The human body contains a vast array of alkaline proteases (AKPs) which regulate protein and amino acid metabolism. Many of these AKPs have been identified and characterized over the last two decades. The human body produces many other important enzymes as well, and these may also be exploited for the manufacture of therapeutic proteins. In most cases, however, the vast majority of proteins produced by the body are critical for normal physiological processes. This is especially true with long-term health problems such as cancer or serious infections. As such, advances in the knowledge of what constitutes the essential molecules necessary to maintain healthy physiology are vital to the success of ongoing and potential medical therapies.
The alkaline proteases enzyme belongs to the class of sulfur synthetases and is cleaved by the action of an amino acid on a pair of metal ions. One such sulfated ester of the glycoside of cysteine is the basis for the popular alpha-sarcosine compound used in herpes vaccine preparations. This versatile compound is also responsible for the catalytic cleavage of the peptide derived from the L-formylated fibers that make up the interior membrane of the human nose. The specialized bacteria isolated from this process have now been tested in various applications, and they seem to be capable of performing several distinct roles in the body.
The catalytic cleavage of certain lipophilic aromatic amino acid derivatives is one of the purest examples of alkaline proteases. These are thought to be produced by anaerobic bacteria living within the gastrointestinal tract, although some evidence suggests that they may also be produced by yeast. Studies using both transgenic and non-transgenic animals show very good levels of production, with the latter being more efficient at breaking down the lipids into peptides useful in applications such as arthritis, skin grafts and wounds treatment.
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