Abusing GRAS #3
Microbiome Metalloprotease destroyed by supplemental EDTA?
Hello Friends. In this instalment we build on the understanding of “natures scissors” explained in article number two which illustrated how protease have the specific function of ungluing protein. Obviously, the entirety of this field is much more complicated but, in my efforts, to simplify these functions down to the ones you can access in your home kitchen we need to have some basic understanding of the overall nature of these scissors to exploit our target molecules. It is good to know how these functions are obligate and a big part of post conformation in the microbiome and multiple gut axis’s in your body. We will see directly that Metalloproteinase [1] plays a critical role in micro differentiation and attraction of fitness, or disease, traits and their inheritance based on proper surface display and static attraction.
We learned from part two that hydrolysis is one of the most important pathways the microbiome uses to communicate with the hosts genes. Nature is full of information and in this context, we can break it into two major categories as they apply to the technology we want to make as to affect these two communicatory growth factors. For our purposes we are trying to target foreign bacterial exotoxins for digestion by our GRAS bacterial product to prevent virulence factors from mobilizing in a first level of order.
But what obligate microbiome function specifically are we targeting? Metalloproteinase and Metalloproteinase Inhibitors are native to wild probiotic bacteria. By targeting natural virulence factors with a flood of fitness molecules supplemented with promoted zinc fingers it is very possible to make this product at home with the right ingredients and preparation technique.
So, let’s have a look at the textbook definition, as described by my agent, of Metalloproteinase with an eye for how they form and how they are broken. By doing this simple analysis we will see the basic function we are going to use but also some quite astounding admissions on industrial chemicals interfering with your microbiomes Metalloproteinase activation/inactivation and communication through normal post translation and how many more people than you previous suspected are suffering from EDTA poisoning.
Metalloproteinases
A metalloproteinase (or metalloprotease) is any protease enzyme whose catalytic mechanism involves a metal ion. Most metalloproteases require zinc, but some use cobalt. The metal ion is coordinated to the protein via three ligands, which can include histidine, glutamate, aspartate, lysine, and arginine. The fourth coordination position is occupied by a labile water molecule.
Metalloproteases are the most diverse of the four main protease types, with more than 50 families classified to date. The metal ion activates the water molecule that performs the hydrolysis reaction. Around half of known metalloproteases contain an HEXXH motif, which forms part of the metal-binding site. This motif can be more stringently defined as 'abXHEbbHbc', where:
'a' is most often valine or threonine
'b' is an uncharged residue
'c' is a hydrophobic residue
Proline is never found in this site, possibly because it would break the helical structure adopted by this motif in metalloproteases.
Classification of Metalloproteinases
Metalloproteinases are classified into two subgroups:
Metalloexopeptidases (EC number: 3.4.17) - cleave peptide bonds at the ends of protein chains
Metalloendopeptidases (EC number: 3.4.24) - cleave peptide bonds within protein chains
Well-known metalloendopeptidases include:
ADAM proteins (A Disintegrin And Metalloproteinase)
Matrix metalloproteinases (MMPs)
M16 metalloproteinases such as Insulin Degrading Enzyme and Presequence Protease
Examples and Functions
ADAM12: Plays a significant role in the fusion of muscle cells during embryo development (myogenesis)
CAAX prenyl protease 1: From family M48, this integral membrane protein proteolytically removes the C-terminal three residues of farnesylated proteins
M50 family: Includes mammalian sterol-regulatory element binding protein (SREBP) site 2 protease and Escherichia coli protease EcfE
Inhibition
Metalloproteinases are effectively inhibited by:
Chelating agents such as EDTA, which remove the essential metal ions
Orthophenanthroline, another chelator
Metalloproteinase inhibitors are also found in numerous marine organisms, including fish, cephalopods, mollusks, algae, and bacteria. [2]
As you can see, this pathway is vital for the signaling of post translational motifs with over 50 diverse combinations of said signals and that EDTA can easily disrupt the function of. Its commonly known, and practiced, that the use of EDTA as a remedy for heavy metals is actually common with many websites suggesting you gobble this supplement down for imaginary health benefits. [3] It is true that under prescribed conditions heavy metals can be remediate it is actually not that necessary because EDTA is ubiquitous in the food supply as an ingredient or preservative.
In the next installment we will determine exactly how excessive EDTA consumption interferes with your body’s natural metalloprotease pathways are damaged by this ubiquitous chelating agent
[1] https://en.wikipedia.org/wiki/Metalloproteinase
[2] Answer from my Agent
[3] https://news.bionoxusa.com/the-comprehensive-guide-to-edta-chelation-detoxifying-
heavy-metals-and-reducing-arterial-calcification/