Tryptophan synthase or tryptophan synthetase is an enzyme that catalyses the final two steps in the biosynthesis of tryptophan. It is commonly found in Eubacteria, Archaebacteria, Protista, Fungi, and Plantae. However, it is absent from Animalia. It is typically found as an α2β2 tetramer. The α subunits catalyze the reversible formation of indole and glyceraldehyde-3-phosphate (G3P) from indole-3-glycerol phosphate (IGP). The β subunits catalyze the irreversible condensation of indole and serine to form tryptophan in a pyridoxal phosphate (PLP) dependent reaction. Each α active site is connected to a β active site by a 25 angstrom long hydrophobic channel contained within the enzyme. This facilitates the diffusion of indole formed at α active sites directly to β active sites in a process known as substrate channeling. The active sites of tryptophan synthase are allosterically coupled.
Aromatic L-amino acid decarboxylase, also known as DOPA decarboxylase (DDC), tryptophan decarboxylase, and 5-hydroxytryptophan decarboxylase, is a lyase enzyme, located in region 7p12.2-p12.1.
Carboxy-lyases, also known as decarboxylases, are carbon–carbon lyases that add or remove a carboxyl group from organic compounds. These enzymes catalyze the decarboxylation of amino acids, beta-keto acids and alpha-keto acids.
In enzymology, an aminomuconate-semialdehyde dehydrogenase (EC 1.2.1.32) is an enzyme that catalyzes the chemical reaction
The enzyme 2,2-dialkylglycine decarboxylase (pyruvate) (EC 4.1.1.64) catalyzes the chemical reaction
The enzyme 2-oxoglutarate decarboxylase (EC 4.1.1.71) catalyzes the chemical reaction: 2-oxoglutarate succinate semialdehyde + CO2
The enzyme 3-dehydro-L-gulonate-6-phosphate decarboxylase (EC 4.1.1.85) catalyzes the chemical reaction
The enzyme 5-oxopent-3-ene-1,2,5-tricarboxylate decarboxylase (EC 4.1.1.68) catalyzes the chemical reaction
The enzyme acetolactate decarboxylase (EC 4.1.1.5) catalyzes the chemical reaction
The enzyme aspartate 1-decarboxylase (EC 4.1.1.11) catalyzes the chemical reaction
In enzymology, an aspartate 4-decarboxylase (EC 4.1.1.12) is an enzyme that catalyzes the chemical reaction
Diphosphomevalonate decarboxylase (EC 4.1.1.33), most commonly referred to in scientific literature as mevalonate diphosphate decarboxylase, is an enzyme that catalyzes the chemical reaction
The enzyme indole-3-glycerol-phosphate synthase (IGPS) (EC 4.1.1.48) catalyzes the chemical reaction
The enzyme indolepyruvate decarboxylase (EC 4.1.1.74) catalyzes the chemical reaction
The enzyme oxalyl-CoA decarboxylase (OXC) (EC 4.1.1.8), primarily produced by the gastrointestinal bacterium Oxalobacter formigenes, catalyzes the chemical reaction
The enzyme phenylalanine decarboxylase (EC 4.1.1.53) catalyzes the chemical reaction
The enzyme phenylpyruvate decarboxylase (EC 4.1.1.43) catalyzes the chemical reaction
The enzyme sulfinoalanine decarboxylase (EC 4.1.1.29) catalyzes the chemical reaction
The enzyme threonine-phosphate decarboxylase (EC 4.1.1.81) catalyzes the chemical reaction
L-Tryptophan decarboxylase is an enzyme distinguished by the substrate L-tryptophan.
