Biphenyl synthase | |||||||||
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Identifiers | |||||||||
EC no. | 2.3.1.177 | ||||||||
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 biphenyl synthase (EC 2.3.1.177) is an enzyme that catalyzes the chemical reaction:
Thus, the two substrates of this enzyme are malonyl-CoA and benzoyl-CoA, whereas its three products are CoA, 3,5-dihydroxybiphenyl, and CO2.
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 malonyl-CoA:benzoyl-CoA malonyltransferase. This enzyme is also called BIS.
(S)-3,5-Dihydroxyphenylglycine or DHPG is a potent agonist of group I metabotropic glutamate receptors (mGluRs) mGluR1 and mGluR5.
In enzymology, a cis-2,3-dihydrobiphenyl-2,3-diol dehydrogenase (EC 1.3.1.56) 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 6-methylsalicylic-acid synthase (EC 2.3.1.165) is a polyketide synthase that catalyzes the chemical reaction
In enzymology, an acridone synthase (EC 2.3.1.159) is an enzyme that catalyzes the chemical reaction
In enzymology, a benzophenone synthase (EC 2.3.1.151) is an enzyme that catalyzes the chemical reaction
In enzymology, a beta-ketoacyl-acyl-carrier-protein synthase I is an enzyme that catalyzes the chemical reaction
In enzymology, a beta-ketoacyl-acyl-carrier-protein synthase II (EC 2.3.1.179) is an enzyme 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 phloroisovalerophenone synthase (EC 2.3.1.156) is an enzyme that catalyzes the chemical reaction
In enzymology, a pinosylvin synthase (EC 2.3.1.146) 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
Benzoyl-CoA is a molecule implied in the activity of the different enzymes 4-hydroxybenzoyl-CoA reductase, benzoyl-CoA reductase, benzoyl-CoA 3-monooxygenase, benzoate-CoA ligase, 2alpha-hydroxytaxane 2-O-benzoyltransferase, anthranilate N-benzoyltransferase, biphenyl synthase, glycine N-benzoyltransferase, ornithine N-benzoyltransferase and phenylglyoxylate dehydrogenase (acylating).
The biosynthesis of phenylpropanoids involves a number of enzymes.
Cinnamoyl-Coenzyme A is an intermediate in the phenylpropanoids metabolic pathway.
Acetoacetyl-CoA synthase (EC 2.3.1.194, NphT7) is an enzyme with systematic name acetyl-CoA:malonyl-CoA C-acetyltransferase (decarboxylating). This enzyme catalyses the following chemical reaction
4-hydroxycoumarin synthase (EC 2.3.1.208, BIS2, BIS3) is an enzyme with systematic name malonyl-CoA:2-hydroxybenzoyl-CoA malonyltransferase. This enzyme catalyses the following chemical reaction
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.