NOMENCLATURE AND USEFUL DATA APPENDIX 1

Enzyme Nomenclature APPENDIX 1A

In 1964, the Nomenclature Committee of the International Union of Biochemistry
provided the first set of guidelines on Enzyme Nomenclature that resulted in the well
known “EC” (Enzyme Commission) designation for each enzyme. These guidelines have
been updated in subsequent years. In 1978, enzymes were grouped into six classes
according to the reaction catalyzed (Table A.1A.1). These were then subclassified in terms
of the donors, then acceptors, and then the actual enzyme reaction. Table A.1A.2 shows
an example of the major sub-subclasses of oxidoreductases with examples of the many
hundreds of enzymes in this class.
It is important to note that this classification procedure came into being when there was
little knowledge of enzyme structure and when protein cloning and expression was in its
infancy. As a result, unlike receptor classification, which relies on structure and coupling,
enzymes are classified according to their function.

Table A.1A.1 Enzyme Classification (Dixon and Webb, 1979)

Enzyme class Enzyme action

1. Oxidoreductases Enzymes catalyzing oxido-reductions
2. Transferases Enzymes transferring a group
3. Hydrolases Enzymes catalyzing hydrolysis of various bonds
4. Lyases Enzymes cleaving C-C, C-O, C-N, and other bonds by
means other than hydrolysis or oxidation
5. Isomerases Enzymes catalyzing changes within one molecule
6. Ligases (Synthetases) Enzymes catalyzing the joining of two molecules with
hydrolysis of the pyrophosphate bond of ATP

Table A.1A.2 Classification of Oxidoreductases (Class 1 Enzymes)

Subclass Sub-subclass Specific examples

1.1 Acting on CH-OH groups of 1.1.1 Acceptor—NAD+, NADP+ 1.1.1.1 Alcohol dehydrogenase
donors 1.1.1.108 Carnitine dehydrogenase
1.1.2 Acceptor—cytochrome 1.1.2.2 Mannitol dehydrogenase
1.1.2.3 Lactate dehydrogenase
1.1.3 Acceptor—oxygen 1.1.3.1 Glycollate oxidase
1.1.3.17 Choline oxidase
1.1.99 Other acceptors 1.1.99.1 Choline dehydrogenase
1.2 Acting on aldehyde or oxo 1.2.1 Acceptor—NAD+, NADP+ 1.2.1.1 Formaldehyde dehydrogenase
group of donors 1.2.1.36 Retinal dehydrogenase
1.2.2 Acceptor—cytochrome 1.2.2.2 Pyruvate dehydrogenase
1.2.3 Acceptor—oxygen 1.2.3.3 Pyruvate oxidase
1.2.4 Acceptor—disulfide 1.2.4.2 Oxoglutarate dehydrogenase
1.2.7 Acceptor—iron-sulfur protein 1.2.7.1 Pyruvate synthase
1.2.99 Other acceptors 1.2.99.1 Uracil dehydrogenase
1.3 Acting on CH-CH group of 1.3.1 Acceptor—NAD+, NADP+ 1.3.1.1 Dihydrouracil dehydrogenase
donors 1.3.2 Acceptor—cytochrome 1.3.2.3 Galactonolactone dehydrogenase
1.3.3 Acceptor—oxygen 1.3.3.1 Dihydro-orate oxidase
1.3.7 Acceptor—iron-sulfur protein 1.3.7.1 6-Hydroxynicotinate reductase
1.3.99 Other acceptors 1.3.99.1 Succinate dehydrogenase
continued

Current Protocols in Pharmacology (1998) A.1A.1-A.1A.3 A.1A.1

Copyright © 1998 by John Wiley & Sons, Inc.
 Table A.1A.2 Classification of Oxidoreductases (Class 1 Enzymes), continued

Subclass Sub-subclass Specific examples

1.4 Acting on CH-NH2 group of 1.4.1 Acceptor—NAD+, NADP+ 1.4.1.1 Alanine dehyrogenase
donors 1.4.2 Acceptor—cytochrome 1.4.2.1 Glycine dehydrogenase
1.4.3 Acceptor—oxygen 1.4.3.1 D-Aspartate oxidase
1.4.7 Acceptor—iron-sulfur protein 1.4.7.1 Glutamate synthase
1.4.9 Other acceptors 1.4.99.2 Taurine dehydrogenase
1.5 Acting on CH-NH group of 1.5.1 Acceptor—NAD+, NADP+ 1.5.1.1 Pyrroline-2-carboxylate reductase
donors 1.5.3 Acceptor—oxygen 1.5.3.1 Sarcosine oxidase
1.5.99 Other acceptors 1.5.99.1 Sarcosine dehydrogenase
1.6 Acting on NADH or NADPH 1.6.1 Acceptor—NAD+, NADP+ 1.6.1.1 NAD(P)+ transhydrogenase
1.6.2 Acceptor—cytochrome 1.6.2.1 Cytochrome b5 reductase
1.6.4 Acceptor—disulfide 1.6.4.1 Cystine reductase
1.6.5 Acceptor—quinone 1.6.5.4 Monodehydroascorbate reductase
1.6.6 Acceptor—nitrogenous group 1.6.6.8 GMP reductase
1.6.99 Other acceptors 1.6.99.1 NADPH dehydrogenase
1.7 Acting on other nitrogenous 1.7.2 Acceptor—cytochrome 1.7.2.1 Nitrite reductase
compounds as donors 1.7.3 Acceptor—oxygen 1.7.3.1 Nitroethane oxidase
1.7.7 Acceptor—iron-sulfur protein 1.7.7.1 Ferredoxin-nitrite reductase
1.7.99 Other acceptors 1.7.99.4 Nitrate reductase
1.8 Acting on a sulfur group of 1.8.1 Acceptor—NAD+, NADP+ 1.8.1.1 Sulfite reductase
donors 1.8.2 Acceptor—cytochrome 1.8.2.1 Sulfite dehydrogenase
1.8.3. Acceptor—oxygen 1.8.3.1 Sulfite oxidase
1.8.4 Acceptor—disulfide 1.8.4.2 Protein-disulfide reductase
1.8.5 Acceptor—quinone 1.8.5.1 Glutathione dehydrogenase
1.8.7 Acceptor—iron-sulfur protein 1.8.7.1 Sulfite reductase (ferredoxin)
1.8.99 Other acceptors 1.8.99.1 Sulfite reductase
1.9 Acting on a heme group of 1.9.3 Acceptor—oxygen 1.9.3.1 Cytochrome c oxidase
donors 1.9.6 Acceptor—nitrogenous group 1.9.6.1 Nitrate reductase
1.9.99 Other acceptors 1.9.99.1 Iron–cytochrome c oxidase
1.10 Acting on diphenols and 1.10.1 Acceptor—NAD+, NADP+ 1.10.1.1 trans-Acenaphthene-1,2-diol
related substances as donors dehydrogenase
1.10.2 Acceptor—cytochrome 1.10.2.1 L-Ascorbate–cytochrome b5
oxidase
1.10.3 Acceptor—oxygen 1.10.3.1 Catechol oxidase
1.11 Acting on hydrogen peroxide 1.11.1 Acceptor—NAD+, NADP+ 1.11.1.1 NAD+ peroxidase
as a donor
1.12 Acting on hydrogen as a donor 1.12.1 Acceptor—NAD+, NADP+ 1.12.1.2 Hydrogen dehydrogenase
1.12.2 Acceptor—cytochrome 1.12.2.1 Cytochrome c3 hydrogenase
1.13 Oxygenases 1.13.11 Incorporation of two atoms of 1.13.11.1 Catechol 1,2-dioxygenase
oxygen
1.13.12 Incorporation of one atom of 1.13.12.1 Arginine-2-monooxygenase
oxygen
1.14 Acting on paired donors with 1.14.11 With 2-oxoglutarate as one donor 1.14.11.1 γ-Butyrobetaine, 2-oxoglutarate
the incorporation of molecular and incorporation of one atom of dioxygenase
oxygen oxygen into both donors
1.14.12 With NADH or NADPH as one 1.14.12.1 Anthranilate 1,2-dioxygenase
donor and incorporation of one
atom of oxygen into both donor
1.14.13 With NADH or NADPH as one 1.14.13.1 Salicylate 1-monooxygenase
donor and incorporation of one
atom of oxygen
continued

Enzyme
Nomenclature

A.1A.2
Current Protocols in Pharmacology
Table A.1A.2 Classification of Oxidoreductases (Class 1 Enzymes), continued

Subclass Sub-subclass Specific examples

1.14 Acting on paired donors with the incorporation of molecular
oxygen (continued)
1.14.14 With reduced flavin or 1.14.14.1 Flavoprotein-linked
flavoprotein as one donor and monooxygenase
incorporation of one atom of
oxygen
1.14.15 With a reduced iron-sulfur 1.14.15.1 Camphor-5-monooxygenase
protein as one donor and
incorporation of one atom of
oxygen
1.14.16 With a reduced pteridine as one 1.14.16.2 Tyrosine 3-monooxygenase
donor and incorporation of one
atom of oxygen
1.14.17 With ascorbate as one donor and 1.14.17.1 Dopamine β-monooxygenase
incorporation of one atom of
oxygen
1.14.18 With another compound as one 1.14.18.1 Monophenol monooxygenase
donor and incorporation of one
atom of oxygen
1.14.99 Miscellaneous 1.14.99.1 Prostaglandin synthase
1.15 Acting on superoxide radicals 1.15.1.1 Superoxide dismutase
as acceptor
1.16 Oxidizing metal ions 1.16.1 Ferroxidase
1.17 Acting on -CH2- groups 1.17.1 Acceptor—NAD+, NADP+ 1.17.1.1 CDP-4-keto-6-deoxy-D-glucose
reductase
1.17.4 Acceptor—disulfide 1.17.4.1 Ribonucleoside-diphosphate
reductase
1.18 Acting on reduced ferredoxin 1.18.1 Acceptor—NAD+, NADP+ 1.18.1.1 Ferredoxin-NAD+ reductase
as donor
1.18.2 Acceptor dinitrogen 1.18.2.1 Nitrogenase
1.18.3 Acceptor H+ 1.18.3.1 Hydrogenase
1.19 Acting on reduced flavodoxin 1.19.2 Acceptor dinitrogen 1.19.2.1 Nitrogenase (flavodoxin)
as donor
1.97 Other oxidoreductases 1.97.1.1 Chlorate reductase

LITERATURE CITED
Dixon, M., and Webb, E.C. 1979. Enzymes, 3rd Ed. Academic Press, New York.

Nomenclature
and Useful Data

A.1A.3
Current Protocols in Pharmacology