6'-Deoxychalcone synthase | |||||||||
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Identifiers | |||||||||
EC no. | 2.3.1.170 | ||||||||
CAS no. | 114308-23-5 | ||||||||
Databases | |||||||||
IntEnz | IntEnz view | ||||||||
BRENDA | BRENDA entry | ||||||||
ExPASy | NiceZyme view | ||||||||
KEGG | KEGG entry | ||||||||
MetaCyc | metabolic pathway | ||||||||
PRIAM | profile | ||||||||
PDB structures | RCSB PDB PDBe PDBsum | ||||||||
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In enzymology, a 6'-deoxychalcone synthase (EC 2.3.1.170) is an enzyme that catalyzes the chemical reaction
The 4 substrates of this enzyme are malonyl-CoA, 4-coumaroyl-CoA, NADPH, and H+, whereas its 5 products are CoA, isoliquiritigenin, CO2, NADP+, and H2O. Deoxychalcone synthase catalyzed activity is involved in the biosynthesis of retrochalcone and certain phytoalexins in the cells of Glycyrrhiza echinata (Russian licorice) and other leguminous plants.
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 malonyl-CoA:4-coumaroyl-CoA malonyltransferase (cyclizing, reducing).
Isoliquiritigenin is a phenolic chemical compound found in licorice.
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 biochemistry, fatty acid synthesis is the creation of fatty acids from acetyl-CoA and NADPH through the action of enzymes called fatty acid synthases. This process takes place in the cytoplasm of the cell. Most of the acetyl-CoA which is converted into fatty acids is derived from carbohydrates via the glycolytic pathway. The glycolytic pathway also provides the glycerol with which three fatty acids can combine to form triglycerides, the final product of the lipogenic process. When only two fatty acids combine with glycerol and the third alcohol group is phosphorylated with a group such as phosphatidylcholine, a phospholipid is formed. Phospholipids form the bulk of the lipid bilayers that make up cell membranes and surrounds the organelles within the cells.
In enzymology, a pterocarpin synthase (EC 1.1.1.246) is an enzyme that catalyzes the chemical reaction
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In enzymology, a 6-methylsalicylic-acid synthase (EC 2.3.1.165) is a polyketide synthase that catalyzes the chemical reaction
Fatty-acyl-CoA Synthase, or more commonly known as yeast fatty acid synthase, is an enzyme complex responsible for fatty acid biosynthesis, and is of Type I Fatty Acid Synthesis (FAS). Yeast fatty acid synthase plays a pivotal role in fatty acid synthesis. It is a 2.6 MDa barrel shaped complex and is composed of two, unique multi-functional subunits: alpha and beta. Together, the alpha and beta units are arranged in an α6β6 structure. The catalytic activities of this enzyme complex involves a coordination system of enzymatic reactions between the alpha and beta subunits. The enzyme complex therefore consists of six functional centers for fatty acid synthesis.
In enzymology, an icosanoyl-CoA synthase (EC 2.3.1.119) is an enzyme that catalyzes the chemical reaction
In enzymology, lovastatin nonaketide synthase (EC 2.3.1.161) is an enzyme that catalyzes the chemical reaction
In enzymology, a mycocerosate synthase (EC 2.3.1.111) is an enzyme that catalyzes the chemical reaction
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The biosynthesis of phenylpropanoids involves a number of enzymes.
Cinnamoyl-Coenzyme A is an intermediate in the phenylpropanoids metabolic pathway.
Ketoacyl synthases (KSs) catalyze the condensation reaction of acyl-CoA or acyl-acyl ACP with malonyl-CoA to form 3-ketoacyl-CoA or with malonyl-ACP to form 3-ketoacyl-ACP. This reaction is a key step in the fatty acid synthesis cycle, as the resulting acyl chain is two carbon atoms longer than before. KSs exist as individual enzymes, as they do in type II fatty acid synthesis and type II polyketide synthesis, or as domains in large multidomain enzymes, such as type I fatty acid synthases (FASs) and polyketide synthases (PKSs). KSs are divided into five families: KS1, KS2, KS3, KS4, and KS5.