Re: Detoxifying acetaldahyde

Enzymes are folded protein conglomerations that facilitate the production of certain molecules required by the body from raw materials that are already present. They are three-dimensional structures that attract and hold the raw material molecules just long enough in just the right orientation for the new product to form. Size, shape, charge, and fluid dynamic motion may all play a role in bringing the reagents together under ideal conditions so that the product can emerge. Enzymes are fast workers, capable of catalyzing several million reactions per second.

An enzyme inhibitor is a substance that prevents a particular enzyme or class of enzymes from performing their specific tasks with the effect that the concentration of desired product is substantially reduced or eliminated even when the raw materials for the enzyme are available. Some enzyme inhibitors work by binding irreversibly into the enzyme reaction pocket, thus preventing the raw materials from assuming their required positions for the reaction to occur.

Some essential molecular configurations required in the body are so complex that several intermediate steps, each with a different enzyme, are necessary before the desired product is formed. Inhibition of any one of the enzymes in the pathway can prevent the formation of the end-product.

Acetaldehyde is such a small electrophilic molecule that it can easily migrate into enzyme reaction pockets and remain there, thus rendering the enzyme, attacked in this way, useless. The product concentration of the enzymes inhibited in this manner may drop so low that deficiency symptoms start to manifest even when adequate reserves of the raw materials are available. Acetaldehyde will preferentially disable enzymes that are keyed to working with structures that are similar to its own shape and atomic configuration or that provide an attractive binding site for its electrophilic carbon, such as an exposed sulfur atom or amine group.

As examples, consider just two of a host of enzymes in metabolic pathways that may be subject to acetaldehyde interference.

CHOLINE ACETYL TRANSFERASE

Acetylcholine is a significant neurotransmitter in both the peripheral and central nervous systems responsible for a host of functions including but not limited to mental concentration, memory, and sleep patterns. Acetylcholine is synthesized in the body from dietary choline and acetyl-coenzyme A, a derivative of vitamin B5, by the enzyme choline acetyltransferase. Acetaldehyde has been shown to inhibit the production side but not the degradation side of acetylcholine thus creating a deficit in this neurotransmitter.

Compare the structures of acetyl-CoA (a necessary precursor of acetylcholine) and acetaldehyde:





The H3C-C=O- portions of these two molecules are identical! Furthermore, it is the enzymatic "transfer" of this structure that transforms choline into acetylcholine.





If rogue molecules of acetaldehyde are contaminating the enzyme reaction pockets at the sites designed to hold acetyl-CoA in place for the acetyl transfer, then the enzyme becomes dysfunctional and acetylcholine can no longer be produced by the affected enzymes. Reduced activity of acetylcholinetransferase has been clinically demonstrated in patients with Alzheimer's disease. It might also be the source of the "brain fog" so commonly reported by individuals with yeast overgrowth.

Is this why coconut oil, an antifungal, that can disrupt yeast cell membranes has anecdotal reports about improving these conditions -- because it reduces the amount of acetaldehyde being released by budding yeast cells that would subsequently be available for enzymatic interference with the production of this essential neurotransmitter?


GLUCOSAMINE-PHOSPHATE N-ACETYLTRANSFERASE

Human joints are bone-to-bone junctions that require special lubricants to reduce friction and provide shock absorption. Synovial fluid in the joint cavities contains hyaluronic acid, a large gooey molecule, that is capable of providing such protection. If the buffering capability of synovial fluid is impaired, then inflammation and joint pain are the result.

Hyaluronic acid, itself is composed of long linked chains of D-glucuronic acid and D-N-acetylglucosamine. A critical step in the production of D-N-acetylglucosamine is the transfer of an acetyl group, again from acetyl-CoA, to D-glucosamine 6-phosphate catalyzed by glosamine-phosphate N-acetyltransferase, producing N-acetyl-D-glucosamine 6-phosphate.





See the familiar H3C-C=O- structure at the lower right hand corner of the molecule. This comes from acetyl-CoA in a manner very similar to the production of acetylcholine but in a different enzyme with a different starting molecule. If free acetaldehyde also contaminates this enzyme, again because of its similarity in shape to acetyl-CoA, then the downstream production of N-acetyl-D-glucosamine and ultimately of hyaluronic acid would be impaired.

One doesn't have to dig too deeply to find attempts to compensate for the failure of this pathway, given the popularity and availability of glucosamine sulfate supplements on the market for arthritic conditions. Is this why acetaldehyde scavengers, such as sulfurated flax oil (Wondro), had such amazing results with a wide variety of arthritic conditions -- by ensnaring the acetaldehyde being released by yeast cells before it could interfere with the maintenance of synovial fluid?

The enzymes described above are just two of a much larger class of acetyl transferase enzymes, all of which may be subject to acetaldehyde inhibition. And this type of attack is not the only way that acetaldehyde can interfere with essential body processes. As suggested by Truss in his research and clinical practice, is this why candidiasis syndrome has such a confusing symptomatic profile with a wide variety of different illnesses responding to yeast abatement protocols?
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