Shikimate O-hydroxycinnamoyltransferase

Last updated
shikimate O-hydroxycinnamoyltransferase
Identifiers
EC no. 2.3.1.133
CAS no. 73904-44-6
Databases
IntEnz IntEnz view
BRENDA BRENDA entry
ExPASy NiceZyme view
KEGG KEGG entry
MetaCyc metabolic pathway
PRIAM profile
PDB structures RCSB PDB PDBe PDBsum
Gene Ontology AmiGO / QuickGO
Search
PMC articles
PubMed articles
NCBI proteins

In enzymology, a shikimate O-hydroxycinnamoyltransferase (EC 2.3.1.133) is an enzyme that catalyzes the chemical reaction

4-coumaroyl-CoA + shikimate CoA + 4-coumaroylshikimate

Thus, the two substrates of this enzyme are 4-coumaroyl-CoA and shikimate, whereas its two products are CoA and 4-coumaroylshikimate.

This enzyme belongs to the family of transferases, specifically those acyltransferases transferring groups other than aminoacyl groups. The systematic name of this enzyme class is 4-coumaroyl-CoA:shikimate O-(hydroxycinnamoyl)transferase. This enzyme is also called shikimate hydroxycinnamoyltransferase. This enzyme participates in phenylpropanoid biosynthesis.

Related Research Articles

<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.

In enzymology, a 5-O-(4-coumaroyl)-D-quinate 3'-monooxygenase (EC 1.14.13.36) is an enzyme that catalyzes the chemical reaction

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

In enzymology, an anthocyanin 5-aromatic acyltransferase is an enzyme that catalyzes the chemical reaction

In enzymology, a chlorogenate-glucarate O-hydroxycinnamoyltransferase 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 galactarate O-hydroxycinnamoyltransferase is an enzyme that catalyzes the chemical reaction

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

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

In enzymology, a putrescine N-hydroxycinnamoyltransferase is an enzyme that catalyzes the chemical reaction

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

In enzymology, a sinapoylglucose---sinapoylglucose O-sinapoyltransferase is an enzyme that catalyzes the chemical reaction

In enzymology, a tartronate O-hydroxycinnamoyltransferase 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>p</i>-Coumaroylated anthocyanin

p-Coumaroylated anthocyanins are a type of anthocyanins with a p-coumaric acid unit linked with a sugar to an anthocyanidin aglycone. 3-(6-p-Coumaroyl)glucosides are found in grape and wine. Cyanidin-3-O-(di-p-coumarylglucoside)-5-glucoside is found in dark opal basil. Red leaves of Perilla frutescens also accumulate cyanidin 3-(6-O-p-coumaroyl-β-D-glucoside)-5-(6-O-malonyl-β-D-glucoside).

Anthocyanin 3-O-glucoside 6″-O-hydroxycinnamoyltransferase is an enzyme forming delphinidin 3-(6-p-coumaroyl)glucoside from delphinidin 3-O-glucoside (myrtillin) and p-coumaroyl-CoA.

Omega-hydroxypalmitate O-feruloyl transferase is an enzyme with systematic name feruloyl-CoA:16-hydroxypalmitate feruloyltransferase. This enzyme catalyses the following chemical reaction

<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.

References