3-(hydroxyamino)phenol mutase

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3-(hydroxyamino)phenol mutase
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EC no. 5.4.4.3
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In enzymology, a 3-(hydroxyamino)phenol mutase (EC 5.4.4.3) is an enzyme that catalyzes the chemical reaction

3-hydroxyaminophenol aminohydroquinone

Hence, this enzyme has one substrate, 3-hydroxyaminophenol, and one product, aminohydroquinone.

This enzyme belongs to the family of isomerases, specifically those intramolecular transferases transferring hydroxy groups. The systematic name of this enzyme class is 3-(hydroxyamino)phenol hydroxymutase. Other names in common use include 3-hydroxylaminophenol mutase, and 3HAP mutase.

Related Research Articles

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:

A mutase is an enzyme of the isomerase class that catalyzes the movement of a functional group from one position to another within the same molecule. In other words, mutases catalyze intramolecular group transfers. Examples of mutases include bisphosphoglycerate mutase, which appears in red blood cells and phosphoglycerate mutase, which is an enzyme integral to glycolysis. In glycolysis, it changes 3-phosphoglycerate to 2-phosphoglycerate by moving a single phosphate group within a single molecule.

<span class="mw-page-title-main">Phosphoglycerate mutase</span> Class of enzymes

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.

<span class="mw-page-title-main">Methylmalonyl-CoA mutase</span> Mammalian protein found in Homo sapiens

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.

<span class="mw-page-title-main">Phosphoribosylaminoimidazole carboxylase</span> Enzyme involved in purine synthesis

The enzyme Phosphoribosylaminoimidazole carboxylase, or AIR carboxylase (EC 4.1.1.21) is involved in nucleotide biosynthesis and in particular in purine biosynthesis. It catalyzes the conversion of 5'-phosphoribosyl-5-aminoimidazole ("AIR") into 5'-phosphoribosyl-4-carboxy-5-aminoimidazole ("CAIR") as described in the reaction:

In enzymology, a berbamunine synthase (EC 1.14.19.66, Formerly EC 1.1.3.34 and EC 1.14.21.3) is an enzyme that catalyzes the chemical reaction

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<span class="mw-page-title-main">Chorismate mutase</span>

In enzymology, chorismate mutase is an enzyme that catalyzes the chemical reaction for the conversion of chorismate to prephenate in the pathway to the production of phenylalanine and tyrosine, also known as the shikimate pathway. Hence, this enzyme has one substrate, chorismate, and one product, prephenate. Chorismate mutase is found at a branch point in the pathway. The enzyme channels the substrate, chorismate to the biosynthesis of tyrosine and phenylalanine and away from tryptophan. Its role in maintaining the balance of these aromatic amino acids in the cell is vital. This is the single known example of a naturally occurring enzyme catalyzing a pericyclic reaction. Chorismate mutase is only found in fungi, bacteria, and higher plants. Some varieties of this protein may use the morpheein model of allosteric regulation.

In enzymology, a (hydroxyamino)benzene mutase is an enzyme that catalyzes the chemical reaction

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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 methylitaconate Δ-isomerase is an enzyme that catalyzes the chemical reaction

<span class="mw-page-title-main">Phosphoacetylglucosamine mutase</span>

In enzymology, a phosphoacetylglucosamine mutase is an enzyme that catalyzes the chemical reaction

<span class="mw-page-title-main">Phosphoenolpyruvate mutase</span> Enzyme

In enzymology, a phosphoenolpyruvate mutase is an enzyme that catalyzes the chemical reaction

<span class="mw-page-title-main">Phosphomannomutase</span>

In enzymology, a phosphomannomutase is an enzyme that catalyzes the chemical reaction

References