Agmatine N4-coumaroyltransferase

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agmatine N4-coumaroyltransferase
Identifiers
EC no. 2.3.1.64
CAS no. 85030-72-4
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MetaCyc metabolic pathway
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In enzymology, an agmatine N4-coumaroyltransferase (EC 2.3.1.64) is an enzyme that catalyzes the chemical reaction

4-coumaroyl-CoA + agmatine CoA + N-(4-guanidinobutyl)-4-hydroxycinnamamide

Thus, the two substrates of this enzyme are 4-coumaroyl-CoA and agmatine, whereas its two products are CoA and N-(4-guanidinobutyl)-4-hydroxycinnamamide.

This enzyme belongs to the family of transferases, to be specific those acyltransferases transferring groups other than aminoacyl groups. The systematic name of this enzyme class is 4-coumaroyl-CoA:agmatine N4-coumaroyltransferase. Other names in common use include p-coumaroyl-CoA-agmatine N-p-coumaroyltransferase, agmatine coumaroyltransferase, and 4-coumaroyl-CoA:agmatine 4-N-coumaroyltransferase.

Related Research Articles

Agmatine, also known as 4-aminobutyl-guanidine, was discovered in 1910 by Albrecht Kossel. It is a chemical substance which is naturally created from the amino acid arginine. Agmatine has been shown to exert modulatory action at multiple molecular targets, notably: neurotransmitter systems, ion channels, nitric oxide (NO) synthesis and polyamine metabolism and this provides bases for further research into potential applications.

Spermine is a polyamine involved in cellular metabolism that is found in all eukaryotic cells. The precursor for synthesis of spermine is the amino acid ornithine. It is an essential growth factor in some bacteria as well. It is found as a polycation at physiological pH. Spermine is associated with nucleic acids and is thought to stabilize helical structure, particularly in viruses. It functions as an intracellular free radical scavenger to protect DNA from free radical attack. Spermine is the chemical primarily responsible for the characteristic odor of semen.

<span class="mw-page-title-main">Phenylpropanoid</span>

The phenylpropanoids are a diverse family of organic compounds that are synthesized by plants from the amino acids phenylalanine and tyrosine. Their name is derived from the six-carbon, aromatic phenyl group and the three-carbon propene tail of coumaric acid, which is the central intermediate in phenylpropanoid biosynthesis. From 4-coumaroyl-CoA emanates the biosynthesis of myriad natural products including lignols, flavonoids, isoflavonoids, coumarins, aurones, stilbenes, catechin, and phenylpropanoids. The coumaroyl component is produced from cinnamic acid.

<span class="mw-page-title-main">Rosmarinic acid</span> Chemical compound found in a variety of plants

Rosmarinic acid, named after rosemary, is a polyphenol constituent of many culinary herbs, including rosemary, perilla, sage, mint, and basil.

<span class="mw-page-title-main">Chalcone synthase</span>

Chalcone synthase or naringenin-chalcone synthase (CHS) is an enzyme ubiquitous to higher plants and belongs to a family of polyketide synthase enzymes (PKS) known as type III PKS. Type III PKSs are associated with the production of chalcones, a class of organic compounds found mainly in plants as natural defense mechanisms and as synthetic intermediates. CHS was the first type III PKS to be discovered. It is the first committed enzyme in flavonoid biosynthesis. The enzyme catalyzes the conversion of 4-coumaroyl-CoA and malonyl-CoA to naringenin chalcone.

In enzymology, a putrescine carbamoyltransferase is an enzyme that catalyzes the chemical reaction

In enzymology, a 4-coumarate—CoA ligase is an enzyme that catalyzes the chemical reaction

<span class="mw-page-title-main">Agmatinase</span> Protein-coding gene in the species Homo sapiens

In enzymology, an agmatinase (EC 3.5.3.11) is an enzyme that catalyzes the chemical reaction

In enzymology, an agmatine deiminase (EC 3.5.3.12) is an enzyme that catalyzes the chemical reaction

In enzymology, a 6'-deoxychalcone synthase (EC 2.3.1.170) is an enzyme that catalyzes the chemical reaction

In enzymology, a diaminobutyrate acetyltransferase (EC 2.3.1.178) is an enzyme that catalyzes the chemical reaction

In enzymology, a flavonol-3-O-triglucoside O-coumaroyltransferase is an enzyme that catalyzes the chemical reaction

In enzymology, a rosmarinate synthase is an enzyme that catalyzes the chemical reaction

In enzymology, a shikimate O-hydroxycinnamoyltransferase is an enzyme that catalyzes the chemical reaction

In enzymology, a trihydroxystilbene synthase (EC 2.3.1.95) is an enzyme that catalyzes the chemical reaction

In enzymology, an agmatine kinase (EC 2.7.3.10) is an enzyme that catalyzes the chemical reaction

Coumaroyl-coenzyme A is the thioester of coenzyme-A and coumaric acid. Coumaroyl-coenzyme A is a central intermediate in the biosynthesis of myriad natural products found in plants. These products include lignols, flavonoids, isoflavonoids, coumarins, aurones, stilbenes, catechin, and other phenylpropanoids.

The biosynthesis of phenylpropanoids involves a number of enzymes.

<i>N</i>-Feruloylserotonin Chemical compound

N-Feruloylserotonin an alkaloid and polyphenol found in safflower seed. Chemically, it is an amide formed between serotonin and ferulic acid. It has in vitro anti-atherogenic activity.

<span class="mw-page-title-main">Hordatine A</span> Chemical compound; biosynthesis of hordatine A

Hordatine A is a phenolic secondary metabolite and an adrenergic antagonist that is found in barley. This natural product is a member of the class benzofurans, and can also be found in barley malt and beer, as it withstands moderate processing. Hordatine A is a hydroxycinnamic acid amide derivative (HCAA) as well as a dimer of coumaroyl agmatine, and is plentiful during the development of barley seedlings, specifically in the shoots. Hordatines and their hydroxycinnamoyl agmatine precursors are of interest because of their antifungal activity against plant pathogens, such as inhibiting spore germination of many fungi species. Hordatine A is thought to be a phytoanticipin, because it is observed in significant amounts in young seedlings and at early growth stages.

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