Glucuronate Isomerase
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Glucuronate Isomerase
In enzymology, a glucuronate isomerase () is an enzyme that catalysis, catalyzes the chemical reaction :D-glucuronate \rightleftharpoons D-fructuronate Hence, this enzyme has one substrate (biochemistry), substrate, D-glucuronate, and one product (chemistry), product, D-fructuronate. This enzyme belongs to the family of isomerases, specifically those intramolecular oxidoreductases interconverting aldoses and ketoses. The List of enzymes, systematic name of this enzyme class is D-glucuronate aldose-ketose-isomerase. Other names in common use include uronic isomerase, uronate isomerase, D-glucuronate isomerase, uronic acid isomerase, and D-glucuronate ketol-isomerase. This enzyme participates in pentose and glucuronate interconversions. Structural studies As of late 2007, two tertiary structure, structures have been solved for this class of enzymes, with Protein Data Bank, PDB accession codes and . References

* * EC 5.3.1 Enzymes of known structure {{isomerase-st ...
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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. Almost all metabolic processes in the cell need enzyme catalysis in order to occur at rates fast enough to sustain life. Metabolic pathways depend upon enzymes to catalyze individual steps. The study of enzymes is called ''enzymology'' and the field of pseudoenzyme analysis recognizes that during evolution, some enzymes have lost the ability to carry out biological catalysis, which is often reflected in their amino acid sequences and unusual 'pseudocatalytic' properties. Enzymes are known to catalyze more than 5,000 biochemical reaction types. Other biocatalysts are catalytic RNA molecules, called ribozymes. Enzymes' specificity comes from their unique three-dimensional structures. Like all catalysts, enzymes increase the reaction ra ...
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