Understanding the Links Between Biochemical Factors and Health

In recent years, scientists have uncovered intriguing links between biochemical factors and health issues. Three key players in this complex interaction are methylene cysteine, also known by the clinical abbreviation Hcy, choline kinase alpha, and phosphatidylethanolamine N-methyltransferase (PEMT). These factors are a convergence context for emergence of life, sequestration of material by the Higgs fields to cause exhibition of the material aspects of the Universe, and sustainment of the anion gap which emerges as modality of sequestration hydrogen anion to foundationally power exhibition and sustainment of Life. Understanding how these elements connect can enhance our grasp of disease origins and open doors to new intervention strategies. This post sheds light on these critical components and their implications for health and disease management.

A Full Stack Perspective of Biology, Physiology, Physiological Structure and Life, Opening the Possibility of Indefinite Sustainable Being Bereft of Disease Enabling the Possibility of Sustainable and Indefinite Sustainment of the Human Experience

Methylene cysteine known as (clinically known as Hcy, homocysteine, (2S) 2 amino 4 sulfanylbutanoic acid, 2 AMINO 4 MERCAPTO BUTYRIC ACID,

0LVT1QZ0BA, L 2 Amino 4 mercaptobutyric acid, 2 amino 4 mercapto Butyric acid, 2 amino 4 sulfanylbutanoate, 2 amino 4 mercapto Butanoic acid, (2S) 2 azaniumyl 4 sulfanylbutanoate, (2S) 2 azaniumyl 4 sulfanylbutanoate, 2 amino 4 mercaptobutyric acid, Butanoic acid, 2, amino 4 mercapto , 2 Amino 4 Mercaptobutyric Acid, 2 Amino 4 Sulfanylbutanoic Acid, (s) 2 amino 4 mercaptobutanoic acid, (S) 2 Amino 4 mercaptobutyric acid, Butyric acid, 2 amino 4 mercapto L , 2 Amino 4 mercaptobutyric acid (VAN), Butanoic acid, 2 amino 4 mercapto , Butanoic acid, 2 amino 4 mercapto , (S) 2 amino 4 mercapto Butanoate, 2 amino 4 mercapto DL Butyrate, (S) 2 amino 4 mercapto Butanoate, L 2 amino 4 mercapto Butyric acid, (s) 2 amino 4 mercaptobutanoicacid, 2 amino 4 mercapto DL Butyric acid, DL 2 amino 4 mercapto Butyric acid, (S) 2 amino 4 mercapto Butanoic acid)

Methylene cysteine and relevant metabolites relegated to these levels and other relevant insight

Methylene cysteine level< 6 µm/L. s adenosyl methylene cysteine < 0.012 µm/L/. NAD+/NADH about 1/1 to 1/10 while in cytoplasm about 700/1, but possibly as low as 60/1 circumstantially in compartments. Therapeutic prevention of NADase activity to prevent catabolism of NAD+. Support and supply of glycolysis supply of substrate to Krebs Cycle, Pyruvate transport to Krebs cycle, Krebs cycle supply of substrate to the electron transport pathway, thioretinaco ozonide complex initiation of electron transport pathway in the cristate of the inner mitochondrial membrane, electron transport pathway access NADH and FADH2, Complex I supply of hydrogen anion quantum multiplicity to thioretinaco ozonide complex for its metabolisms to the ATP synthase Complex/Complex V, Complex v/ATP Synthase obtain of hydrogen anion multiplicity from electron transport pathway to enable the packing of the boundless multiplicity of hydrogen anion into two oxygen atoms to produce oxonium that is packed between the phosphate groups of ATP.

The information presented in this context explains how experimental conditions produced an inability to ascertain cognitive, observational, diagnostic, clinical, functional, and activity differences in early developmental and extremely advanced age small nonhuman mammals, which present opportunities to support indefinitely sustainable being in Homo Sapiens Sapiens.

Regulation of the mitochondrial permeability pore and its supply of ATP to phosphorylation cascades. Regulation choline kinase alpha potential for overexpression and overuse of ATP. Assure that ATP is available for synthesis of s adenosyl methionine. Assure that s adenosyl methylene cysteine becomes s adenosyl methionine or is metabolized to methylene cysteine for attachment of a methyl group to produce methionine or is depleted through the transsulfuration pathway of cystathionine beta synthase and cystathionine gamma lyase.

Assuring that early biome exhibition of methylene cysteine Hcy, mercaptopropanal and methionine as potentially the first amino acids the encoding of methionine in more than 99 percent of proteins and the insertion of methionine by tRNA at ribosome molecular machines as the first amino acid in protein synthesis even if methionine is not encoded by DNA for a protein.

Assuring that ATP is available for attachment to methionine which causes a carbocation rearrangement in which the hydrogen multiplicity of its oxonium is redistributed throughout the s adenosyl methionine molecule to cause an ionization of the sulfur to S+.

Assurance that CH3 and its hydrogen anion component within s adenosyl methionine is available for removal from s adenosyl methionine by PEMT, packing into membranes by the enzyme PEMT1 S beginning near conception or before and then PEMT2 L and PEMT3 L beginning near conclusion of gestation both in regulation of the developmental and to massively decrease mitotic velocity potentiated by PEMT1 S.

Regulating mTorc1 in factor of Mtorc2 because mTorc2 because mTorc2 promotes the exhibition of the mitochondrial associated membrane shared by the endoplasmic reticulum and the mitochondria which is the only known habitat for PEMT2 L and PEMT 3L, while PEMT1 is exhibited in the membrane of the endoplasmic reticulum.

Assuring Cx43 and AQP4 is available for transport of NAD+ and modulated to prevent gap junction exchange of antimetabolites and elements disease used in disease proliferation and expansion, although the same regulation must be used to regulate detriment vesicles exported from the cytoplasm to other local and distal tissues.

Regulation and management of primary inhibitors of PEMT such as CRP protein, tmao protein, AP1 protein and SP1 protein which interact to produce a primary escape mechanisms from replicative senescence, Methylglyoxal, IDO, iNOS/NOS2, Oxalate, and methylene cysteine known as Hcy.

Requiring the implementation of these capabilities in all instances of care.

Inpatient admittance when methylene cysteine is at or above 15 µmol/L, regardless of if there are symptoms or not.

Inpatient admittance if methylene cysteine Hcy is at 10 µmol/L or higher along with symptoms.

Outpatient care if methylene cysteine is 10 µmol/L or higher without symptoms.

Outpatient care if methylene cysteine is above 6 µmol/L with symptoms.

Office Visit, Primary or other modalities of care if methylene cysteine is µmol/L is above 6 µmol/L

Therapies of methylene cysteine should have a priority of creating 2 weeks of methylene cysteine lower than 6 µmol/L with a goal of reaching 3.7 µmol/L, while managing methylene cysteine after two weeks of lower than 6 µmol/L is reached.

Practice management analytics and Agentic AI should be used to refine practice parameters used in each practice instance using improvement statistics and extended duration follow up outcomes because the capabilities of care are so expansive and the physiologically causal factor can be metabolic, behavioral and environmental including activation of the HRE hypoxia response element, genetic status, environmental toxins which activate Aryl Hydrocarbon receptor and HIF2 alpha activation by AHr, response to external factors by PEMT, Choline Kinase Alpha, and methyltransferase other than PEMT.

Implementation of factors that are known to alleviate the effects of methylene cysteine because methylene cysteine might be increase instantaneously or circumstantially as well persistently or otherwise.

Agrin hypodermic insertion into ECM matrix to cause complete regeneration of central most substantial circulatory function tissue complex.

Repression of methylene cysteine to < 6 µmol/L toward 3.7 µmol/L which are causally linked to all factors occurring detrimentally with increase age and differences in prognosis, health status, susceptibility to disease and level of disease.

Modulate NAD+ attrition pathways, NAD+ production pathways, NAD+/NADH ratio, NMN/NADH ratio and NAD+/ADPR and NAD+/cADPR ratios, which are causally linked to all factors occurring detrimentally with increase age and differences in prognosis, health status, susceptibility to disease and level of disease.

Requiring tmao protein to be proactively repressed and repressed in every care intervention because it is the among the most causal risk elements to adverse health outcomes, sudden adverse events, sudden adverse vascular events, perioperative complications, cardiovascular risk, and other adverse outcomes.

Repression of USAG1 and BMP7 to cause complete regeneration of all dental structure.

Use of an environmental and individual group of EMF protection capabilities, modalities, tools and protocols.

Modulation of USAG1 and BMP7 to cause complete regeneration of the renal tissues and renal complexes.

Use of FoxN1 to cause complete regeneration of the thymus complex and tissues.

Use of PROTAC to specifically remove particular disease factors and proteins

Use of CRISPR Genetic Editing to resolve any genetic anomalies which have emerged to cause disease, enable susceptibility to disease.

Use of CRISPR Genetic Editing to specifically genetically deteriorate or impede genetic expression by microbes with a formulation for every microbe known to cause disease.

Circumstantial modulation of SARM1 Armadillo Domain affect functional tissue, NMN/NAD+ ratio, NAD+/ADPR ratio, ADP/cADPR ratio, GDNF, Cx43, AQP4, MCP1, MCP2 and MCP3, along with L arginine availability modulation, emerge as dual a strong factors in therapeutically preventing and repressing conditions such MS, Parkinson's, AZ, and ALS conditions as well as the preventing and repression dysregulated control of proliferation of tissue in the same area of anatomy relevant to these conditions.

Resolving access to housing, clean water, clean restrooms, care coverage, care which considers that foundational causal factors to disease, nutritional stability, social stability, economic stability, safety, cognitive care, other social welfare requirements and other Human welfare requirements.

The factors presented in this context might be reasonable considered as including factors that might be the most causally relevant in exhibition, persistence and advancement of massive aspects of disease diminished behavior, advancement of disease and potential for detrimental prognosis.

Circumstantial modulation of NADases PARP1 or other PARP, CD38, CD157, Sirt1, and SARM1, although there can be other NADases in this context, because these cause attrition of NAD+ and diminished the effectiveness of NAD+ synthesis, recycling and supplementation in sustaining the between 1 and 10 or 3 ratio of NAD+/NADH in tissue, and sustaining the between 60 and 700 or 700 ratio of NAD+/NADH in areas of the cytoplasm, each of which are important because these provide gradients that power the capture of the interstellar/terrestrial/biome/physiological hydrogen anion lake into NAD+ to produce NADH. Hydrogen anion in its boundless nonquantized multiplicity and integrated into helium capture energy and redirect resources into producing celestial entities including stars that are similar to or cooler than the Sun, while hydrogen is the foundational atom including in every atom, hydrogen in its different status captures particles obtaining mass from the Higgs field as they assemble themselves, Hydrogen emerges from uncoordinated movement of electrons and protons which becomes coordinated in an orbital arrangement known as the hydrogen atom, while neutrons emerge slightly differently but are integrated to produce other atoms, such that hydrogen is a group of particles given mass by the Higgs fields to produce uncoordinated electrons and protons which then become coordinated into an orbital relationship to produce Hydrogen. Hydrogen might be regarded as an orbiting relationship between an electron and proton which involves the electron presuming more prominently its particle multiplicity compared to its energy, wave, superposition multiplicities, although these other multiplicities are maintained and can even independently interact with as in quantum computing dynamics.

A Hydrogen anion, involves capture of an electron into hydrogen resulting in an integrated high energy electron used to power important pathways such as glycolysis production of pyruvate and NADH, directing of pyruvate to the mitochondria and Krebs Cycle instead of other pathways including instead of potential directing of NADH and Pyruvate toward NAD+ and Lactate anion to supply substrate to dysregulated PARP signaling, the Electron Transport Pathway, thioretinaco ozonide complex metabolic transition to become the ATP synthase complex or Complex V of the Electron Transport Pathway, fragmented aspects of hydrogen anion which are packed into Oxygen as oxonium between the phosphate groups of ATP in catalysis known as Oxidative Phosphorylation performed by ATP Synthase (complex 5 of the Electron Transport Pathway), and culminating in regulated dispensing of ATP and stabilization of the mitochondrial permeability pore. Important to these is the import of pyruvate into the mitochondria to enter the Krebs Cycle which becomes disrupted by redirecting of pyruvate and mPOS syndrome which prevents import of proteins into the mitochondria. The mitochondrial pyruvate carrier is involved in moving pyruvate into the mitochondria where the Krebs cycle uses pyruvate within the matrix of the inner mitochondrial membrane.

Hydrogen is the most abundant atom in the universe, perhaps as much as a hydrogen/other atom ratio of 10/1 (according to some perspectives in some contexts of consideration which suggest that 90 percent all atoms are hydrogen, 92 percent of all atoms are hydrogen, 93 percent of all atoms are hydrogen, 75% of all atoms in the universe are hydrogen, 99 percent of all the atoms are hydrogen or hydrogen/helium conjugates and an estimated 61 percent of atoms in physiology are atoms, although, again, all atoms are purported to constitutively exhibit hydrogen) and this ratio is at least relevant to NAD+NADH ratios that power capture of hydrogen anion as a basis of sources of power that enable independent activity in coordination with, parallel to and sometimes in surmounting of the fundamental gradients of the biome. This capture and redirection of power is a characteristic of Life. The anion gap or strong ions loosely regard the gap between NAD+ and NADH or the gap between other similar primary carriers of hydrogen anion(NADP+/NADPH, FAD/FADH2, or other) because this is an indicator of the availability of Hydrogen anion in both its integral molecular status and its boundless status as an excited integral hydrogen anion or as an ejected electron in its boundless multiplicity which more strongly is exhibited as 2 eV per Hydrogen anion( or fragmented variable eV as hydrogen anion absorbs between 0.75 and 4.0 eV of the electromagnetic spectrum and can donate or abdicate and receive such electromagnetic vectors in fragmented amounts), fluorescence, wave function, or Multiplicity.

Nutritional, environmental, mineral, biosynthetic, paramagnetic and quantum spin liquid, or other, modalities of hydrogen anion or electron multiplicity onboard or obtainment are known of, while particular research observes that nearest neighbor or first level exchange cannot exceed the velocity of light, although transitive multiple order exchange escapes this limitation, such that the known interaction of quantum spin liquids to reach to universes level exchange networks confirm experiments that present the ability to produce unobserved outcomes and then change those outcomes in subsequent instances of time by introducing and modulating new relationships with the multiple factors participating in the incipient observation. The information in the literature does not seem to be sure if this a fluid or spatial dynamic and is not sure if this results from hydrogen's encompassing multiplicities or if these dynamics are the result of the outer energy levels of all atoms being an open system which shares spatial and quantum aspects of the Universe. One fact seems to be certain, the multiplicities of all particles in the Universe such as wave, particle, energy, fluorescent, superposition and including other which are not yet completely ascertained and understood, involve paradoxes in which the material comprising an electron to permeate the nucleus of an atom, multiplicities that do not require impeding interactions, whereas all throughout the universe the exhibition of material aspects of the Universes seem inconsequential which require such impeding interaction largely benefit the exhibition of life and largely benefit cognitive aspects of intelligent being. Hardly any celestial interaction between material aspects of the universes are beneficial to the entities involved, except that these are beneficial to life.

Exchange of photons is essential in observation of material factors and material of the Universe which result in collapse of quantum material and electrons in particular into their particle multiplicity. Such interactions are coupled with transitive interactions occurring at universes levels that are quantumly entangled, which are presented as occurring as rapidly as 30,000 times the velocity of light, which through transitive interactions escape axioms or postulations which relegate nearest neighbor interactions among quantumly entangled interactions to the velocity of light, including interactions into antecedent eras and into eras which are to come and even into eras that have already emerged in aspects of the future. There is a possibility that Life, increasingly in expansiveness of all Universes, interactively into antecedent instances of time and interactively into eras which are to come, including interaction with eras of immediacy, enable the inanimate aspects of the universes, too, to Live.

These irrefutably represent a favor afforded by the creative forces of the universe to life, extended into all antecedent eras, all future eras, eras immediacy, all aspects of the material universe and untranslated substrate of the Higgs field, which through hydrogen and its multiplicities and version, encompassing of all structure of the universes, and culminated in the anion gap where hydrogen anion, electrons ejected from hydrogen anion, hydrogen otherwise and its electrons in it quantum multiplicities are shared as a foundational resource in the catalytic nuances that sustain Life. Although the anion gap is clinical phenomenon used clinically to determine balance between particular anions, there is a very strong correlation that suggests that these anions interact with quantum multiplicities enabled or supported by NAD+/NADH and other Hydrogen anion carriers as these supportive factors exhibit exchange, release, capture, regeneration, and interactivity through space and otherwise which constitute fields and resources. These fields and resource seem to emerge as factors that other atoms, molecules, physiology and physiological conditions may share, use or benefit from.

The anion gap used in clinical medicine is presented as being detrimentally effected by disrupted NADH/NAD+ ratio while numerous factors which disrupt PEMT, commandeer glycolysis, affect redox exchange of ions, require toxicity intervention, or which cause disrupted cysteine pathways, increase methylene cysteine, or otherwise confirm the observation in this compendium of research. www.ebmcosult.com presents information on the Anion Gap differential diagnoses. The literature presents a typical anion gap between 8 and 12, with -2 or +2 variance possible. The anion gap diagnostically indicate toxic effects of Acetaminophen, alcoholic ketoacidosis, diabetic ketoacidosis, exposure to ethylene glycol, iron, metformin, phenformin, methanol, salicylates including salicylic acid, paraldehyde, cyano molecules, lactic acid, isoniazid INH, or other syndromes and toxic factors or conditions that repress PEMT, increase methylene cysteine, increase choline kinase alpha, redirect ATP toward phosphorylation cascade, disrupt mitochondrial respiration and production of ATP, overuse methyl groups, prevent adequate availability of s adenosyl methionine for PEMT catalysis, or directly sequester electrons or sequester hydrogen anion from NAD+/NADH gap, FAD/FADH2 gap, NADP+/NADPH gap, or from any other redox capable oxidized/reduce paired ion versions, all of which can be counteracted. Research also correlated each standard deviation in the circulatory fluid anion gap with a 120 percent increase in risk for all causes of the most detrimental of outcomes in highly interventional care contexts, correlates increased anion gap with all causes of the most detrimental of outcomes when very advanced renal conditions are exhibited, nonlinearly correlates anion gap with all causes of the most adverse of outcomes in mature phases of being. Calculated anion gap without potassium is Na-(CL + HCO3), calculated anion gap with potassium K is (Na + K) – (Cl + HCO3+), and calculation for the delta gap which does not use potassium K is [Na – (Cl + HCO3)] – 12. Typical anion gap is between 8 and 12 mEq/L or between 8 and 12 μM/L. D lactic acid is an obscure substantial risk factor for the most detrimental of outcomes and is typically correlated to lower than typical anion gap observations. However, D lactic acid is linked to inability to metabolize D Lactate, L Lactate and L lactic acid, which are linked to methylglyoxal availability, and methyl glyoxyl, L Lactic Acid and D Lactic acid are each linked to repression of the enzyme PEMT.

The slopes of metabolites which decrease from age 20 to age 60 and older are presented as - 0.040 for NAD+, -0.016 for NAAD, - 0.025 for NADP+, having strong correlation with methylene cysteine. The slope of other relevant metabolites between age 20 and age 60 are 0.023 for NAM, 0.028 for MeNAM, 0.017 for ADPR, 0.027 for NADPH.

Methylene cysteine, hcy, is strongly correlated with increasing phase of being. Methylene cysteine 15 um/L, and thus above 6 um/L, is correlating with advancing age and risk of the most detrimental of outcomes, the attrition among cohorts caused be methylene cysteine and methylene cysteine hcy > 15 um/L and thus above 6 um/L is changed once 80 years of age is reached because attrition among these advanced age cohorts escapes lower methylene cysteine Hcy.

NADase PARP including PARP!, SARM1, CD38, CD157, SIRT including SIRT1, but potentially other other NADases release ribose as ADPR, cADPR or other from NAD+, thus diminishing the strength of the NAD+/NADH specific anion gap, while also producing s adenosyl methylene cysteine. At least two of these result in a strong gradient of glycolysis NADH and Pyruvate to NAD+ and Lactate which deprives Krebs cycle of substrate and potentially deprives mitochondria of pyruvate, deprives pentose phosphate pathway of substrate nucleotide synthesis and NADPH synthesis, while also increasingly relegating pyruvate and NADH away from other pathways of glycolytic supply, all occuring in a way that that directs NADH to NAD+ which is then catabolized by NADases. PARP and SARM1, and potentially these other NADases, then produce methylene cysteine Hcy from NAD+ while at least PARP1 exhibits persistent signaling awaiting availability of nucleotides that are repressed in this context of pentose phosphate pathway repression while PARP1 continues to deplete catabolize and deplete NAD+ to produce a gradient upon which substrate for DNA repair is recruited. ribose is attached to local substrate through parylation which uses the ribose to create a gradient to recruit DNA deoxy ribonucleotides which exhibit ribose and use ribose to create a gradient to recruit RNA as ribonucleotides which exhibit ribose.

SARM1 and PARP1, at least, among NADase promote a condition known as parthanatos in which already differentiated tissue experiences deterioration, stem reserves are caused to emerge from stemness but are prevented from complete repression of stemness and are complexted from complete obtainment of fully differentiated status. This is highly trained phenotype that is linked with disease because it diminishes the plasticity and versatility of tissues.

SARM1 activation by increased NMN compared to NAD+ levels, produces ADPR and cADPR which repress GDNF and causes neurons and axons to deteriorate unders stress or impairment. MCP1, MCP2 and MCP3 recruite leukocytes and activate luekocytes which perform deterioration of neurological tissue incipiently but then are repressed or move to the perimeter of expanding areas of pathology in a dynamic enabled by Cx43 and AQP4 while these same similar contexts are exhibited in oncology such as GBM oncology, except deterioration becomes repressed and is replaced by expandion of the pathology at perimeter of pathology using Cx43 and AQP4 signaling. MCP1 is presented as being required and SARM1 is emerging as an important factor along with Cx43 and AQP4 in GBM Oncology, multiple sclerosis, ALS, Alzheimer's, Parkinson's, Huntington's, dimentia, neurodegenerative, and other conditions, which now have numerous pathways available for being developed for represson, prevention and alleviation.

Enlyte and EnlyteRX repress methylene cysteine.

Inhibitors of PARP including PARP1, SARM1, CD38, CD157, potentially circumstantially also SIRT1 repress highly toxic increases of methylene cysteine Hcy.

S adenosyl methionine provides substrate for PEMT which increases methylene cysteine but also produces numerous benefitial factors compared to toxic metabolites produced by other factors such as some NADases.

The literature observes that PEMT decreases levels of methylene cysteine Hcy through a mechanisms not fully and plainly described, although PEMT creates methylene cysteine, Hcy, as S-adenosyl methylene cysteine as product of its catalytic activity. PEMT use phosphatidylethanolamine and S-adenosylmethionine as substrate to produce de novo choline as phosphatidylcholine, S adenosyl methylene cysteine and H+. PEMT moves CH3 involved in carbocation rearrangement within s adenosyl methionine where the hydrogen multiplicity of ATP within the adenosyl group of s adenosylmethionine is removed, resulting in fractal both in the leaving group of s adenosyl methylene cysteine and fractal within the CH3 being transferred to the Nitrogen of the lead ethanolamine group of the receiving phosphatidylethanolamine. Phosphatidylmonomethylethanolamine by transferring a methyl group to phosphatidylethanolamine and producing S adenosyl methylene cysteine, followed by subsequent catalysis in the same pattern to produce phosphatidyl2methyletabolamine PDME, then producing phosphatidylcholine from PDME, resulting in de novo synthesis of choline within the newly synthesized phosphatidylcholine, preferentially using newly synthesized, unglycosylated or lightly glycosylated phosphatidylethanolamine, phosphatidylethanolamine with nonresolution fatty acids docosahexaenoic acid, arachidonic Acid, Palmitoylic Acid, Oleoylic Acid, and Omega-3 fatty acid.

PEMT production of methylene csysteine, Hcy, is probably integrated into its beneficial products to provide or sustain availability of methylene cysteine for the methyltransferases which produce methionine and do not produce methylene cysteine such as methionine synthase, BHMT, BHMT2, THMT, although cystathionine beta synthase and cystathionine gamma lyase can produced beneficial substrates also otherwise. PEMT may be in interstitial capability between methyltransferase that do not produce methionine, methyltransferase which do produce methionine and methylene cysteine metabolizing enzymes such as cystathionine beta synthase and cystathionine gamma lyase which produce other beneficial metabolites.

PEMT uses newly produced, lightly glycosylates or unglycosylated phosphatidylethanolamine, beneficial fatty acid, and carbocation rearrangement (methyl shift, (H2e1p) shift, Hydrogen anion Shift) CH3 from S-adenosyl methionine.

PEMT Produces PMME, PDME and then de novo choline as phosphatidylcholine with beneficial fatty acids at SN1 and SN2 positions. Also produces methylene cysteine, Hcy, that is considered to be nonharmful, although it contributes to levels of methylene cysteine (Hcy). Might be a reason for disparities in health status.

PEMT enzyme Moves a methyl group, CH3 that has at least on Hydrogen with an extra electron known as Hydrogen anion (H2e1p), from S-adenosyl methionine in three sequential transfers to the open locations of the Nitrogen in the ethanolamine lead group of phosphatidylethanolamine. The first methyl group transfer produces PMME, the second methylene produces PDME and the third methylation causes ethanolamine to become choline to cause de novo synthesis of choline. Pemt prefers newly produced phosphatidylethanolamine with lightly glycosylated tails or unglycosylated tails. Pemt selects or prefers including of resolution phase fatty acids including Docosahexaenoyl, extended length Arachidonoyl, Palmitoyl, Oleoyl, and Omega-3 species.

Phosphatidylethanolamine derived from the CDP-ethanolamine pathway (which is homologous to the CDP-Choline pathway synthesis of phosphatidylcholine which using existing choline to produce phosphatidylcholine) and phosphatidylcholine derived from phosphatidylserine decarboxylase in the Inner Mitochondrial Membrane and in the Golgi Apparatus, participates with components of the CDP-ethanolamine pathway and Methylthioglycolic acid to deteriorate the structural basis of oncology cause molecules, cause expression of tissue plasminogen activator which is a super clot busting factor, cause separation of the abiotic phase from the biotic phase and sequesters useful factors from the abiotic phase for import into the biotic phase while also causing derivatization of factors into more useful biological factors.

PEMT production packs CH3 and CH3 cargo of hydrogen anion into membranes which can be mined such as lands cycle phosphodiesterase and phospholipase freeing of fatty acids, phosphatides and choline factors from membranes for eicosanoid availability to control nonresolution phase signaling followed by recomplexing these factors to shuffle the beneficial fatty acids focused upon by PEMT catalysis and produced nonspecifically by the CDP-choline pathway. CH3 is optimally exhibited on a one to one basis with growth factors membranes, while CH3 attaches itself to the leading edges of expanding structural lattices to abate their expansion.

h) Pemt1 S, is of shorter length compared to both PEMT2 L and PEMT3 L, such that PEMT2 L and PEMT3 L both have only 1 known habitat which is the mitochondrial associated membrane. Confirmingly, Activated FoxO1 inhibits mTorc1 either using Tsc2 or without requirement of Tsc2. FoxO1 activates Sestrin3 causing increases in Sestrin3, while increased Sestrin3 represses mTorc1 signaling, particularly in the presences of Tsc2, while the increased expression of Rictor also causes increase in mTorc2 activity in a manner that leads to Akt activation. However, when Tsc2 is not exhibited, FoxO1 increasing of Rictor results in increased mTorc2 assembly in a manner correlated to the decreased expression of mTorc1. Importantly, mTorc2 performs in promoting of and as a linking factor for the mitochondrial associated membrane between the endoplasmic reticulum and the mitochondria. The mitochondrial associated membrane is where Pemt2 L and Pemt3 L function, is where Pemt2 L and Pemt3 L emerge near conclusion of gestation to perform their catalysis, is where Pemt2 L and Pemt3 L regulate the activity of Pemt1 S. Pemt1 S is exhibited in the endoplasmic reticulum membrane and Pemt1 S emerges at conception or before conception.

THMT thetine Methylene Cysteine methyltransferase use 2methyltetin or trimethylsulphonium and methylene cysteine to produce methylthioglycolic acid and methionine.

BHMT uses methylene cysteine and Betaine or Trimethylglycine or n,n,n glycine betaine to produce methionine and dimethylglycine.

BHMT2 uses methylene cysteine and s methylmethionine sulfonium to produce methionine and dimethylglycine.

INMT uses primary or secondary amines or amide, including selenium, or sulfur or telluride or other along with S adenosyl methylene cysteine to bidirectionally produce s adenosyl methionine and a methylated, 2methylated, or trimethylated version of a primary amine, secondary amine, amide, selenonium, sulphonium, tellurium or other.

Tetrahydrofolate trimethylsulphonium methyltransferase Trimethylsulfonium and 6s 5678 Tetrahydrofolate are bidirectionally metabolized to dimethylsulfide and 5 methyltetrahydrofolate.

S adenosyl methionine synthase uses Methionine, Water and ATP, to produce phosphate, diphosphate and S-Adenosyl Methionine, resulting in a carbocation rearrangement which redistributes the multiplicity of the hydrogen anion multiplicity from the oxonium between the phosphate groups of ATP to instead encompass s adenosyl methionine which results in ionization of the Sulfur to S+.

MARS1/MARS2 Methionyl tRNA Methionyl Ligase. Methionine is important because it is a starting factor or primer in synthesis of more than 99.5 percent of gene transcription products. MARS1, for instance, as Methionine tRNA Ligase catalyzes synthesis of AMP, diphosphate, L-methionyl tRNAMet from ATP, L – methionine and tRNAMet. MARS1 occurs in the Nucleus of Homo Sapiens and MARS2 occurs in the mitochondria, performing a role in enabling incipient nuances of synthesis of RNA in Ribosomal Molecular Machines. This enzyme might be Methionyl tRNA synthetase. MARS is inhibited by methylene cysteine complexing through N methylene cysteinylation of itaconate to produce methylene cysteine itaconate. Also, methylene cysteine itaconate represses both MARS and the NLRP3 nonresolution phase signaling pathways. Itaconate also represses the nonresolution phase including repression of NLRP3. Itaconate also actives NRF2 signaling.

Using NAD+ as a cofactor, H20 and s adenosyl L methylene cysteine are metabolized by S adenosyl Methylene cysteine Hydrolase (SAH Hydrolase) to adenosine and methylene cysteine.

Choline kinase alpha is increased when PEMT is repressed to replace the typically 30 percent of phosphatidylcholine synthesis that PEMT produces compared to the about 70 percent of phosphatidylcholine synthesis produced by the CDP Choline pathway. The CDP choline pathway produces phosphocholine, Citidylylcholine and phosphatidylcholine using ATP and recycle choline which compares to de novo synthesis of choline when PEMT produces phosphatidylcholine. PEMT also preferentially selects newly produce, lightly glycosylated or nonglycosylated phosphatidylethanolamine as substrate, while also preferring phosphatidylcholine substates which exhibit docosahexaenoic acid, arachidonic acid (extended length versions), oleoylate, palmitoylate, and omega-3 fatty acid species. Choline kinase is increased when PEMT is repressed and the CDP choline pathway supplies high energy phosphocholine used to surmount apoptosis, promote instability, diminish plasticity, produce a xenobiotic/toxic/allergic response, supply energy and substrate to proteolysis activity, increase S1P/S1P receptors activation, increase GPCR receptor activations, activate subclinical complements immunological system, directly activate platelets, and activate S!P lyase therapeutic/immunological resistance pathways. Phosphocholine supplies phosphate groups to pathology, pathology vectors, microbes and nonresolution phase signaling, presenting why repression of PEMT can be of consideration detrimental effect.

Choline kinase enable lipolysis of lipid droplets following deprivation of glucose as it is phosphorylated by AMPK to cause movement to lipid droplets, followed by acetylation by KAT5 causing the homodimer to dissociate into a monomer, such that the monomeric Choline Kinase Alpha version 1 becomes a tyrosine protein kinase which phosphorylates proteins PLIN2 and PLIN3 exhibited upon lipid droplets to activate lipolysis.

Choline Kinase Alpha catalyzes choline and ATP metabolism to phosphocholine, ADP and H+.

Choline Kinase Alpha catalyzes ethanolamine and ATP metabolisms to phosphoethanolamine, ADP and H+.

Choline Kinase Alpha version 1 catalyzes L tyrosyl [protein] and ATP metabolism into 0 phospho L tyrosyl [protein], ADP and H+.

The enzymes of the CDP choline and CDP ethanolamine pathway have some catalytic activity that uses substrate and produces products of their correlated enzyme in the other’s pathway. CDP choline pathway activity produces some products of the CDP ethanolamine pathway while the CDP ethanolamine pathway activity also produces some products of the CDP choline pathway.

S-adenosyl methylene cysteine Hydrolase, SAH, SAHH. NAD+ availability, compared to NADH, potentiates production of methylene cysteine or HCY from S-Adenosyl methylene cysteine or SAH. This enzyme has bidirectional activity. SAH hydrolase prevents S adenosyl methylene cysteine, S adenosyl Hcy, from repressing methyltransferase which use S adenosyl methionine as a substrate. This review made a directed effort determine in S adenosyl methylene cysteine Hcy and methylene cysteine Hcy differentially repressed methyltransferases which use adenosyl methionine compared to methylene csysteine was not able to find a distinction. However, this does not indicate that a distinction does not exist, at least from a potency of repression perspective.

Using NAD+ as a cofactor, H20 and s adenosyl L methylene cysteine are metabolized by S adenosyl Methylene cysteine Hydrolase, SAH Hydrolase, to adenosine and methylene cysteine. Adenosine is an inhibitor of choline kinase and mitigates increase in the CDP-choline pathway that can occur when PEMT is repressed. CDP-Choline pathway synthesizes a less specifically resolution phase fatty acid exhibiting phosphatidylcholine compared to PEMT production of highly resolution phase promoting fatty acids. PEMT also produces de novo choline when it produces phosphatidylcholine from phosphatidylethanolamine. S adenosyl methylene cysteine is presented as being optimally repressed to lower than 0.012 μM/L, although the literature does specify if such repression should include SAH Hydrolase, INMT, and other post synthesis metabolism pathways, or if this repression should occur before SAH and INMT because SAH hydrolase produces methylene cysteine from S adenosyl methylene cysteine, such that methylene cysteine is presented as being toxic. Although being repressive of choline kinase, and although repression of choline kinase alpha has the potential of disrupting almost every known pathology affecting homo sapiens, adenosine can then be directed to AMP by adenosine kinase bidirectionally with 5’ Nucleotidase production of Adenosine from AMP. Adenosine can also be directed to Inosine by Adenosine Deaminase.

Methylene cysteine can be of D or L chirality while the research observes that biologically activate version of methylene cysteine are of L chirality, although D methylene cysteine can exist in experimental condition and possibly at nominal levels in physiology as levels of methylene cysteine increase. It has been putatively presents that PEMT production of s adenosyl methylene cysteine is not toxic, while other research does not observe such paradox, while PEMT production of D chirality as an explanation has not even been putatively presented. PEMT production of s-adenosyl methylene cysteine is interesting because PEMT also produces methionine compared to other methyltransferases which use s adenosyl methionine as substrate, suggesting that PEMT is particularly intended to initiate and sustain biosynthesis by supplying methylene cysteine for BHMT, BHMT2, Methionine Synthases, and Cystathionine Beta Synthase to release sequestration of resources performed by methylene cysteine and to sustain availability of methionine for 99.5 percent or protein encoding and supply methionine for 100 percent of protein synthesis as the first protein which tRNA includes in any protein synthesis. There are numerous methyltransferases and methylpherases which produced S adenosyl methylene cysteine and this include histone methyltransferase which promote methylation of transcription factors and methylation of DNA, constituting important epigenetic modulation of genetic transcription.

Indolethylamine N Methyltransferase catalyzes the bidirectional metabolisms of an amine( primary, secondary or tertiary amine) and S-adenosyl methionine to a methylated tertiary amine, S Adenosyl methylene cysteine and H+. Indolethylamine N Methyltransferase catalyzes the bidirectional metabolisms of dimethylsulfide and S-adenosyl methionine to trimethylsulfonium and S Adenosyl methylene cysteine. Trimethylsulfonium is a substrate for THMT and Tetrahydrofolate Sulphonium methyltransferase. Dimethyl Sulfide, Trimethylsulfonium, a primary methylated amine, a secondary methylated amine. 2-teinmethylthioethanol, Dimethyl Selenide, Dimethyl Telluride, Diethylsulfide, Tryptamine, Diethylsulfide, all along with H+ are substrates of INMT. Increased levels of S-Adenosyl Methionine can naturally potentiate this enzyme toward S-Adenosyl Methionine, but the trimethylated versions of these substrate are exclusive in catalyzing activity toward S –Adenosyl Methionine. Trimethylsulfonium, Trimethylselenonium, Trimethyltellurium , and possibly Trimethylglycine, although Trimethylglycine can be used by BHMT to produce Methionine and Dimethylglycine. Trimethylsulfonium produces linear graphs of the depletion of S-Adenosyl methylene cysteine or SAH because it is used by TTMT toward 6s 5678 Tetrahydrofolate/Dimethylsulfide, used toward Thioglycolic Acid/Methionine by Thetin methylene cysteine methylpherase, and used toward S-Adenosyl Methionine/Dimethyl Sulfide.

Cystathionine beta synthase is activated by S-adenosyl methionine and by methylene cysteine, Hcy as substrate, although methylene cysteine is regarded as an inhibitor of Cystathionine Beta Synthase. Cystathionine beta synthase canonical function is present as pyridoxal 5’ phosphate reliant metabolisms of L methylene cysteine and L serine to Water, and L,L cystathionine. The cystathionine enzymes of the transsulfuration pathway are known to potentially have multiple alternate catalysis. Pyridoxal 5’ Phosphate is the catalytic cofactor version of Vitamin B6 which can be known as pyridoxine. Cystathionine beta synthase is increased in both early gestation before emergence of structure supplying nutrition of from the gestational host to the emerging gestational development complex emerges and is increased in disease such as oncology. Cystathionine beta synthase can be imported into the mitochondria by HSP70 during Hypoxia or activation of the Hypoxia Response Element regardless of if there is an actual exhibition of hypoxia. Cystathionine beta synthase is canonically presented as catalyzing metabolism of L methylene cysteine and L serine to H2O, L,L cystathionine, using also pyridoxal 5’ phosphate as a cofactor. This review is finding that most enzymes can have multiple other pathways, substrates and products.

Cystathionine has been suggested to now have more than merely putative exhibition of an attached heme oxygenase which metabolizes Retinol to Retinoic Acid, Retinoic Acid to Retinamide, Retinamide to thioretinaco, thus enabling the exhibition of thioretinaco ozonide in the cristae of the inner mitochondrial membrane where the electron transport pathway is then resultantly initiated. The thioretinaco ozonide complex then receives high energy electrons that have been packed into NADH and released as the boundless version of Hydrogen Anion as 2 eV, Fluorescence including quantum multiplicity which can include wave, energy, superposition potentialities but are not quantized enabling their hydrogen anion boundless condition to receive and redistribute in fractals up to about 4 eV at a time. This boundless activity by Hydrogen anion and Helium/hydrogen anion conjugates enable exhibition of celestial entities or stars among the universes and enables distribution or receiving of hydrogen anion boundless influences to physiology, biology, energy production, energy storage, structural polymerization and other activity. Thioretinaco ozonide receiving of high energy electrons allows it to become metabolized to become the ATP synthase complex which is complex 5 of the electron transport pathway, while also being a primary of the mitochondrial permeability transition pore which control production and distribution of ATP and which when dysregulated opens to promote apoptosis and necrosis. ATP synthase and electron transport pathway complex 5, then performs oxidative phosphorylation in which about 42, 43, or 44 percent of the high energy electrons released as hydrogen anion multiplicity that has not be used to support the electron transport pathway, which uses about 57, 58 or 59 percent of this resource, is then packed into oxygen to produce oxonium that is then also packed between the phosphate groups of ATP. Cystathionine beta synthase is increased in catalysis above baseline, similarly to cystathionine gamma lyase, by influx of CA2+, while this Ca2+ can also be used by mitochondria to increase ATP synthase because the electron transport pathway typically requires Ca2+.

Cystathionine Gamma Lyase follows cystathionine beta synthase in the transsulfuration pathway. Cystathionine beta synthase is not presented in the research and data as being repressed by methylene cysteine. Cystathionine gamma lyase uses cystathionine to produce L cysteine and can use L cysteine and L methylene cysteine as substrate, resulting in synthesis also of H2S and lanthionine. Cystathionine gamma lyase using two molecules of methylene cysteine which are metabolized to H2S and lanthionine or methyllanthionine.

Human cystathionine gamma lyase exhibits a “profligacy” which includes synthesis of H2S from cysteine and includes synthesis of H2S from methylene cysteine which is clinically known as Hcy. Cystathionine gamma lyase performs a gamma replacement catalysis which condenses two molecules of methylene cysteine to produced H2S and Homolanthionine. Cystathionine gamma lyase exhibits a beta replacement catalysis which condenses two molecules of cysteine to produce lanthionine. The alpha exclusion catalysis of cystathionine gamma lyase, in a specific research article, is presumably the use of L,L cystathionine to produce L cysteine, ammonia, and 2 oxobutanoate at a rate supported by pyridoxal 5’ phosphate availability, although this catalysis is not presented in the research literature as including H2S synthesis. Lanthionine differs from L,L cystathionine by a methylene group. Homolanthionine differs from L,L cystathionine by a methylene group. Alpha and Beta catalysis of cystathionine gamma lyase is linked to about 70 percent of H2S synthesis within typical physiological conditions although increasing methylene cysteine levels can make alpha and gamma catalytic contribution of cystathionine gamma lyase activity increase to nearly 90 percent of H2S production.

Thiopurine/Thioether S Methyltransferase use substrates, Existing S-Adenosyl l methylene cysteine , H+, and 6 methylthiopurine, substrates 6 – methyl thioguanine, H+ and existing S -adenosyl L methylene cysteine, and substrates S -adenosyl L methylene cysteine and a thiopurine s – methylether. Thiopurine S methyltransferase catalyzes the methylation or attachment of a methyl group to thiopurine pharmacological products including S methylation of 6 mercaptopurine, 6 thioguanine, azathioprine, and others, resulting deactivation of these factors to prevent accumulation and repress toxic effect. Allopurinol represses TPMT and Azathioprine potentially enhances TPMT availability and activity. TPMT catalyzes s adenosyl L methionine and a thiopurine metabolism to S-adenosyl L methylene cysteine and a thiopurine S methylether. TPMT catalyzes mercaptopurine and s adenosyl L methionine metabolism to 6 methylthiopurine, S adenosyl L methylene cystine and H+. 6 thioguanine and S adenosyl L methionine are metabolized by TPMT to 6 methylthioguinine, S adenosyl L methylene cysteine and H+. TPMT and BHMT2 are interesting because TPMT has not had a naturally occurring substrate ascertained although it is a naturally occurring enzyme, while BHMT2 has not had a primary physiological substrate ascertained for it although s methylmethionine sulfonium is a primary substrate that is naturally occurring and originates outside of physiology.

Composite of central factors in all cause conclusion of being and detrimental aspects of advancing age, experimentally verified as preventable and able to be alleviated