enzymology Enzymes () are proteins that act as biological catalysts by accelerating chemical reactions. The molecules upon which enzymes may act are called substrates, and the enzyme converts the substrates into different molecules known as products. A ...

, a phosphoglucosamine mutase () is an

enzyme Enzymes () are proteins that act as biological catalysts by accelerating chemical reactions. The molecules upon which enzymes may act are called substrates, and the enzyme converts the substrates into different molecules known as products. A ...

that

catalyzes Catalysis () is the process of increasing the rate of a chemical reaction by adding a substance known as a catalyst (). Catalysts are not consumed in the reaction and remain unchanged after it. If the reaction is rapid and the catalyst recyc ...

the

chemical reaction A chemical reaction is a process that leads to the IUPAC nomenclature for organic transformations, chemical transformation of one set of chemical substances to another. Classically, chemical reactions encompass changes that only involve the pos ...

:alpha-D-glucosamine 1-phosphate

\rightleftharpoons

D-glucosamine 6-phosphate Hence, this enzyme has one substrate, alpha-D-glucosamine 1-phosphate, and one product,

D-glucosamine 6-phosphate Glucosamine (C6H13NO5) is an amino sugar and a prominent precursor in the biochemical synthesis of glycosylated proteins and lipids. Glucosamine is part of the structure of two polysaccharides, chitosan and chitin. Glucosamine is one of the most ...

. This enzyme belongs to the family of isomerases, specifically the phosphotransferases ( a-D-phosphohexomutases), which transfer phosphate groups within a molecule. The systematic name of this enzyme class is alpha-D-glucosamine 1,6-phosphomutase. This enzyme participates in

aminosugars metabolism In organic chemistry, an amino sugar (or more technically a 2-amino-2-deoxysugar) is a sugar molecule in which a hydroxyl group has been replaced with an amine group. More than 60 amino sugars are known, with one of the most abundant being ''N''- ...

. Crystal structures of two bacterial phosphoglucosamine mutases are known (PDB entries 3I3W and 3PDK), from Francisella tularensis and Bacillus anthracis. Both share a similar dimeric quaternary structure, as well as conserved features of the active site, as found their enzyme superfamily, the a-D-phosphohexomutases.

References

* * * * * EC 5.4.2 Enzymes of unknown structure {{isomerase-stub