In consultation with the IUPAC-IUBMB Joint Commission on Biochemical Nomenclature (JCBN)
World Wide Web version prepared by G.P. Moss
School of Biological and Chemical Sciences, Queen Mary University of London,
Mile End Road, London, E1 4NS, UK
This page contains general information on enzyme nomenclature. It includes links to individual documents, and the number of these will increase as more sections of the enzyme list are revised. Links to other relevant databases are provided. It also provides advice on how to suggest new enzymes for listing, or correction of existing entries. There is a list of abbreviations used in the database.
In Enzyme Nomenclature 1992 there was an historical introduction. This web version is slightly edited from that in the book.
Published in Enzyme Nomenclature 1992 [Academic Press, San Diego, California, ISBN 0-12-227164-5 (hardback), 0-12-227165-3 (paperback)] with Supplement 1 (1993), Supplement 2 (1994), Supplement 3 (1995), Supplement 4 (1997) and Supplement 5 (in Eur. J. Biochem. 1994, 223, 1-5; Eur. J. Biochem. 1995, 232, 1-6; Eur. J. Biochem. 1996, 237, 1-5; Eur. J. Biochem. 1997, 250; 1-6, and Eur. J. Biochem. 1999, 264, 610-650; respectively) [Copyright IUBMB].
Each enzyme has recorded at the end details of when first published in Enzyme Nomenclature or when added to the database and its subsequent history.
Web Version of Enzyme Nomenclature
The complete contents of Enzyme Nomenclature, 1992 (plus subsequent supplements and other changes) are listed below in enzyme number order giving just the recommended name. Each entry provides a link to details of that enzyme. Alternatively if looking for a specific reaction used in the classification of enzymes the broad outline defined by the first two numbers are given below. Each of these subclass entries is linked to a location where the category is subdivided to sub-subclasses. These in turn are linked to a list of recommended names for each enzyme in the sub-subclass.
List of Recommended Names for Enzymes
The common names of all listed enzymes are listed below, along with their EC numbers. Where an enzyme has been deleted or transferred to another EC number, this information is also indicated. Each list is linked to either separate entries for each entry or to files with up to 50 enzymes in each file.
Proposed additions and changes to this list are given separately (details below).
Common Names for: List linked to: EC 1.1 to EC 1.3 separate up to 50 EC 1.4 to EC 1.97 separate up to 50 EC 2.1 to EC 2.4.1 separate up to 50 EC 2.4.2 to EC 2.9 separate up to 50 EC 3.1 to EC 3.3 separate up to 50 EC 3.4 to EC 3.12 separate up to 50 EC 4 separate up to 50 EC 5 separate up to 50 EC 6 separate up to 50
Glossary, Reaction pathways and Links to Other Databases
A start has been made in showing the pathways in which enzymes participate. Thus, for example, a link under EC 188.8.131.52 (isopentenyl-diphosphate isomerase) leads to the pathway from mevalonate to terpenes, and links under EC 184.108.40.206 (squalene monooxygenase) and EC 220.127.116.11 (lanosterol synthase) lead to pathways of steroid formation. For other enzymes a glossary entry has been added which may be just a systematic name or a link to a graphic representation. The glossary from Enzyme Nomenclature, 1992 may also be consulted. This has been updated with subsequent glossary entries. Each enzyme entry has links to other databases. For recent entries these may not yet have been implemented on the other datebase. For details on the information provided click here.
Enzyme Supplement 6 to 19 (electronic only)
Six documents listing additions and corrections to previous entries were approved in 2000. These together form Supplement 6.
Five documents were approved in 2001 and form Supplement 7.
Three documents (six files) were approved in 2002 and form Supplement 8.
Three documents (five files) have been approved in 2003 and form Supplement 9.
Three documents have been approved in 2004 and form Supplement 10.
Six documents have been approved in 2005 and form Supplement 11.
Four files have been approved in 2006 and form Supplement 12.
Two files have been approved in 2007 and form Supplement 13.
Eleven files has been approved in 2008 and form Supplement 14.
Seven files have been approved in 2009 and form Supplement 15.
Seven files have been approved in 2010 and form Supplement 16.
Eight files have been approved in 2011 and form Supplement 17.
Five files have been approved in 2012 and form Supplement 18.
Three files have been approved in 2013 and forms Supplement 19.
Minor corrections or changes are listed separately.
The entries are © Copyright to the International Union of Biochemistry and Molecular Biology.
Proposed New Entries and Revised Entries
Proposals for new entries to the Enzyme List and revisions of previously published entries are available from the following file:
New Enzymes (last batch added February 2014)Suggestions and comments should be made to Dr Andrew McDonald (Department of Biochemistry, Trinity College Dublin, Dublin 2, Ireland)
Criteria for inclusion
Before an enzyme can be included in the list direct experimental evidence is required that the proposed enzyme actually catalyses the reaction claimed. Close sequence similarity is not sufficient without evidence for the reaction catalysed, because only a small change in sequence is sufficient to change the activity or specificity of an enzyme. Furthermore, because classification is based solely on the reaction catalysed, there are cases where proteins of very different sequences catalyse the same reaction. The existence of an apparent gap in a biochemical pathway, are not, in themselves, sufficient for classification purposes.
How to suggest new entries and correct existing entries
Information about new enzymes or corrections to existing entries may be reported directly from these web pages or by using the form printed in the back of Enzyme Nomenclature. Advice is available on how to suggest new enzymes for listing, or corrections of existing entries. Comments and suggestions on enzyme classification and nomenclature also may be sent to Dr Andrew McDonald (Department of Biochemistry, Trinity College Dublin, Dublin 2, Ireland)
Rules for the Classification and Nomenclature of Enzymes
In Enzyme Nomenclature 1992 there was a section on general principles; recommended and systematic names; scheme of classification and numbering of enzymes; and rules for classification and nomenclature. This web version is slightly edited from that in the book.
The links are to a list of sub-subclasses which in turn list the enzymes linked to separate files for each enzyme, or to a list as part of a file with up to 50 enzymes per file.
|Subclass||Name||Enzyme file type|
|EC 1.1||Acting on the CH-OH group of donors||sub-subclasses||up to 50|
|EC 1.2||Acting on the aldehyde or oxo group of donors||sub-subclasses||up to 50|
|EC 1.3||Acting on the CH-CH group of donors||sub-subclasses||up to 50|
|EC 1.4||Acting on the CH-NH2 group of donors||sub-subclasses||up to 50|
|EC 1.5||Acting on the CH-NH group of donors||sub-subclasses||up to 50|
|EC 1.6||Acting on NADH or NADPH||sub-subclasses||up to 50|
|EC 1.7||Acting on other nitrogenous compounds as donors||sub-subclasses||up to 50|
|EC 1.8||Acting on a sulfur group of donors||sub-subclasses||up to 50|
|EC 1.9||Acting on a heme group of donors||sub-subclasses||up to 50|
|EC 1.10||Acting on diphenols and related substances as donors||sub-subclasses||up to 50|
|EC 1.11||Acting on a peroxide as acceptor||sub-subclasses||up to 50|
|EC 1.12||Acting on hydrogen as donor||sub-subclasses||up to 50|
|EC 1.13||Acting on single donors with incorporation of molecular oxygen (oxygenases)||sub-subclasses||up to 50|
|EC 1.14||Acting on paired donors, with incorporation or reduction of molecular oxygen||sub-subclasses||up to 50|
|EC 1.15||Acting on superoxide radicals as acceptor||sub-subclasses||up to 50|
|EC 1.16||Oxidising metal ions||sub-subclasses||up to 50|
|EC 1.17||Acting on CH or CH2 groups||sub-subclasses||up to 50|
|EC 1.18||Acting on iron-sulfur proteins as donors||sub-subclasses||up to 50|
|EC 1.19||Acting on reduced flavodoxin as donor||sub-subclasses||up to 50|
|EC 1.20||Acting on phosphorus or arsenic in donors||sub-subclasses||up to 50|
|EC 1.21||Acting on X-H and Y-H to form an X-Y bond||sub-subclasses||up to 50|
|EC 1.22||Acting on halogen in donors||sub-subclasses||up to 50|
|EC 1.23||Reducing C-O-C group as acceptor||sub-subclasses||up to 50|
|EC 1.97||Other oxidoreductases||sub-subclasses||up to 50|
|EC 2.1||Transferring one-carbon groups||sub-subclasses||up to 50|
|EC 2.2||Transferring aldehyde or ketonic groups||sub-subclasses||up to 50|
|EC 2.3||Acyltransferases||sub-subclasses||up to 50|
|EC 2.4||Glycosyltransferases||sub-subclasses||up to 50|
|EC 2.5||Transferring alkyl or aryl groups, other than methyl groups||sub-subclasses||up to 50|
|EC 2.6||Transferring nitrogenous groups||sub-subclasses||up to 50|
|EC 2.7||Transferring phosphorus-containing groups||sub-subclasses||up to 50|
|EC 2.8||Transferring sulfur-containing groups||sub-subclasses||up to 50|
|EC 2.9||Transferring selenium-containing groups||sub-subclasses||up to 50|
|EC 2.10||Transferring molybdenum- or tungsten-containing groups||sub-subclasses||up to 50|
|EC 3.1||Acting on ester bonds||sub-subclasses||up to 50|
|EC 3.2||Glycosylases||sub-subclasses||up to 50|
|EC 3.3||Acting on ether bonds||sub-subclasses||up to 50|
|EC 3.4||Acting on peptide bonds (peptidases)||sub-subclasses||up to 50|
|EC 3.5||Acting on carbon-nitrogen bonds, other than peptide bonds||sub-subclasses||up to 50|
|EC 3.6||Acting on acid anhydrides||sub-subclasses||up to 50|
|EC 3.7||Acting on carbon-carbon bonds||sub-subclasses||up to 50|
|EC 3.8||Acting on halide bonds||sub-subclasses||up to 50|
|EC 3.9||Acting on phosphorus-nitrogen bonds||sub-subclasses||up to 50|
|EC 3.10||Acting on sulfur-nitrogen bonds||sub-subclasses||up to 50|
|EC 3.11||Acting on carbon-phosphorus bonds||sub-subclasses||up to 50|
|EC 3.12||Acting on sulfur-sulfur bonds||sub-subclasses||up to 50|
|EC 3.13||Acting on carbon-sulfur bonds||sub-subclasses||up to 50|
|EC 4.1||Carbon-carbon lyases||sub-subclasses||up to 50|
|EC 4.2||Carbon-oxygen lyases||sub-subclasses||up to 50|
|EC 4.3||Carbon-nitrogen lyases||sub-subclasses||up to 50|
|EC 4.4||Carbon-sulfur lyases||sub-subclasses||up to 50|
|EC 4.5||Carbon-halide lyases||sub-subclasses||up to 50|
|EC 4.6||Phosphorus-oxygen lyases||sub-subclasses||up to 50|
|EC 4.7||Carbon-phosphorus lyases||sub-subclasses||up to 50|
|EC 4.99||Other lyases||sub-subclasses||up to 50|
|EC 5.1||Racemases and epimerases||sub-subclasses||up to 50|
|EC 5.2||cis-trans-Isomerases||sub-subclasses||up to 50|
|EC 5.3||Intramolecular isomerases||sub-subclasses||up to 50|
|EC 5.4||Intramolecular transferases (mutases)||sub-subclasses||up to 50|
|EC 5.5||Intramolecular lyases||sub-subclasses||up to 50|
|EC 5.99||Other isomerases||sub-subclasses||up to 50|
|EC 6.1||Forming carbonoxygen bonds||sub-subclasses||up to 50|
|EC 6.2||Forming carbonsulfur bonds||sub-subclasses||up to 50|
|EC 6.3||Forming carbonnitrogen bonds||sub-subclasses||up to 50|
|EC 6.4||Forming carboncarbon bonds||sub-subclasses||up to 50|
|EC 6.5||Forming phosphoric ester bonds||sub-subclasses||up to 50|
|EC 6.6||Forming nitrogenmetal bonds||sub-subclasses||up to 50|
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