Coenzyme A (CoA, SHCoA, CoASH) is a coenzyme, notable for its role in the synthesis and oxidation of fatty acids, and the oxidation of pyruvate in the citric acid cycle. All genomes sequenced to date encode enzymes that use coenzyme A as a substrate, and around 4% of cellular enzymes use it (or a thioester) as a substrate. In humans, CoA biosynthesis requires cysteine, pantothenate (vitamin B5), and adenosine triphosphate (ATP).
In biochemistry and metabolism, beta oxidation (also β-oxidation) is the catabolic process by which fatty acid molecules are broken down in the cytosol in prokaryotes and in the mitochondria in eukaryotes to generate acetyl-CoA. Acetyl-CoA enters the citric acid cycle, generating NADH and FADH2, which are electron carriers used in the electron transport chain. It is named as such because the beta carbon of the fatty acid chain undergoes oxidation and is converted to a carbonyl group to start the cycle all over again. Beta-oxidation is primarily facilitated by the mitochondrial trifunctional protein, an enzyme complex associated with the inner mitochondrial membrane, although very long chain fatty acids are oxidized in peroxisomes.
Calcium propanoate or calcium propionate has the formula Ca(C2H5COO)2. It is the calcium salt of propanoic acid.
Methylmalonyl-CoA mutase is a mitochondrial homodimer apoenzyme that focuses on the catalysis of methylmalonyl CoA to succinyl CoA. The enzyme is bound to adenosylcobalamin, a hormonal derivative of vitamin B12 in order to function. Methylmalonyl-CoA mutase deficiency is caused by genetic defect in the MUT gene responsible for encoding the enzyme. Deficiency in this enzyme accounts for 60% of the cases of methylmalonic acidemia.
Propionyl-CoA is a coenzyme A derivative of propionic acid. It is composed of a 24 total carbon chain and its production and metabolic fate depend on which organism it is present in. Several different pathways can lead to its production, such as through the catabolism of specific amino acids or the oxidation of odd-chain fatty acids. It later can be broken down by propionyl-CoA carboxylase or through the methylcitrate cycle. In different organisms, however, propionyl-CoA can be sequestered into controlled regions, to alleviate its potential toxicity through accumulation. Genetic deficiencies regarding the production and breakdown of propionyl-CoA also have great clinical and human significance.
In enzymology, a 2-oxobutyrate synthase (EC 1.2.7.2) is an enzyme that catalyzes the chemical reaction
In enzymology, a methylmalonate-semialdehyde dehydrogenase (acylating) (EC 1.2.1.27) is an enzyme that catalyzes the chemical reaction
In enzymology, a methylmalonyl-CoA carboxytransferase is an enzyme that catalyzes the chemical reaction
In enzymology, an acetate CoA-transferase is an enzyme that catalyzes the chemical reaction
In enzymology, a malonate CoA-transferase is an enzyme that catalyzes the chemical reaction
The enzyme methylisocitrate lyase catalyzes the chemical reaction
In enzymology, a methylmalonyl-CoA decarboxylase (EC 7.2.4.3) is an enzyme that catalyzes the chemical reaction
In enzymology, a vanillin synthase is an enzyme that catalyzes the chemical reaction
In enzymology, an acetate—CoA ligase (ADP-forming) is an enzyme that catalyzes the chemical reaction
In enzymology, a propionate—CoA ligase is an enzyme that catalyzes the chemical reaction
In enzymology, a 2-methylcitrate synthase (EC 2.3.3.5) is an enzyme that catalyzes the chemical reaction
In enzymology, an acetyl-CoA C-acetyltransferase is an enzyme that catalyzes the chemical reaction
In enzymology, a propionyl-CoA C2-trimethyltridecanoyltransferase is an enzyme that catalyzes the chemical reaction
Propionate kinase is an enzyme with systematic name ATP:propanoate phosphotransferase. This enzyme catalyses the following chemical reaction
Coenzyme A transferases (CoA-transferases) are transferase enzymes that catalyze the transfer of a coenzyme A group from an acyl-CoA donor to a carboxylic acid acceptor. Among other roles, they are responsible for transfer of CoA groups during fermentation and metabolism of ketone bodies. These enzymes are found in all three domains of life.
