and it’s essential for life to survive.
The researchers used a technique called ancestral sequence reconstruction to figure out what the enzyme’s genes might have looked like at different points in the last 3 billion years,
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. The scientists edited E,
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. coli’s genes to make the bacteria produce those probable ancient enzymes,
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, and then looked at how the reincarnated molecules held up under different temperatures.
“These very old enzymes were way more lousy at low temperatures than anyone expected,” says Kern. But over time, natural selection gradually pushed the enzymes to work better at cooler temperatures, she found. The enzymes accumulated mutations that swapped some of their amino acid building blocks,
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, ultimately lowering the enzymes’ energy demands. That let the enzymes keep moving essential reactions along at a fast-enough pace for life to survive.?
There wasn’t a corresponding disadvantage to also working well in heat,
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, so the enzymes didn’t immediately lose their heat tolerance. Some of them became what Kern calls “superenzymes” — they worked impressively fast and could catalyze reactions at low temperatures,
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, but they remained stable at high temperatures.
That finding goes against a widely held assumption that an increase in an enzyme’s activity — which would allow it to keep trucking at the same speed at lower temperatures — typically comes with a corresponding decrease in stability,
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.
That assumption was a logical one: Like chilly fingers struggling to tie shoelaces,
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, enzymes get stiffer and don’t work as well when the temperature

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