Biology, the crew solved the structure of a nitrilases enzyme to an in the depth-to-atomic decision. They used the structural insights to design a mutant enzyme that could be fine-tuned in biotechnology. This task was made possible through an access program funded by the Synchrotron Strategies for African Analysis and Technology mission, a collaborative grant which seeks to create collaborations between world-leading scientists in Africa and the UK working together on analysis using synchrotron science.
Nitrilases are am an attractive class of plant enzymes that are vital players in the synthesis of a broad range of vital chemical compounds. These enzymes sometimes have specificity for a small variety of substrates, but they’ve large biotechnological potential. A crew of scientists from the University of Cape Town set out to understand this potential by investigating the structure of the enzymes utilizing cryo-EM at the electron Bio-imaging Centre (eBIC).
After efficiently managing to obtain high-res basic info, the group obtained a close-to-atomic resolution picture (3.4 Å) of a nitrilase derived from cabbage. Utilizing this structure, the group semi-rationally designed a brand new mutant nitrilase that acted on substrates not catalyzed by every other naturally occurring nitrilase.
The group hope that they will progress to making ‘designer’ nitrilases for any substrate required by industry—whether pharmaceuticals, fine chemical substances, or even meals. More work at the eBIC is intended to proceed with this fruitful research.
Nitrilases are a category of enzymes that are used to provide carboxylic acids and amides for the large-scale synthesis of medicines and industrially essential chemical compounds. The researchers group was fascinated by these enzymes and wanted to review how they evolved and correlate their structure and function.