In biochemistry, isomerases are a general class of enzymes that convert a molecule from one isomer to another. Isomerases facilitate intramolecular rearrangements in which bonds are broken and formed. The general form of such a reaction is as follows:
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:
Substances, mixtures and exposure circumstances in this list have been classified by the International Agency for Research on Cancer (IARC) as group 2B: The agent (mixture) is "possibly carcinogenic to humans". The exposure circumstance entails exposures that are possibly carcinogenic to humans. This category is used for agents, mixtures and exposure circumstances for which there is limited evidence of carcinogenicity in humans and less than sufficient evidence of carcinogenicity in experimental animals. It may also be used when there is inadequate evidence of carcinogenicity in humans but there is sufficient evidence of carcinogenicity in experimental animals. In some instances, an agent, mixture or exposure circumstance for which there is inadequate evidence of carcinogenicity in humans but limited evidence of carcinogenicity in experimental animals together with supporting evidence from other relevant data may be placed in this group. Further details can be found in the preamble to the IARC Monographs.
Prolyl isomerase is an enzyme found in both prokaryotes and eukaryotes that interconverts the cis and trans isomers of peptide bonds with the amino acid proline. Proline has an unusually conformationally restrained peptide bond due to its cyclic structure with its side chain bonded to its secondary amine nitrogen. Most amino acids have a strong energetic preference for the trans peptide bond conformation due to steric hindrance, but proline's unusual structure stabilizes the cis form so that both isomers are populated under biologically relevant conditions. Proteins with prolyl isomerase activity include cyclophilin, FKBPs, and parvulin, although larger proteins can also contain prolyl isomerase domains.
Mannose-6 phosphate isomerase (MPI), alternately phosphomannose isomerase (PMI) is an enzyme which facilitates the interconversion of fructose 6-phosphate (F6P) and mannose-6-phosphate (M6P). Mannose-6-phosphate isomerase may also enable the synthesis of GDP-mannose in eukaryotic organisms. M6P can be converted to F6P by mannose-6-phosphate isomerase and subsequently utilized in several metabolic pathways including glycolysis and capsular polysaccharide biosynthesis. PMI is monomeric and metallodependent on zinc as a cofactor ligand. PMI is inhibited by erythrose 4-phosphate, mannitol 1-phosphate, and to a lesser extent, the alpha anomer of M6P.
In enzymology, a 2-chloro-4-carboxymethylenebut-2-en-1,4-olide isomerase is an enzyme that catalyzes the chemical reaction
In enzymology, an aconitate Δ-isomerase is an enzyme that catalyzes the chemical reaction
In enzymology, a farnesol 2-isomerase is an enzyme that catalyzes the chemical reaction
In enzymology, a linoleate isomerase is an enzyme that catalyzes the chemical reaction
In enzymology, a maleate isomerase, or maleate cis-tran isomerase, is a member of the Asp/Glu racemase superfamily discovered in bacteria. It is responsible for catalyzing cis-trans isomerization of the C2-C3 double bond in maleate to produce fumarate, which is a critical intermediate in citric acid cycle. The presence of an exogenous mercaptan is required for catalysis to happen.
In enzymology, a maleylpyruvate isomerase is an enzyme that catalyzes the chemical reaction
In enzymology, a polyenoic fatty acid isomerase is an enzyme that catalyzes the chemical reaction
Retinal isomerase is an enzyme that catalyzes the isomerisation of all-trans-retinal in the eye into 11-cis-retinal which is the form that most opsins bind.
In enzymology, a retinol isomerase is an enzyme that catalyzes the chemical reaction
In enzymology, a trans-2-decenoyl-[acyl-carrier protein] isomerase is an enzyme that catalyzes the chemical reaction
In enzymology, a vinylacetyl-CoA Delta-isomerase is an enzyme that catalyzes the chemical reaction
ζ-Carotene isomerase is an enzyme with systematic name 9,15,9'-tricis-zeta-carotene cis-trans-isomerase. This enzyme catalyses the following chemical reaction
Prolycopene isomerase is an enzyme with systematic name 7,9,7',9'-tetracis-lycopene cis-trans-isomerase. This enzyme catalyses the following chemical reaction
Beta-carotene isomerase is an enzyme with systematic name beta-carotene 9-cis-all-trans isomerase. This enzyme catalyses the following chemical reaction
