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Mutase

Protein

Wikipedia contributorsAdapted for Fathomly · View authors
1 min read
Source updated October 20, 2024

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.

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This article is adapted from the Wikipedia article “Mutase”, written by its contributors and licensed under CC BY-SA 4.0. Fathomly has changed the layout, removed citation markers, navigation and maintenance notices, and adjusted punctuation. This adapted version is shared under the same license. For references, see the original article.

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Related topics

Phosphoglucomutase

Phosphoglucomutase is an enzyme that transfers a phosphate group on an α-D-glucose monomer from the 1 to the 6 position in the forward direction or the 6 to the 1 position in the reverse direction.

Methylmalonyl-CoA mutase

Methylmalonyl-CoA mutase, mitochondrial, also known as methylmalonyl-CoA isomerase, is a protein that in humans is encoded by the MMUT gene (previously MUT). This vitamin B12-dependent enzyme catalyzes the isomerization of methylmalonyl-CoA to succinyl-CoA in humans.

Phosphoglycerate mutase

This enzyme is not to be confused with Bisphosphoglycerate mutase which catalyzes the conversion of 1,3-bisphosphoglycerate to 2,3-bisphosphoglycerate. Phosphoglycerate mutase 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.