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Enzyme nomenclature: https://www.qmul.ac.uk/sbcs/iubmb/enzyme/ http://enzyme.expasy.org/

Name: Systematic: (5Z,8Z,11Z,14Z)-icosa-5,8,11,14-tetraenoate,-donor:

Accepted: prostaglandin-endoperoxidsynthasa

Trivial: cyclooxygenase

Enzyme classification code: EC 1.14.99.1

Enzyme classes:

EC 1.x.x.x EC 2.x.x.x EC 3.x.x.x EC 4.x.x.x EC 5.x.x.x EC 6.x.x.x EC 7.x.x.x

Oxidoreductases: EC 1.x.x.x

Systematic name: donor:acceptor oxidoreductase

Accepted: xxx (oxidation using a coenzyme), xxx oxidase (oxidation by O2, O2 not incorporated into the ), xxx monooxygenase (oxidation by O2, one O of

O2 incorporated into the product), xxx dioxygenase (oxidation by O2, both O of O2 incorporated into the product/s), xxx reductase (can be anything), catalase

(decomposes H2O2 to O2), peroxidases (oxidation of something by H2O2)

Oxidoreductases: EC 1.1.1.1

Systematic: :NAD+ oxidoreductase

Accepted:

Oxidoreductases: EC 1.1.3.4 = oxidase EC 1.1.3.9 = oxidase EC 1.6.1.1 = NAD(P)+ transhydrogenase EC 1.6.3.1 = NAD(P)H oxidase EC 1.9.3.1 = cytochrom-c oxidase EC 1.10.3.2 = laccase EC 1.11.1.6 = katalase EC 1.12.1.2 = hydrogen dehydrogenase EC 1.14.99.1 = cyclooxygenase EC 1.15.1.1 = dismutase EC 1.18.6.1 = nitrogenase

Transferases: EC 2.x.x.x

Systematic name: donor:acceptor grouptransferase

Accepted: xxx (phosphorylate by P from ATP), xxx (usually take a group form activated substrates, such as UDP-glucose), xxx synthase (can be anything), xxx phosphorylase (cleavage by Pi), xxx transaminase ( + oxo-acid <-> amino acid + oxo-acid)

Transferases: EC 2.7.1.86

Systematic name: ATP:NADH 2'-

Accepted: NADH kinase

Tranferases: EC 2.3.3.1 = EC 2.4.1.1 = phosphorylase EC 2.4.1.11 = glykogen synthase EC 2.4.2.4 = thymidine phosphorylase EC 2.6.1.1 = EC 2.7.1.1 = EC 2.7.11.19 = phosphorylase kinase

Hydrolases: EC 3.x.x.x

Systematic name: grouphydrolase

Accepted: xxxase, exo-xxxase (cleave terminal residues), endo-xxxase (cleave in the middle)

Proteases have special nomenclature!

Hydrolases: EC 3.2.1.23

Systematic name: β-D-galactoside galactohydrolase

Accepted: β-galactosidase

Hydrolases: EC 3.1.1.7 = acetylcholineesterase EC 3.1.3.1 = alkaline phosphatase EC 3.1.3.2 = acid phosphatase EC 3.1.3.17 = [phosphorylase]-phosphatase EC 3.1.4.4 = phospholipase C EC 3.1.21.1 = DNase I EC 3.2.1.1 = α-amylase EC 3.2.1.2 = β-amylase EC 3.2.1.4 = cellulase EC 3.2.1.17 = lysozyme EC 3.4.21.1 = chymotrypsin EC 3.4.21.4 = trypsin EC 3.4.21.5 = EC 3.4.22.2 = papain EC 3.5.1.5 = urease EC 3.5.5.1 = nitrilase EC 3.6.1.1 = inorganic diphosphatase

Lyases: EC 4.x.x.x

Systematic name: substrate group-

Accepted: xxx decarboxylase, xxx dehydratase (water elimination), xxx hydratase (water addition), xxx aldolase (aldol condensation), xxx cyclase (e.g. cAMP production), xxx synthase (can be anything)

Lyases: EC 4.1.1.1

Systematic name: pyruvate carboxy-lyase

Accepted:

Lyases: EC 4.1.1.1 = pyruvate decarboxylase EC 4.1.2.13 = fructosebisphosphate aldolase EC 4.2.1.1 = carbonic anhydrase EC 4.2.1.22 = cystathionine-β synthase EC 4.3.2.1 = argininosuccinate lyase EC 4.6.1.1 = adenylate cyclase EC 4.99.1.1 = ferrochelatase

Isomerases: EC 5.x.x.x

Systematic name: depends on sub-class

Sub-classes: racemases, epimerases, aldose-ketose-isomerases, keto-enol-isomerases, -isomerases, and others

Isomerases: EC 5.1.1.1

Systematic and accepted name: alanine racemase

Isomerases: EC 5.1.1.1 = alanine racemase EC 5.3.1.1 = triosaphosphate EC 5.99.1.2 = I EC 5.99.1.3 = topoisomerase II

Ligases: EC 6.x.x.x

Systematic name: substrate1:substrate2 (product forming) (product is ADP, AMP, GMP...)

Accepted: xxx-xxx ligase, xxx synthetase

Ligases: EC 6.1.1.1

Systematic name: L-:tRNATyr ligase (AMP forming)

Accepted: tyrosin-tRNA ligase, tyrosyl-tRNA synthetase

Ligases: EC 6.1.1.1 = tyrosin-tRNA ligase EC 6.2.1.3 = long-chain fatty acid-CoA ligase EC 6.3.1.1 = asparagine synthetase EC 6.4.1.2 = acetyl-CoA carboxylasa EC 6.5.1.1 = DNA-ligase (ATP) EC 6.5.1.2 = DNA-ligase (NAD+)

Translocases (new in 2018): EC 7.x.x.x

Systematic name: original from pre-2018 nomenclature

Translocases (new in 2018): EC 7.1.2.1

Systematic name: ATP phosphohydrolase (H+-exporting)

Accepted name: H+-exporting ATPase

What can go wrong: More complicated reactions:

Citrate synthase: acetyl-CoA + oxalacetate + H2O → citrate + HSCoA lyase? (addition), ? (hydrolysis of C-S bond), transferase? (acetate transfer) From 1962 to 2002: EC 4.1.3.7 Since 2002: EC 2.3.3.1 acetyl-CoA:oxaloacetate C-acetyltransferase [thioester-hydrolysing, (pro-S)-carboxymethyl forming]

Broader substrate specificity: β-galactosidase (β-D-galactoside galactohydrolase, EC 3.2.1.23) lactase (lactose galactohydrolase, EC 3.2.1.108)

More reactions possible: Xanthine dehydrogenase/oxidase + xanthin + NAD + H2O → uric acid + NADH + hypoxanthin + NAD + H2O → xanthin + NADH xanthin + O2 + H2O → uric acid + H2O2 change from dehydrogene to oxidase can be done by disulfide bridge reduction, partial proteolysis, heavy metals, thawing and freezing etc.

What can go wrong: Polymeric substrates: α-Amylase (4-α-D-glucan glucanohydrolase) [ (NADP+)] kinase (ATP:[isocitrate dehydrogenase (NADP+)] phosphotransferase)

Direction of the reaction: Hexokinase (ATP:D-hexose 6-phosphotransferase, EC 2.7.1.1) Glc + ATP → Glc-6-P + ADP (ATP:pyruvate 2-O-phosphotransferase, EC 2.7.1.40) phosphoenolpyruvate + ADP → pyruvate + ATP

Enzyme or multi-enzyme complex? pyruvate dehydrogenasove complex: pyruvate dehydrogenase (E1, EC 1.2.4.1) dihydrolipoyl transacetylase (E2, EC 2.3.1.12) dihydrolipoyl dehydrogenase (E3, EC 1.8.1.4)

Specials: Cyclophilin:

1984 – cyclophilin discovered as a receptor of cyclosporin Handschumacher R.E., Harding M.W., Rice J., Drugge R.J., Speicher D.W. (1984) Science 226, 544-547.

1984 – group of PPIases dicovered Fischer G., Bang H., Mech C. (1984) Biomed. Biochim. Acta. 43, 1101-1111.

1989 – cyclophilin is one of them Fischer G., Wittmann-Liebold B., Lang K., Kiefhaber T., Schmid F.X. (1989) Nature 337, 476-478.

1992 – both activities are more or less independent Zydowsky L.D., Etzkorn F.A., Chang H.Y., Ferguson S.B., Stolz L.A., Ho S.I., Walsh C.T. (1992) Prot. Sci. 1, 1092–1099.