AK6, an enzyme found in the nucleus of human cells, contains clear traces of single-celled organisms called Asgard archaea, according to new research led by Umeå University.
Asgard archaeon. Scale bar – 500 nm. Image credit: Imachi et al., doi: 10.1038/s41586-019-1916-6.
“The discovery adds a small piece of the puzzle to understanding how human cells have evolved from more primitive predecessors,” said Umeå University’s Professor Magnus Wolf-Watz, senior author of the study.
“The timing is interesting given that the Nobel Prize in Physiology or Medicine went to the great discovery that we humans have a lot of Neanderthal DNA in our genetic material.”
In the research, the authors focused on OdinAK, an enzyme isolated from a phylum of Asgard archaea called Odinarchaeota.
They compared the structural and functional properties of OdinAK with similar enzymes of both human and bacterial origin.
They found that the enzyme from Odinarchaeota has a unique and valuable feature in comparison with the human enzyme AK6.
While AK6 can only recognize and use one specific molecule when catalyzing a chemical reaction, OdinAK can use a wide range of molecules.
“In the study, we discovered the molecular mechanism for this broad spectrum,” said Umeå University’s Professor Elisabet Sauer-Eriksson, co-author of the study.
“The trick is that OdinAK uses the amino acid glutamine, which has unique chemical properties that are used to their full potential in the enzyme.”
“The general and broad recognition of different molecules takes place with a short loop sequence in the enzyme and this loop could be used as a Lego piece in the design of new enzymes.”
“The area of enzyme design aims to develop enzymes that can be used, for example, in green chemistry,” the researchers said.
“An example of this is the processing of wood raw materials, which is a strong research area at Umeå University.”
A paper on the findings was published in the journal Science Advances.
_____
Apoorv Verma et al. 2022. Insights into the evolution of enzymatic specificity and catalysis: From Asgard archaea to human adenylate kinases. Science Advances 8 (44); doi: 10.1126/sciadv.abm4089
Source link: https://www.sci.news/biology/odinarchaeota-enzyme-11368.html
