In biochemistry, a lyase is an enzyme that catalyzes the breaking of various chemical bonds by means other than hydrolysis and oxidation, often forming a new double bond or a new ring structure. The reverse reaction is also possible. For example, an enzyme that catalyzed this reaction would be a lyase:
In biochemistry, mixed acid fermentation is the metabolic process by which a six-carbon sugar is converted into a complex and variable mixture of acids. It is an anaerobic (non-oxygen-requiring) fermentation reaction that is common in bacteria. It is characteristic for members of the Enterobacteriaceae, a large family of Gram-negative bacteria that includes E. coli.
In enzymology, a [formate-C-acetyltransferase]-activating enzyme is an enzyme that catalyzes the chemical reaction
The enzyme ethanolamine ammonia-lyase (EC 4.3.1.7) catalyzes the chemical reaction
In enzymology, an indoleacetaldoxime dehydratase (EC 4.99.1.6) is an enzyme that catalyzes the chemical reaction
In enzymology, a 17α-hydroxyprogesterone aldolase is an enzyme that catalyzes the chemical reaction
The enzyme 4-hydroxy-2-oxovalerate aldolase catalyzes the chemical reaction
The enzyme deoxyribose-phosphate aldolase catalyzes the reversible chemical reaction
The enzyme fucosterol-epoxide lyase catalyzes the chemical reaction
The enzyme indolepyruvate decarboxylase (EC 4.1.1.74) catalyzes the chemical reaction
In enzymology, an oxalate decarboxylase (EC 4.1.1.2) is an oxalate degrading enzyme that catalyzes the chemical reaction
The enzyme threonine aldolase is an enzyme that catalyzes the chemical reaction
The enzyme ethanolamine-phosphate phospho-lyase (EC 4.2.3.2) catalyzes the chemical reaction
The enzyme lactoyl-CoA dehydratase (EC 4.2.1.54) catalyzes the chemical reaction
The enzyme methylglyoxal synthase catalyzes the chemical reaction
The enzyme octopamine dehydratase (EC 4.2.1.87) catalyzes the chemical reaction
The enzyme synephrine dehydratase (EC 4.2.1.88) catalyzes the chemical reaction
In enzymology, formate C-acetyltransferase is an enzyme. Pyruvate formate lyase is found in Escherichia coli and other organisms. It helps regulate anaerobic glucose metabolism. Using radical non-redox chemistry, it catalyzes the reversible conversion of pyruvate and coenzyme-A into formate and acetyl-CoA. The reaction occurs as follows:
Glyoxylate and dicarboxylate metabolism describes a variety of reactions involving glyoxylate or dicarboxylates. Glyoxylate is the conjugate base of glyoxylic acid, and within a buffered environment of known pH such as the cell cytoplasm these terms can be used almost interchangeably, as the gain or loss of a hydrogen ion is all that distinguishes them, and this can occur in the aqueous environment at any time. Likewise dicarboxylates are the conjugate bases of dicarboxylic acids, a general class of organic compounds containing two carboxylic acid groups, such as oxalic acid or succinic acid.
Isethionate sulfite-lyase is a glycyl radical enzyme that catalyzes the degradation of isethionate into acetaldehyde and sulfite through the cleavage of a carbon-sulfur bond. This conversion is a necessary step for taurine catabolism in anaerobic bacteria like Bilophila wadsworthia. IslA is activated by the enzyme IslB which uses S-adenoslymethionine (SAM) as the initial radical donor.
