In molecular biology, biosynthesis is a multi-step, enzyme-catalyzed process where substrates are converted into more complex products in living organisms. In biosynthesis, simple compounds are modified, converted into other compounds, or joined to form macromolecules. This process often consists of metabolic pathways. Some of these biosynthetic pathways are located within a single cellular organelle, while others involve enzymes that are located within multiple cellular organelles. Examples of these biosynthetic pathways include the production of lipid membrane components and nucleotides. Biosynthesis is usually synonymous with anabolism.
The enzyme cystathionine γ-lyase (EC 4.4.1.1, CTH or CSE; also cystathionase; systematic name L-cystathionine cysteine-lyase (deaminating; 2-oxobutanoate-forming)) breaks down cystathionine into cysteine, 2-oxobutanoate (α-ketobutyrate), and ammonia:
In enzymology, an alliin lyase is an enzyme that catalyzes the chemical reaction
Cystathionine beta-lyase, also commonly referred to as CBL or β-cystathionase, is an enzyme that primarily catalyzes the following α,β-elimination reaction
The enzyme 2,2-dialkylglycine decarboxylase (pyruvate) (EC 4.1.1.64) catalyzes the chemical reaction
The enzyme aconitate decarboxylase (EC 4.1.1.6) catalyzes the chemical reaction
In enzymology, an aspartate 4-decarboxylase (EC 4.1.1.12) is an enzyme that catalyzes the chemical reaction
The enzyme dehydro-L-gulonate decarboxylase (EC 4.1.1.34) catalyzes the chemical reaction
The enzyme diaminopimelate decarboxylase (EC 4.1.1.20) catalyzes the cleavage of carbon-carbon bonds in meso 2,6 diaminoheptanedioate to produce CO2 and L-lysine, the essential amino acid. It employs the cofactor pyridoxal phosphate, also known as PLP, which participates in numerous enzymatic transamination, decarboxylation and deamination reactions.
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 hydroxyglutamate decarboxylase (EC 4.1.1.16) catalyzes the chemical reaction
The enzyme indole-3-glycerol-phosphate synthase (IGPS) (EC 4.1.1.48) catalyzes the chemical reaction
The enzyme pantothenoylcysteine decarboxylase (EC 4.1.1.30) catalyzes the chemical reaction
The enzyme phenylalanine decarboxylase (EC 4.1.1.53) catalyzes the chemical reaction
The enzyme phosphatidylserine decarboxylase (EC 4.1.1.65) 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
The enzyme tyrosine decarboxylase (EC 4.1.1.25) catalyzes the chemical reaction
In enzymology, a phosphopantothenate—cysteine ligase also known as phosphopantothenoylcysteine synthetase (PPCS) is an enzyme that catalyzes the chemical reaction which constitutes the second of five steps involved in the conversion of pantothenate to Coenzyme A. The reaction is:
3-Deoxy-D-arabinoheptulosonate 7-phosphate (DAHP) synthase is the first enzyme in a series of metabolic reactions known as the shikimate pathway, which is responsible for the biosynthesis of the amino acids phenylalanine, tyrosine, and tryptophan. Since it is the first enzyme in the shikimate pathway, it controls the amount of carbon entering the pathway. Enzyme inhibition is the primary method of regulating the amount of carbon entering the pathway. Forms of this enzyme differ between organisms, but can be considered DAHP synthase based upon the reaction that is catalyzed by this enzyme.
