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22:28exactly the same. >> Yes. >> Except for a hydroxal group, an O. >> Yeah. >> Okay. The phenol alanine just has an O attached. And that O is the entire difference. >> That's so funny. such a minuscule. >> It's a tiny Yeah. All it is is one of the carbons is attached to an O. Otherwise, the entire amino acid is exactly the same. But that one sight difference in the active site is what causes this entire change >> downstream. It's what basically changes the down all of the downstream >> all of the downstream. Because if you don't have the O effectively what that means is if you don't have the O the cadaavverine comes in or you make the
23:08cadaavverine and then the O if you have the O the it it stops another hydrogen from coming in >> and sort of freeing this guy. >> Got it. Got it. >> Okay. Before there was nothing to stop another H+ ion from coming in and just like freeing this. This thing goes away and then you know some other enzyme hooks up with it. here because I've got the O, I'm not messing with this cadaavverine. The cadaavverine stays inside my enzyme for longer and then the process of oxidation can actually happen within the same spot. >> That makes sense. It it's sort of like this because of its presence, it dictates whether it will stay or whether it will go. >> Yeah. For like the time that it stays inside the enzyme is determined by
23:50whether that oxygen and hydrogen are there or not. >> Okay. What's again very cool about this particular enzyme is also it is very promiscuous. It's not loyal to lysine or ornithine. It does lysine or ornithine arginine. So it's incredibly versatile if we want to use it for industrial purposes. This goes back to the idea we keep coming up with with some of these things where is is it a single point discovery or is it in my analogy of it more of a platform that has multiple use case uh possibilities because it's a fundamental unlock that has more than a single a singular point solution. >> Exactly. Yeah. So it's it's very cool in
24:31that way right because it's it's very versatile. It can it can use all sorts of amino acids to create these compounds of many different types. >> Mhm. >> Okay. It's like a little mini factory. >> Yeah. Yeah. Yeah. It's very cool. And it's it's doing both processes at once, you know. It's like a single machine that end to end. >> Yes. >> Which is it like an efficiency play, less like likelihood for issues, transitioning from a step one to a step two, all these kind of things. >> All these Yeah. And and you're already getting to sort of what I'm going to talk about at the end, which is the applications. But before we do that, the last bit that they that they studied was the evolution of this particular enzyme. Okay. How did plants figure out how to make this? >> Yeah.
25:11>> Okay. Yeah, >> you would think that the plants, you know, usually you naively think the plants have some precursor protein >> and then that precursor protein gets mutated in some way and then I have this new use case. This particular enzyme is actually more related to bacterial enzymes, not plants. >> Interesting. >> Okay, that's kind of weird because bacteria are not plants, >> right? Unless we remember that the chloroplasts that are inside bacteria were once I mean sorry the chloroplasts that were in that are inside plants now were once cyanobacteria they were once bacteria that through endo symbiosis became inter integrated inside the plant
25:54cell and they've just stuck around for like a billion years because they've had a good the plant cell has had a good the plant cell gets glucose and ATP so energy and food out of the cyanobacteria. The cyanobacteria is in a nice like all-inclusive resort. It doesn't have to worry about like trying to get food for itself because the plant is just supplying it as long as it does the work, right? So, this particular enzyme is more related to the decarboxilaces in bacteria than it is to plants. And if we look through the evolution, there's independent lineages >> that all of these different plants have because remember, we've got different plants, right? We've got Rosids, um,
26:35Nicotiana, um Armishia. All of these are different plants that are finding ways to make this happen. >> They've independently found this bacteria >> enzyme and they've repurposed it. So, it's not like one guy did it and then he let everyone know. All of these different lineages >> did it at different times, but they found the same use case. >> That's so fascinating, >> which is pretty interesting. There's it's almost like a fundamental >> uh thing that's like each of these lineages were like this is the most