April 1, 2021

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This article was originally published as a chapter in the book “Design and Catastrophe: 51 Scientists Explore Evidence in Nature"

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Shortly after beginning my studies for a PhD in biochemistry at Columbia University, I came face to face with an unexpected, very difficult situation. In a laboratory session I was asked to kill a cute white laboratory rat, remove its liver, and study the synthesis of cholesterol. During my undergraduate work for a BS degree in chemistry I did not take any course in biology where animals were routinely dissected. I was devastated as I performed the gruesome task, and I could not see myself repeatedly killing animals in the future. Fortunately, there were laboratories in the biochemistry department that worked with microorganisms rather than animals. I joined one such laboratory and did my research for the degree on the bacterium Escherichia coli (E. coli).

I spent my subsequent 39 years in “E.-coli land,” happily digging into the mysteries of this fascinating organism.[1] Along the way I encountered numerous examples of the Creator’s unspeakable genius, such as the mystery of two enzymes: β-galactosidase in Escherichia coli and alcohol dehydrogenase in the human liver.

Undergirding all life processes are thousands of chemical changes. Enzymes, mostly proteins, are formidable and complex molecular machines, which promote and control every chemical change.

For my PhD thesis work, I studied how a unique variety of E. coli synthesized the enzyme β-galactosidase. E. coli cells manufacture more than 4,000 different types of proteins, but not all at the same time. Bacterial cells only make the proteins that are needed for growth at that time. The bacterium produces this enzyme when it encounters the milk sugar, lactose. Beta-galactosidase facilitates the rapid cleavage of this double sugar to glucose and galactose, and the bacterium gobbles up glucose for growth.

At the time of my studies, no one understood why E. coli cells produced β-galactosidase because, while the bacterium resides in the human colon, lactose never makes it that far during digestion.

More recently it was discovered that the double-sugar lactose is not the only substance that can evoke the synthesis of β-galactosidase in E. coli. A compound called β-galactosyl glycerol will do it just as well. And where do we find β-galactosyl glycerol, but in the indigestible content of vegetable matter of our diet, which actually travels all the way to the colon.

We learn from the Bible that the Creator designated fruits, nuts, and seed-bearing plants as food for humans. Thus He made provision for the lowly E. coli to live on the crumbs of our vegetarian diet.

But why was it so important for humans to have happy E. coli cells in their colons? Because most of the hundreds of species of microorganisms residing in our colons are “obligate anaerobes,” that is, they can live only in oxygen-free environments. Air is toxic for these microbes. The main task of E. coli cells in the colon is to preserve an oxygen-free environment. E. coli cells are excellent oxygen scavengers. Along with other colon bacteria, E. coli also makes vitamin K and biotin and protects the gut from pathogenic organisms.

Five genes on human chromosome #4, ADH1-ADH5, direct the manufacture of five versions of the liver enzyme, alcohol dehydrogenase. These enzymes convert ethyl alcohol to acetaldehyde, which then is utilized for energy. However, their presence in the liver is a conundrum because the human body does not produce ethyl alcohol. A professor in graduate school explained this curiosity to us students, but did not offer a solution. Many years later, while teaching bacterial physiology to graduate students, the solution finally occurred to me.

In the oxygen-free environment of the colon, E. coli exhibits a “mixed acid fermentation” type of metabolism where one of the secreted substances is ethyl alcohol. Alcohol finds its way into the bloodstream when it is absorbed in the colon along with water. Were it not for the mysterious alcohol dehydrogenase in our liver, all of us would walk around inebriated!

So the mystery of both enzymes is solved. The Creator, who placed E. coli and other microorganisms in the human colon for our benefit, inserted the requisite gene for this enzyme into human chromosome #4, keeping Adam and Eve and their offspring from being continually intoxicated!

The creationist’s understanding of the biosphere—that the welfare of each organism hinges on support from other living entities— is clearly illustrated here. This concept may serve us well when we are searching for solutions to other apparent conundrums in nature.

NOTES

[1] For selected publications stemming from this research, see GT Javor. Searching for the Creator through the study of a bacterium. Christ in the Class-room 1997; 19:129–139. Republished in https:// classicapologetics.com/ under “J” [accessed June 25, 2020]; GT Javor. A scientist celebrates creation. Ringold (GA): TEACH Services; 2012; GT Javor. Thiol-sensitive genes of Escherichia coli. Journal of Bacteriology 1989; 171:5607–5613; H Zhang, GT Javor. Identification of the ubiD gene on the Escherichia coli chromosome. Journal of Bacteriology 2000; 182:6243–6246; M Gulmezian, KR Hyman, BN Marbois, CF Clarke, GT Javor. The role of UbiX in Escherichia coli coenzyme Q biosynthesis. Archives of Biochemistry and Biophysics 2007; 467:144–153.

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George T. Javor is a professor emeritus of the Loma Linda University School of Medicine. After receiving a PhD in Biochemistry from Columbia University, he did postdoctoral work at Rockefeller University. In his scientific career he investigated the mysteries of heme and ubiquinone biosyntheses in Escherichia coli, publishing several important papers on these topics. He also wrote numerous articles in support of the biblical story of Creation, one of which, titled “Searching for the Creator through the Study of a Bacterium,” has been incorporated in the series Classic Works of Apologetics. He also published five books, the latest being The Best News Possible: You May Live Forever!