Enzyme Commission number
The Enzyme Commission number (EC number) is a numerical classification scheme for enzymes, based on the chemical reactions they catalyze. As a system of enzyme nomenclature, every EC number is associated with a recommended name for the respective enzyme.
Strictly speaking, EC numbers do not specify enzymes, but enzyme-catalyzed reactions. If different enzymes (for instance from different organisms) catalyze the same reaction, then they receive the same EC number. Furthermore, through convergent evolution, completely different protein folds can catalyze an identical reaction and therefore would be assigned an identical EC number (these are called non-homologous isofunctional enzymes, or NISE). By contrast, UniProt identifiers uniquely specify a protein by its amino acid sequence.
Format of number
Every enzyme code consists of the letters “EC” followed by four numbers separated by periods. Those numbers represent a progressively finer classification of the enzyme. Preliminary EC numbers exist and have an ‘n’ as part of the fourth (serial) digit (e.g. EC 3.5.1.n3).
For example, the tripeptide aminopeptidases have the code “EC 18.104.22.168”, whose components indicate the following groups of enzymes:
- EC 3 enzymes are hydrolases (enzymes that use water to break up some other molecule)
- EC 3.4 are hydrolases that act on peptide bonds
- EC 3.4.11 are those hydrolases that cleave off the amino-terminal amino acid from a polypeptide
- EC 22.214.171.124 are those that cleave off the amino-terminal end from a tripeptide
Top level codes
|Class||Reaction catalyzed||Typical reaction||Enzyme example(s) with trivial name|
|To catalyze oxidation/reduction reactions; transfer of H and O atoms or electrons from one substance to another||AH + B → A + BH (reduced)
A + O → AO (oxidized)
|Transfer of a functional group from one substance to another. The group may be methyl-, acyl-, amino- or phosphate group||AB + C → A + BC||Transaminase, kinase|
|Formation of two products from a substrate by hydrolysis||AB + H2O → AOH + BH||Lipase, amylase, peptidase, phosphatase|
|Non-hydrolytic addition or removal of groups from substrates. C-C, C-N, C-O or C-S bonds may be cleaved||RCOCOOH → RCOH + CO2 or [X-A+B-Y] → [A=B + X-Y]||Decarboxylase|
|Intramolecule rearrangement, i.e. isomerization changes within a single molecule||ABC → BCA||Isomerase, mutase|
|Join together two molecules by synthesis of new C-O, C-S, C-N or C-C bonds with simultaneous breakdown of ATP||X + Y + ATP → XY + ADP + Pi||Synthetase|
|Catalyse the movement of ions or molecules across membranes or their separation within membranes||Transporter|
The enzyme nomenclature scheme was developed starting in 1955, when the International Congress of Biochemistry in Brussels set up an Enzyme Commission. The first version was published in 1961. The current sixth edition, published by the International Union of Biochemistry and Molecular Biology in 1992, contains 3196 different enzymes. Supplements 1-4 were published 1993-1999. Subsequent supplements have been published electronically, at the website of the Nomenclature Committee of the International Union of Biochemistry and Molecular Biology. In August 2018, the Enzyme Commission reorganized the nomenclature by adding the top-level EC 7 category describing translocases.
- Webb, E. C. (1992). Enzyme nomenclature 1992: recommendations of the Nomenclature Committee of the International Union of Biochemistry and Molecular Biology on the nomenclature and classification of enzymes. Academic Press. ISBN 978-0-12-227164-9. Archived from the original on 11 July 2017.
- “ENZYME (Enzyme nomenclature database)”. ExPASy. Archived from the original on 21 March 2019. Retrieved 24 April 2019.
- Omelchenko MV, Galperin MY, Wolf YI, Koonin EV (2010). “Non-homologous isofunctional enzymes: a systematic analysis of alternative solutions in enzyme evolution”. Biology Direct. 5 (1): 31. doi:10.1186/1745-6150-5-31. PMC 2876114. PMID 20433725.
- Apweiler R, Bairoch A, Wu CH, Barker WC, Boeckmann B, Ferro S, Gasteiger E, Huang H, Lopez R, Magrane M, Martin MJ, Natale DA, O’Donovan C, Redaschi N, Yeh LS (Jan 2004). “UniProt: the Universal Protein knowledgebase”. Nucleic Acids Research. 32 (Database issue): D115–9. doi:10.1093/nar/gkh131. PMC 308865. PMID 14681372.
- Moss GP. “Recommendations of the Nomenclature Committee”. International Union of Biochemistry and Molecular Biology on the Nomenclature and Classification of Enzymes by the Reactions they Catalyse. Retrieved 2006-03-14.
- Rahman SA, Cuesta SM, Furnham N, Holliday GL, Thornton JM (Feb 2014). “EC-BLAST: a tool to automatically search and compare enzyme reactions”. Nature Methods. 11 (2): 171–174. doi:10.1038/nmeth.2803. PMC 4122987. PMID 24412978.
- Tipton, Keith (August 2018). “Enzyme Nomenclature News: Translocases (EC 7): A new EC Class”. ExplorEnz: the primary source of the IUBMB enzyme list. Archived from the original on 10 September 2018. Retrieved 3 November 2018.
- Enzyme Nomenclature, authoritative website by the Nomenclature Committee of the International Union of Biochemistry and Molecular Biology, maintained by G.P. Moss
- Enzyme nomenclature database — by ExPASy
- List of all EC numbers — by BRENDA
- Browse PDB structures by EC number
- Browse SCOP domains by EC number — by dcGO
- Compare EC numbers using EC-Blast