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:
The transsulfuration pathway is a metabolic pathway involving the interconversion of cysteine and homocysteine through the intermediate cystathionine. Two transsulfurylation pathways are known: the forward and the reverse.
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 D-serine ammonia-lyase (EC 4.3.1.18), with systematic name D-serine ammonia-lyase (pyruvate-forming), catalyzes the chemical reaction
The enzyme ethanolamine ammonia-lyase (EC 4.3.1.7) catalyzes the chemical reaction
The enzyme Glucosaminate ammonia-lyase (EC 4.3.1.9) catalyzes the chemical reaction
The enzyme L-serine ammonia-lyase (EC 4.3.1.17) catalyzes the chemical reaction
The enzyme methionine γ-lyase (EC 4.4.1.11, MGL) is in the γ-family of PLP-dependent enzymes. It degrades sulfur-containing amino acids to α-keto acids, ammonia, and thiols:
The enzyme threonine aldolase is an enzyme that catalyzes the chemical reaction
The enzyme tryptophanase (EC 4.1.99.1) catalyzes the chemical reaction
The enzyme tyrosine phenol-lyase (EC 4.1.99.2) catalyzes the chemical reaction
In molecular biology, the protein domain SAICAR synthase is an enzyme which catalyses a reaction to create SAICAR. In enzymology, this enzyme is also known as phosphoribosylaminoimidazolesuccinocarboxamide synthase. It is an enzyme that catalyzes the chemical reaction
The enzyme threonine synthase (EC 4.2.3.1) catalyzes the chemical reaction
In enzymology, an acyl-[acyl-carrier-protein]-phospholipid O-acyltransferase is an enzyme that catalyzes the chemical reaction
In enzymology, a cysteine synthase is an enzyme that catalyzes the chemical reaction
In enzymology, an O-phosphoserine sulfhydrylase is an enzyme that catalyzes the chemical reaction
In enzymology, an ethanolamine-phosphate cytidylyltransferase is an enzyme that catalyzes the chemical reaction
In molecular biology, the Cys/Met metabolism PLP-dependent enzyme family is a family of proteins including enzymes involved in cysteine and methionine metabolism which use PLP (pyridoxal-5'-phosphate) as a cofactor.
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.
5-Phosphonooxy-L-lysine phospho-lyase (EC 4.2.3.134, 5-phosphohydroxy-L-lysine ammoniophospholyase, AGXT2L2 (gene)) is an enzyme with systematic name (5R)-5-phosphonooxy-L-lysine phosphate-lyase (deaminating; (S)-2-amino-6-oxohexanoate-forming). This enzyme catalyses the following chemical reaction
