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- etymologie
Wat (wie) is O-succinylbenzoate synthase - definitie
O-succinylbenzoate synthase
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CLASS OF ENZYMES
EC 4.2.1.113; O-succinylbenzoic acid synthase; OSB synthase; OSBS; 2-succinylbenzoate synthase; (1R,6R)-6-hydroxy-2-succinylcyclohexa-2,4-diene-1-carboxylate hydrolyase (2-succinylbenzoate-forming); (1R,6R)-6-hydroxy-2-succinylcyclohexa-2,4-diene-1-carboxylate hydrolyase
o-Succinylbenzoate synthase (OSBS) () is an enzyme encoded by the menC gene in E.coli, and catalyzes the dehydration of 2-succinyl-6-hydroxy-2,4-cyclohexadiene-1-carboxylate (SHCHC) to form 4-(2'-carboxyphenyl)-4-oxobutyrate, also called o-succinylbenzoate or OSB, hence the name of the enzyme.
Cystathionine beta synthase
![Cysteine metabolism. Cystathionine beta synthase catalyzes the upper reaction and [[cystathionine gamma-lyase]] catalyzes the lower reaction.](https://commons.wikimedia.org/wiki/Special:FilePath/Cysteine biosynthesis.svg?width=200 "Cysteine metabolism. Cystathionine beta synthase catalyzes the upper reaction and [[cystathionine gamma-lyase]] catalyzes the lower reaction.")
MAMMALIAN PROTEIN FOUND IN HOMO SAPIENS
Cystathionine Beta-Synthase; Cystathionine-β-synthase; Cystathionine-beta-synthase; Cystathionine b-synthase; Cystathionine beta-synthase; Cystathionine-b-synthase; Cystathionine synthase; CBS (gene); EC 4.2.1.22; Methylcysteine synthase; L-serine hydro-lyase (adding homocysteine; L-cystathionine-forming)
Cystathionine-β-synthase, also known as CBS, is an enzyme () that in humans is encoded by the CBS gene. It catalyzes the first step of the transsulfuration pathway, from homocysteine to cystathionine:
Chalcone synthase
CLASS OF ENZYMES
Naringenin-chalcone synthase; Naringerin-chalcone synthase; EC 2.3.1.74
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.
