(March 31, 2016 at 2:04 pm)LadyForCamus Wrote:(March 31, 2016 at 1:59 pm)AAA Wrote: I agree, let's not appeal to authority. Although some of the other people seem to want me to list scientists who support ID. Lets appeal to the evidence:
Glycolysis is thought to be the most primitive metabolic pathway in existence. Glycolysis (in most organisms, there are variations) requires 10 different enzymes to effectively catalyze the breakdown of glucose to pyruvate. All of them are necessary with the possible exception of triose phosphate isomerase. If you are missing one enzyme, the reaction no longer proceeds. Then you are unable to make pyruvate. How do you think these 10 (or 9) enzymes managed to gradually arise independently of one another when the absence of one prevents the formation of pyruvate. In addition to this, the cell needs to have pathways in place to further catabolize pyruvate to form high energy potential molecules. Which option is better from a scientific point of view: 1) All the enzymes formed at the same time (because they are all necessary to do the job), or 2) they gradually formed independent of each other in a way that allowed them to work together while the job that they had to complete was somehow accomplished by some other unknown/unobservable mechanism.
One of those options is highly speculative while the other is consistent with observations.
Okay, someone please correct me if I am wrong because I am not a scientist, but I am almost CERTAIN that glycolysis has been naturally reproduced in the lab. As in...it was by accident. No one was trying. It just emerged...naturally.
https://www.newscientist.com/article/dn2...out-cells/
So, yes. let's appeal to the evidence.
It was not by accident, they were definitely trying. Here's a link to the primary article:
http://msb.embopress.org/content/10/4/725
The tertiary article made it seem like it just happened without any direction. The experiment was well done, and they placed known metabolites or intermediates of both glycolysis and the pentose phosphate pathway into different test tubes containing concentrations of catalytic metal ions. They then incubated the molecules at 70 C, which is like 158 degrees F. They then analyzed the tubes and found that other intermediates of glycolysis were found. In other words, the molecules that were initially put into the tubes changed into other molecules. This is expected when a lot of energy is applied (70 C worth of thermal energy). At different temperatures different molecular strucutres are favored for molecules. I don't think that the tertiary article does it justice. In other words, it looks like molecules of glycolysis can convert between each other (except they found no 1,3-biphosphoglycerate, which is an intermediate) with sufficient energy. I still think it is speculative to say that organisms were able to take advantage of this until they evolved enzymes to do it themselves. What would be interesting is to look to see if there are organisms near hydrothermal vents that do not use glycolysis. That would support the idea that organisms could sustain themselves without glycolysis if they were in an environment similar to the experimental one.