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. ...

, an UDP-galactopyranose 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 ...

that catalyzes the

chemical reaction A chemical reaction is a process that leads to the chemical transformation of one set of chemical substances to another. Classically, chemical reactions encompass changes that only involve the positions of electrons in the forming and breaking ...

:UDP-D-galactopyranose

\rightleftharpoons

UDP-D-galacto-1,4-furanose Hence, this enzyme has one substrate, UDP-D-galactopyranose, and one product, UDP-D-galacto-1,4-furanose. This enzyme belongs to the family of isomerases, specifically those intramolecular

transferase A transferase is any one of a class of enzymes that catalyse the transfer of specific functional groups (e.g. a methyl or glycosyl group) from one molecule (called the donor) to another (called the acceptor). They are involved in hundreds o ...

s transferring other groups. The systematic name of this enzyme class is UDP-D-galactopyranose furanomutase. UDP-D-galactofuranose then serves as an activated sugar donor for the biosynthesis of galactofuranose glycoconjugates. The exocyclic 1,2-diol of galactofuranose is the epitope recognized by the putative chordate immune lectin

intelectin Intelectins are lectins (carbohydrate-binding proteins) expressed in humans and other chordates. Humans express two types of intelectins encoded by ITLN1 and ITLN2 genes respectively. Several intelectins bind microbe-specific carbohydrate res ...

Structural studies

Because UGM is not present in the mammalian systems but is essential among several pathogenic microbes, the enzyme is an attractive antibiotic target. As of late 2007, 5 structures have been solved for this class of enzymes, with PDB accession codes , , , , and .

References

* EC 5.4.99 Enzymes of known structure {{isomerase-stub