Enzyme nomenclature and classification: the state of the art

The IUBMB enzyme classification system, available at the IUBMB ExplorEnz website, uses a four‐component number (the EC number) that identifies an enzyme in terms of reaction catalysed. There were originally six recognized groups of enzymes: Oxidoreductases (EC 1), Transferases (EC 2), Hydrolases (EC...

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Veröffentlicht in:The FEBS journal 2023-05, Vol.290 (9), p.2214-2231
Hauptverfasser: McDonald, Andrew G., Tipton, Keith F.
Format: Artikel
Sprache:eng
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Zusammenfassung:The IUBMB enzyme classification system, available at the IUBMB ExplorEnz website, uses a four‐component number (the EC number) that identifies an enzyme in terms of reaction catalysed. There were originally six recognized groups of enzymes: Oxidoreductases (EC 1), Transferases (EC 2), Hydrolases (EC 3), Lyases (EC 4), Isomerases (EC 5) and Ligases (EC 6). Of these, the lyases, which are defined as ‘enzymes that cleave C‐C, C‐O, C‐N and other bonds by means other than by hydrolysis or oxidation’, present particular recognition and classification problems. Recently, a new class, the Translocases (EC 7), has been added, which incorporates enzymes that catalyse the movement of ions or molecules across membranes or their separation within membranes. A new subclass of the isomerases has also been included for those enzymes that alter the conformations of proteins and nucleic acids. Newly reported enzymes are being regularly added to the list after validation and where new information affects the classification of an existing entry, a new EC number is created, but the old one is not reused. The IUBMB Enzyme Classification and Nomenclature System classifies enzymes according to the reactions they catalyse, and is being continuously expanded to include newly characterized enzymes. It included six broad enzyme classes, to which a seventh (EC 7), the Translocases, has now been added. Macromolecular isomerases have been also added as a separate subclass of the isomerases as EC 5.6.
ISSN:1742-464X
1742-4658
DOI:10.1111/febs.16274