Enzyme Origins Traced Via Evolutionary Time Travel to Know How They Evolved Over Time

Albert Einstein once wrote that: "The distinction between the past, present, and future is only a stubbornly persistent illusion." In a similar sense, time travel is a concept in protein evolution that shows the past and present versions of an enzyme existing in two different species today, which could open doors to designing future versions of the enzyme.

Researchers of the study, titled "Evolutionary Origins of Enzymatic Specificity and Dynamics," presented in the fall meeting of the American Chemical Society (ACS) 2021 how they used evolutionary time travel to trace the origins of an enzyme and learn how its evolution throughout the history, from being ancient organisms to modern-day humans.

SciTech Daily reported that the ACS Fall 2021 meeting is a virtual and in-person meeting conducted from August 22 to August 26 with on-demand content available for one month from August 30 to September 30. It is a meeting with more than 7,000 presentations that discusses various topics in the field of science.

Evolutionary Time Travel Reveals Ancient Forms of Enzymes

Study lead author Magnus Wolf-Watz, Ph.D. from Umeå University in Sweden, said that a person living in a certain area, like Rome, would like to learn the history of ancient Rome to better understand themselves and their culture.

Similarly, scientists want to conduct evolutionary time travel to a time when enzymes of today are at their ancient forms to understand their processes and how they can be improved to make new versions in the future.

Wolf-Watz and his team looked back around 2-3 billion years ago to the ancient organisms called archaea, a single-celled life form that still exists in the modern world. This organism has both the characteristics of a prokaryote and a eukaryote.

Its branch organism, known as Asgard archaea, was discovered six years ago in 2015; scientists have identified four more types of Asgard archaea, including Odin archaea found in the hydrothermal volcanoes in the Atlantic Ocean.

According to SciTech Daily, the team used X-ray crystallization and nuclear magnetic resonance spectroscopy to study two human types of Odin archaea's enzyme adenylate kinase (AK), the AK1 located in the cytoplasm and AK3 that resides in mitochondria.

This enabled the team to look at the structure of the AK enzyme and predict whether it will use adenosine triphosphate (ATP) or guanosine triphosphate (GTP). Then they examined a more ancient type of AK enzyme by purifying it and determining its structure to see how AK1 and AK3 evolved.

The team found a longer loop for discriminating ATP and GTP and has chemical groups that bind to either nucleotide substrates. That means it can use both ATP and GTP and use all naturally occurring nucleotide triphosphates (NTPs), but evolution has led it to become more specific for one of the nucleotide substrates.

ALSO READ: DNA Helix Torsional Stiffness Measured Through a Novel Technique to Understand How Cells Work

Designing Future Versions of the Enzyme

Wolf-Watz said they could identify a universal NTP binding motif that could be the building block for the future designs of newer versions of the enzyme, SciTech Daily reported.

Researchers noted that novel enzymes from the archaeal AK could someday be useful in organic synthesis or new drugs to treat diseases. They also hope to examine Odin archaea and learn more about it to see how they might have evolved millions of years ago.

The team believes there is more to discover about these ancient life forms after studying one enzyme, pointing out that it is like digging through a treasure chest.