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:
Bisphosphoglycerate mutase is an enzyme expressed in erythrocytes and placental cells. It is responsible for the catalytic synthesis of 2,3-Bisphosphoglycerate (2,3-BPG) from 1,3-bisphosphoglycerate. BPGM also has a mutase and a phosphatase function, but these are much less active, in contrast to its glycolytic cousin, phosphoglycerate mutase (PGM), which favors these two functions, but can also catalyze the synthesis of 2,3-BPG to a lesser extent.
Phosphoglycerate mutase (PGM) is any enzyme that catalyzes step 8 of glycolysis - the internal transfer of a phosphate group from C-3 to C-2 which results in the conversion of 3-phosphoglycerate (3PG) to 2-phosphoglycerate (2PG) through a 2,3-bisphosphoglycerate intermediate. These enzymes are categorized into the two distinct classes of either cofactor-dependent (dPGM) or cofactor-independent (iPGM). The dPGM enzyme is composed of approximately 250 amino acids and is found in all vertebrates as well as in some invertebrates, fungi, and bacteria. The iPGM class is found in all plants and algae as well as in some invertebrate, fungi, and Gram-positive bacteria. This class of PGM enzyme shares the same superfamily as alkaline phosphatase.
Methylmalonyl-CoA mutase (EC 5.4.99.2, MCM), mitochondrial, also known as methylmalonyl-CoA isomerase, is a protein that in humans is encoded by the MUT gene. This vitamin B12-dependent enzyme catalyzes the isomerization of methylmalonyl-CoA to succinyl-CoA in humans. Mutations in MUT gene may lead to various types of methylmalonic aciduria.
3β-Hydroxysteroid dehydrogenase/Δ5-4 isomerase (3β-HSD) is an enzyme that catalyzes the biosynthesis of the steroid progesterone from pregnenolone, 17α-hydroxyprogesterone from 17α-hydroxypregnenolone, and androstenedione from dehydroepiandrosterone (DHEA) in the adrenal gland. It is the only enzyme in the adrenal pathway of corticosteroid synthesis that is not a member of the cytochrome P450 family. It is also present in other steroid-producing tissues, including the ovary, testis and placenta. In humans, there are two 3β-HSD isozymes encoded by the HSD3B1 and HSD3B2 genes.
The enzyme 4-hydroxybenzoate 3-monooxygenase, also commonly referred to as para-hydroxybenzoate hydroxylase (PHBH), is a flavoprotein belonging to the family of oxidoreductases. Specifically, it is a hydroxylase, and is one of the most studied enzymes and catalyzes reactions involved in soil detoxification, metabolism, and other biosynthetic processes.
In enzymology, a 2-acetolactate mutase is an enzyme that catalyzes the chemical reaction
In enzymology, a 3-(hydroxyamino)phenol mutase is an enzyme that catalyzes the chemical reaction
In enzymology, a 5-(carboxyamino)imidazole ribonucleotide mutase is an enzyme that catalyzes the chemical reaction
In enzymology, a cycloartenol synthase is an enzyme that catalyzes the chemical reaction
Isochorismate synthase ( EC 5.4.4.2) is an isomerase enzyme that catalyzes the first step in the biosynthesis of vitamin K2 (menaquinone) in Escherichia coli.
In enzymology, a leucine 2,3-aminomutase is an enzyme that catalyzes the chemical reaction
In enzymology, a methylaspartate mutase is an enzyme that catalyzes the chemical reaction
In enzymology, a precorrin-8X methylmutase is an enzyme that catalyzes the chemical reaction
The enzyme 4-hydroxy-2-oxovalerate aldolase catalyzes the chemical reaction
In enzymology, 2-aminomuconate deaminase (EC 3.5.99.5) (also known as amnd) is an enzyme that catalyzes the chemical reaction
Cobalamin biosynthesis is the process by which bacteria and archea make cobalamin, vitamin B12. Many steps are involved in converting aminolevulinic acid via uroporphyrinogen III and adenosylcobyric acid to the final forms in which it is used by enzymes in both the producing organisms and other species, including humans who acquire it through their diet.
Hydroquinone 1,2-dioxygenase (EC 1.13.11.66, hydroquinone dioxygenase) is an enzyme with systematic name benzene-1,4-diol:oxygen 1,2-oxidoreductase (decyclizing). This enzyme catalyses the following chemical reaction
The alpha-D-phosphohexomutases are a large superfamily of enzymes, with members in all three domains of life. Enzymes from this superfamily are ubiquitous in organisms from E. Coli to humans, and catalyze a phosphoryl transfer reaction on a phosphosugar substrate. Four well studied subgroups in the superfamily are:
- Phosphoglucomutase (PGM)
- Phosphoglucomutase/Phosphomannomutase (PGM/PMM)
- Phosphoglucosamine mutase (PNGM)
- Phosphoaceytlglucosamine mutase (PAGM)
Isochorismate pyruvate lyase is an enzyme responsible for catalyzing part of the pathway involved in the formation of salicylic acid. More specifically, IPL will use isochorismate as a substrate and convert it into salicylate and pyruvate. IPL is a PchB enzyme originating from the pchB gene in Pseudomonas aeruginosa.
