Agmatine ((4-aminobutyl)guanidine, NH2-CH2-CH2-CH2-CH2-NH-C(-NH2)(=NH)) is the decarboxylation product of the amino acid arginine and is an intermediate in polyamine biosynthesis. It is discussed as a putative neurotransmitter. It is synthesized in the brain, stored in synaptic vesicles, accumulated by uptake, released by membrane depolarization, and inactivated by agmatinase. Agmatine binds to a2-adrenergic receptor and imidazoline binding sites, and blocks NMDA receptors and other cation ligand-gated channels. Agmatine inhibits nitric oxide synthase (NOS), and induces the release of some peptide hormones.
Peptides are the family of molecules formed from the linking, in a defined order, of various amino acids. The link between one amino acid residue and the next is an amide bond, and is sometimes referred to as a peptide bond. An amide bond is somewhat shorter than a typical carbon-nitrogen single bond, and has a partial double-bond character, because the participating carbon molecule is doubly bonded to an oxygen molecule and the nitrogen has a lone pair of electrons available for bonding.
Peptides (like proteins) occur in nature and are responsible for a wide array of functions, many of which are not yet understood. Antimicrobial peptides generally disrupt the membranes of a target cell, causing lysis of the cell. How this occurs, and what determines the activity and selectivity of these peptides, is currently only known approximately.
It has also beed documented that when certain food proteins such as gluten, casein, egg protein and spinach protein are broken down, opioid peptides are formed. These peptides mimick the effects of morphine, and those who are unable to break them down will experience mental illness. These peptides are quite short and are given names such as casomorphine, gluten exorphine and dermorphine.
Peptides differ from proteins, which are also long chains of amino acids, by virtue of their size. Traditionally, those peptide chains that are short enough to make synthetically from the constituent amino acids are called peptides rather than proteins. The dividing line is at approximately 50 amino acids in length, since naturally-occurring proteins tend, at their smallest, to be hundreds of residues long. So, in essence, a peptide is a small protein.
Peptidomimetics (such as peptoids and Гџ-peptides) are molecules related to peptides, but with different properties.
Decarboxylation>From Wikipedia, the free encyclopedia.
A Decarboxylation is any chemical reaction in which a carboxyl group (-COOH) is split off from a compound as carbon dioxide (CO2).
Common biosynthetic decarboxylations of amino acids to amines are:
tryptophan to tryptamine, phenylalanine to phenylethylamine, tyrosine to tyramine, histidine to histamine, serine to ethanolamine, glutamic acid to GABA, lysine to cadaverine, arginine to agmatine, ornithine to putrescine, 5-HTP to serotonin, and L-DOPA to dopamine.
Other decarboxylation reactions from the citric acid cycle include:
pyruvate to acetyl-CoA, oxalosuccinate to a-ketoglutarate, and a-ketoglutarate to succinyl-CoA.
Enzymes that catalyze decarboxylations are called decarboxylases or, more formally, carboxy-lyases (E.C.4.1.1).
Chemical decarboxylations reactions often require extensive heating in high-boiling solvents. Copper salts are often added as catalysts. Also the addition of catalytic amounts of cyclohexen-2-one has been reported to catalyze the decarboxylation of amino acids. Decarboxylations are especially easy for alpha-keto acids due to the formation of a cyclic transitional state.
Perl Molson 28 February 2005 09:37:22 [ permanent link ]
Perl Molson wrote:> Agmatine> >From Wikipedia, the free encyclopedia.>
Agmatine ((4-aminobutyl)guanidine,
NH2-CH2-CH2-CH2-CH2-NH-C(-NH2)(=NH))> is the decarboxylation product of the amino acid arginine and is an> intermediate in polyamine biosynthesis. It is discussed as a putative> neurotransmitter. It is synthesized in the brain, stored in synaptic> vesicles,
Synaptic vesicle>From Wikipedia, the free encyclopedia.
In a neuron, synaptic vesicles, also called neurotransmitter vesicles, store the various neurotransmitters that are released during calcium-regulated exocytosis at the presynaptic terminal into the synaptic cleft of a synapse. They are essential for the propagation of nerve impulses between neurons and are constantly recreated by the cell.
Synaptic vesicles are made of a bilipid layer in which transport proteins specific to each type of neurotransmitters are inserted. Neurotransmitters are moved from the cytoplasm into the vesicles by active transport mechanisms involving an exchange of protons. The necessary proton gradient is created by hydrogen ATPase. The stoichiometry for the movement of different neurotransmitters into a vesicle is given in the following table.
Neurotransmitter type(s) Inward movement Outward movement norepinephrine, dopamine, histamine, serotonin and acetylcholine neurotransmitter+ 2 H+ GABA and glycine neurotransmitter 1 H+ glutamate neurotransmitter- + Cl- 1 H
accumulated by uptake, released by membrane depolarization,> and inactivated by agmatinase. Agmatine binds to a2-adrenergic> receptor and imidazoline binding sites, and blocks NMDA receptors and> other cation ligand-gated channels. Agmatine inhibits nitric oxide> synthase (NOS), and induces the release of some peptide hormones.>
Peptides are the family of molecules formed from the linking, in a> defined order, of various amino acids. The link between one amino
acid> residue and the next is an amide bond, and is sometimes referred to
a peptide bond. An amide bond is somewhat shorter than a typical> carbon-nitrogen single bond, and has a partial double-bond character,> because the participating carbon molecule is doubly bonded to an
oxygen> molecule and the nitrogen has a lone pair of electrons available for> bonding.>
Peptides (like proteins) occur in nature and are responsible for a
wide> array of functions, many of which are not yet understood. Antimicrobial> peptides generally disrupt the membranes of a target cell, causing> lysis of the cell. How this occurs, and what determines the activity> and selectivity of these peptides, is currently only known> approximately.>
It has also beed documented that when certain food proteins such as> gluten, casein, egg protein and spinach protein are broken down,
opioid> peptides are formed. These peptides mimick the effects of morphine,
those who are unable to break them down will experience mental
illness.> These peptides are quite short and are given names such as> casomorphine, gluten exorphine and dermorphine.>
Peptides differ from proteins, which are also long chains of amino> acids, by virtue of their size. Traditionally, those peptide chains> that are short enough to make synthetically from the constituent
amino> acids are called peptides rather than proteins. The dividing line is
approximately 50 amino acids in length, since naturally-occurring> proteins tend, at their smallest, to be hundreds of residues long.
So,> in essence, a peptide is a small protein.>
Peptidomimetics (such as peptoids and Гџ-peptides) are molecules> related to peptides, but with different properties.>
Decarboxylation> >From Wikipedia, the free encyclopedia.>
A Decarboxylation is any chemical reaction in which a carboxyl group> (-COOH) is split off from a compound as carbon dioxide (CO2).>
Common biosynthetic decarboxylations of amino acids to amines are:>
tryptophan to tryptamine, phenylalanine to phenylethylamine, tyrosine> to tyramine, histidine to histamine, serine to ethanolamine, glutamic> acid to GABA, lysine to cadaverine, arginine to agmatine, ornithine
putrescine, 5-HTP to serotonin, and L-DOPA to dopamine.>
Other decarboxylation reactions from the citric acid cycle include:>
pyruvate to acetyl-CoA, oxalosuccinate to a-ketoglutarate, and> a-ketoglutarate to succinyl-CoA.>
Enzymes that catalyze decarboxylations are called decarboxylases or,> more formally, carboxy-lyases (E.C.4.1.1).>
Chemical decarboxylations reactions often require extensive heating
high-boiling solvents. Copper salts are often added as catalysts.
Also> the addition of catalytic amounts of cyclohexen-2-one has been reported> to catalyze the decarboxylation of amino acids. Decarboxylations are> especially easy for alpha-keto acids due to the formation of a cyclic> transitional state.
Hey, Perlie, do you have something against this group, or any of the> people who post here?>
no, I am a supporter of this group. Things go a bit too far sometimes, that's it.
What is the PURPOSE of the continued nonsense?>
most of the stuff I've posted was very useful in my understanding upon how the herpes virus works. I know it's getting a bit too far aside from the main course but that's how the problem develops.
Are you seeking or offering support? It isn't clear.>
Either way; I seek support and I try to offer my support, as well. I know I am off the topic sometimes but the chain of thought takes me to such topics.
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