A cofactor is a non-protein chemical compound or metallic ion that is required for an enzyme's role as a catalyst. Cofactors can be considered "helper molecules" that assist in biochemical transformations. The rates at which these happen are characterized in an area of study called enzyme kinetics. Cofactors typically differ from ligands in that they often derive their function by remaining bound.
Enoyl-CoA-(∆) isomerase (EC 5.3.3.8, also known as dodecenoyl-CoA- isomerase, 3,2-trans-enoyl-CoA isomerase, ∆3 ,∆2 -enoyl-CoA isomerase, or acetylene-allene isomerase, is an enzyme that catalyzes the conversion of cis- or trans-double bonds of coenzyme A bound fatty acids at gamma-carbon to trans double bonds at beta-carbon as below:
Ferredoxins are iron–sulfur proteins that mediate electron transfer in a range of metabolic reactions. The term "ferredoxin" was coined by D.C. Wharton of the DuPont Co. and applied to the "iron protein" first purified in 1962 by Mortenson, Valentine, and Carnahan from the anaerobic bacterium Clostridium pasteurianum.
In biochemistry, flavin adenine dinucleotide (FAD) is a redox-active coenzyme associated with various proteins, which is involved with several enzymatic reactions in metabolism. A flavoprotein is a protein that contains a flavin group, which may be in the form of FAD or flavin mononucleotide (FMN). Many flavoproteins are known: components of the succinate dehydrogenase complex, α-ketoglutarate dehydrogenase, and a component of the pyruvate dehydrogenase complex.
Aconitase is an enzyme that catalyses the stereo-specific isomerization of citrate to isocitrate via cis-aconitate in the tricarboxylic acid cycle, a non-redox-active process.
A hydrogenase is an enzyme that catalyses the reversible oxidation of molecular hydrogen (H2), as shown below:
2,4 Dienoyl-CoA reductase also known as DECR1 is an enzyme which in humans is encoded by the DECR1 gene which resides on chromosome 8. This enzyme catalyzes the following reactions
Serine dehydratase or L-serine ammonia lyase (SDH) is in the β-family of pyridoxal phosphate-dependent (PLP) enzymes. SDH is found widely in nature, but its structural and properties vary among species. SDH is found in yeast, bacteria, and the cytoplasm of mammalian hepatocytes. SDH catalyzes is the deamination of L-serine to yield pyruvate, with the release of ammonia.
In enzymology, a 3-hydroxyacyl-CoA dehydrogenase (EC 1.1.1.35) is an enzyme that catalyzes the chemical reaction
In enzymology, a 3-hydroxybutyryl-CoA dehydrogenase (EC 1.1.1.157) is an enzyme that catalyzes the chemical reaction
In enzymology, carbon monoxide dehydrogenase (CODH) (EC 1.2.7.4) is an enzyme that catalyzes the chemical reaction
In enzymology, a pyruvate synthase is an enzyme that catalyzes the interconversion of pyruvate and acetyl-CoA. It is also called pyruvate:ferredoxin oxidoreductase (PFOR).
In enzymology, a CoB—CoM heterodisulfide reductase (EC 1.8.98.1) is an enzyme that catalyzes the chemical reaction
In enzymology, a 3-hydroxybutyryl-CoA epimerase is an enzyme that catalyzes the chemical reaction
In enzymology, a vinylacetyl-CoA Delta-isomerase is an enzyme that catalyzes the chemical reaction
The enzyme 2-methylcitrate dehydratase (EC 4.2.1.79) catalyzes the chemical reaction
The enzyme 3-hydroxybutyryl-CoA dehydratase (EC 4.2.1.55) catalyzes the chemical reaction
In enzymology, a crotonoyl-[acyl-carrier-protein] hydratase (EC 4.2.1.58) is an enzyme that catalyzes the chemical reaction
In enzymology, a citrate (Re)-synthase (EC 2.3.3.3) is an enzyme that catalyzes the chemical reaction
Succinate-semialdehyde dehydrogenase (acylating) (EC 1.2.1.76, succinyl-coA reductase, coenzyme-A-dependent succinate-semialdehyde dehydrogenase) is an enzyme with systematic name succinate semialdehyde:NADP+ oxidoreductase (CoA-acylating). This enzyme catalyses the following chemical reaction
