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DLKcat/DeeplearningApproach/Data/EC_enzyme/enzclass.txt
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1 |
+
---------------------------------------------------------------------------
|
2 |
+
ENZYME nomenclature database
|
3 |
+
SIB Swiss Institute of Bioinformatics; Geneva, Switzerland
|
4 |
+
---------------------------------------------------------------------------
|
5 |
+
|
6 |
+
Description: ENZYME class hierarchy
|
7 |
+
Name: enzclass.txt
|
8 |
+
Release: 17-Jun-2020
|
9 |
+
|
10 |
+
---------------------------------------------------------------------------
|
11 |
+
|
12 |
+
1. -. -.- Oxidoreductases.
|
13 |
+
1. 1. -.- Acting on the CH-OH group of donors.
|
14 |
+
1. 1. 1.- With NAD(+) or NADP(+) as acceptor.
|
15 |
+
1. 1. 2.- With a cytochrome as acceptor.
|
16 |
+
1. 1. 3.- With oxygen as acceptor.
|
17 |
+
1. 1. 4.- With a disulfide as acceptor.
|
18 |
+
1. 1. 5.- With a quinone or similar compound as acceptor.
|
19 |
+
1. 1. 9.- With a copper protein as acceptor.
|
20 |
+
1. 1.98.- With other, known, acceptors.
|
21 |
+
1. 1.99.- With other acceptors.
|
22 |
+
1. 2. -.- Acting on the aldehyde or oxo group of donors.
|
23 |
+
1. 2. 1.- With NAD(+) or NADP(+) as acceptor.
|
24 |
+
1. 2. 2.- With a cytochrome as acceptor.
|
25 |
+
1. 2. 3.- With oxygen as acceptor.
|
26 |
+
1. 2. 4.- With a disulfide as acceptor.
|
27 |
+
1. 2. 5.- With a quinone or similar compound as acceptor.
|
28 |
+
1. 2. 7.- With an iron-sulfur protein as acceptor.
|
29 |
+
1. 2.98.- With other, known, acceptors.
|
30 |
+
1. 2.99.- With other acceptors.
|
31 |
+
1. 3. -.- Acting on the CH-CH group of donors.
|
32 |
+
1. 3. 1.- With NAD(+) or NADP(+) as acceptor.
|
33 |
+
1. 3. 2.- With a cytochrome as acceptor.
|
34 |
+
1. 3. 3.- With oxygen as acceptor.
|
35 |
+
1. 3. 4.- With a disulfide as acceptor.
|
36 |
+
1. 3. 5.- With a quinone or related compound as acceptor.
|
37 |
+
1. 3. 7.- With an iron-sulfur protein as acceptor.
|
38 |
+
1. 3. 8.- With a flavin as acceptor.
|
39 |
+
1. 3.98.- With other, known, acceptors.
|
40 |
+
1. 3.99.- With other acceptors.
|
41 |
+
1. 4. -.- Acting on the CH-NH(2) group of donors.
|
42 |
+
1. 4. 1.- With NAD(+) or NADP(+) as acceptor.
|
43 |
+
1. 4. 2.- With a cytochrome as acceptor.
|
44 |
+
1. 4. 3.- With oxygen as acceptor.
|
45 |
+
1. 4. 4.- With a disulfide as acceptor.
|
46 |
+
1. 4. 5.- With a quinone or similar compound as acceptor.
|
47 |
+
1. 4. 7.- With an iron-sulfur protein as acceptor.
|
48 |
+
1. 4. 9.- With a copper protein as acceptor.
|
49 |
+
1. 4.98.- With other, known, acceptors.
|
50 |
+
1. 4.99.- With other acceptors.
|
51 |
+
1. 5. -.- Acting on the CH-NH group of donors.
|
52 |
+
1. 5. 1.- With NAD(+) or NADP(+) as acceptor.
|
53 |
+
1. 5. 3.- With oxygen as acceptor.
|
54 |
+
1. 5. 4.- With a disulfide as acceptor.
|
55 |
+
1. 5. 5.- With a quinone or similar compound as acceptor.
|
56 |
+
1. 5. 7.- With an iron-sulfur protein as acceptor.
|
57 |
+
1. 5. 8.- With a flavin as acceptor.
|
58 |
+
1. 5.98.- With other, known, acceptors.
|
59 |
+
1. 5.99.- With other acceptors.
|
60 |
+
1. 6. -.- Acting on NADH or NADPH.
|
61 |
+
1. 6. 1.- With NAD(+) or NADP(+) as acceptor.
|
62 |
+
1. 6. 2.- With a heme protein as acceptor.
|
63 |
+
1. 6. 3.- With oxygen as acceptor.
|
64 |
+
1. 6. 4.- With a disulfide as acceptor.
|
65 |
+
1. 6. 5.- With a quinone or similar compound as acceptor.
|
66 |
+
1. 6. 6.- With a nitrogenous group as acceptor.
|
67 |
+
1. 6. 7.- With a iron-sulfur protein as acceptor.
|
68 |
+
1. 6. 8.- With a flavin as acceptor.
|
69 |
+
1. 6.99.- With other acceptors.
|
70 |
+
1. 7. -.- Acting on other nitrogenous compounds as donors.
|
71 |
+
1. 7. 1.- With NAD(+) or NADP(+) as acceptor.
|
72 |
+
1. 7. 2.- With a cytochrome as acceptor.
|
73 |
+
1. 7. 3.- With oxygen as acceptor.
|
74 |
+
1. 7. 5.- With a quinone or similar compound as acceptor.
|
75 |
+
1. 7. 6.- With a nitrogenous group as acceptor.
|
76 |
+
1. 7. 7.- With an iron-sulfur protein as acceptor.
|
77 |
+
1. 7. 9.- With a copper protein as acceptor.
|
78 |
+
1. 7.99.- With other acceptors.
|
79 |
+
1. 8. -.- Acting on a sulfur group of donors.
|
80 |
+
1. 8. 1.- With NAD(+) or NADP(+) as acceptor.
|
81 |
+
1. 8. 2.- With a cytochrome as acceptor.
|
82 |
+
1. 8. 3.- With oxygen as acceptor.
|
83 |
+
1. 8. 4.- With a disulfide as acceptor.
|
84 |
+
1. 8. 5.- With a quinone or similar compound as acceptor.
|
85 |
+
1. 8. 6.- With an nitrogenous group as acceptor.
|
86 |
+
1. 8. 7.- With an iron-sulfur protein as acceptor.
|
87 |
+
1. 8.98.- With other, known, acceptors.
|
88 |
+
1. 8.99.- With other acceptors.
|
89 |
+
1. 9. -.- Acting on a heme group of donors.
|
90 |
+
1. 9. 3.- With oxygen as acceptor.
|
91 |
+
1. 9. 6.- With a nitrogenous group as acceptor.
|
92 |
+
1. 9.98.- With other, known, acceptors.
|
93 |
+
1. 9.99.- With other acceptors.
|
94 |
+
1.10. -.- Acting on diphenols and related substances as donors.
|
95 |
+
1.10. 1.- With NAD(+) or NADP(+) as acceptor.
|
96 |
+
1.10. 2.- With a cytochrome as acceptor.
|
97 |
+
1.10. 3.- With oxygen as acceptor.
|
98 |
+
1.10. 5.- With a quinone or related compound as acceptor.
|
99 |
+
1.10. 9.- With a copper protein as acceptor.
|
100 |
+
1.10.98.- With other, known, acceptors.
|
101 |
+
1.10.99.- With other acceptors.
|
102 |
+
1.11. -.- Acting on a peroxide as acceptor.
|
103 |
+
1.11. 1.- Peroxidases.
|
104 |
+
1.11. 2.- With H(2)O(2) as acceptor, one oxygen atom of which is incorporated into the product.
|
105 |
+
1.12. -.- Acting on hydrogen as donors.
|
106 |
+
1.12. 1.- With NAD(+) or NADP(+) as acceptor.
|
107 |
+
1.12. 2.- With a cytochrome as acceptor.
|
108 |
+
1.12. 5.- With a quinone or similar compound as acceptor.
|
109 |
+
1.12. 7.- With an iron-sulfur protein as acceptor.
|
110 |
+
1.12.98.- With other, known, acceptors.
|
111 |
+
1.12.99.- With other acceptors.
|
112 |
+
1.13. -.- Acting on single donors with incorporation of molecular oxygen (oxygenases). The oxygen incorporated need not be derived from O(2).
|
113 |
+
1.13. 1.- With NADH or NADPH as one donor.
|
114 |
+
1.13.11.- With incorporation of two atoms of oxygen.
|
115 |
+
1.13.12.- With incorporation of one atom of oxygen (internal monooxygenases or internal mixed function oxidases).
|
116 |
+
1.13.99.- Miscellaneous.
|
117 |
+
1.14. -.- Acting on paired donors, with incorporation or reduction of molecular oxygen. The oxygen incorporated need not be derived from O(2).
|
118 |
+
1.14. 1.- With NADH or NADPH as one donor.
|
119 |
+
1.14. 2.- With ascorbate as one donor.
|
120 |
+
1.14. 3.- With reduced pteridine as one donor.
|
121 |
+
1.14.11.- With 2-oxoglutarate as one donor, and incorporation of one atom each of oxygen into both donors.
|
122 |
+
1.14.12.- With NADH or NADPH as one donor, and incorporation of two atoms of oxygen into one donor.
|
123 |
+
1.14.13.- With NADH or NADPH as one donor, and incorporation of one atom of oxygen.
|
124 |
+
1.14.14.- With reduced flavin or flavoprotein as one donor, and incorporation of one atom of oxygen.
|
125 |
+
1.14.15.- With reduced iron-sulfur protein as one donor, and incorporation of one atom of oxygen.
|
126 |
+
1.14.16.- With reduced pteridine as one donor, and incorporation of one atom of oxygen.
|
127 |
+
1.14.17.- With reduced ascorbate as one donor, and incorporation of one atom of oxygen.
|
128 |
+
1.14.18.- With another compound as one donor, and incorporation of one atom of oxygen.
|
129 |
+
1.14.19.- With oxidation of a pair of donors resulting in the reduction of molecular oxygen to two molecules of water.
|
130 |
+
1.14.20.- With 2-oxoglutarate as one donor, and the other dehydrogenated.
|
131 |
+
1.14.21.- With NADH or NADPH as one donor, and the other dehydrogenated.
|
132 |
+
1.14.99.- Miscellaneous.
|
133 |
+
1.15. -.- Acting on superoxide as acceptor.
|
134 |
+
1.15. 1.- Acting on superoxide as acceptor.
|
135 |
+
1.16. -.- Oxidizing metal ions.
|
136 |
+
1.16. 1.- With NAD(+) or NADP(+) as acceptor.
|
137 |
+
1.16. 3.- With oxygen as acceptor.
|
138 |
+
1.16. 5.- With a quinone or similar compound as acceptor.
|
139 |
+
1.16. 8.- With a flavin as acceptor.
|
140 |
+
1.16. 9.- With a copper protein as acceptor.
|
141 |
+
1.16.98.- With other known acceptors.
|
142 |
+
1.17. -.- Acting on CH or CH(2) groups.
|
143 |
+
1.17. 1.- With NAD(+) or NADP(+) as acceptor.
|
144 |
+
1.17. 2.- With a cytochrome as acceptor.
|
145 |
+
1.17. 3.- With oxygen as acceptor.
|
146 |
+
1.17. 4.- With a disulfide as acceptor.
|
147 |
+
1.17. 5.- With a quinone or similar compound as acceptor.
|
148 |
+
1.17. 7.- With an iron-sulfur protein as acceptor.
|
149 |
+
1.17. 8.- With a flavin as acceptor.
|
150 |
+
1.17. 9.- With a copper protein as acceptor.
|
151 |
+
1.17.98.- With other, known, acceptors.
|
152 |
+
1.17.99.- With other acceptors.
|
153 |
+
1.18. -.- Acting on iron-sulfur proteins as donors.
|
154 |
+
1.18. 1.- With NAD(+) or NADP(+) as acceptor.
|
155 |
+
1.18. 2.- With dinitrogen as acceptor.
|
156 |
+
1.18. 3.- With H(+) as acceptor.
|
157 |
+
1.18. 6.- With dinitrogen as acceptor.
|
158 |
+
1.18.96.- With other, known, acceptors.
|
159 |
+
1.18.99.- With H(+) as acceptor.
|
160 |
+
1.19. -.- Acting on reduced flavodoxin as donor.
|
161 |
+
1.19. 1.- With NAD(+) or NADP(+) as acceptor.
|
162 |
+
1.19. 6.- With dinitrogen as acceptor.
|
163 |
+
1.20. -.- Acting on phosphorus or arsenic in donors.
|
164 |
+
1.20. 1.- With NAD(+) or NADP(+) as acceptor.
|
165 |
+
1.20. 2.- With a cytochrome as acceptor.
|
166 |
+
1.20. 4.- With disulfide as acceptor.
|
167 |
+
1.20. 9.- With a copper protein as acceptor.
|
168 |
+
1.20.98.- With other, known acceptors.
|
169 |
+
1.20.99.- With other acceptors.
|
170 |
+
1.21. -.- Catalyzing the reaction X-H + Y-H = 'X-Y'.
|
171 |
+
1.21. 1.- With NAD(+) or NADP(+) as acceptor.
|
172 |
+
1.21. 3.- With oxygen as acceptor.
|
173 |
+
1.21. 4.- With a disulfide as acceptor.
|
174 |
+
1.21.98.- With other, known acceptors.
|
175 |
+
1.21.99.- With other acceptors.
|
176 |
+
1.22. -.- Acting on halogen in donors.
|
177 |
+
1.22. 1.- With NAD(+) or NADP(+) as acceptor.
|
178 |
+
1.23. -.- Reducing C-O-C group as acceptor.
|
179 |
+
1.23. 1.- With NADH or NADPH as donor.
|
180 |
+
1.23. 5.- With a quinone or similar compound as acceptor.
|
181 |
+
1.97. -.- Other oxidoreductases.
|
182 |
+
1.97. 1.- Other oxidoreductases.
|
183 |
+
1.98. -.- Enzymes using H(2) as reductant.
|
184 |
+
1.98. 1.- Other oxidoreductases.
|
185 |
+
1.99. -.- Other enzymes using O(2) as oxidant.
|
186 |
+
1.99. 1.- Hydroxylases.
|
187 |
+
1.99. 2.- Oxygenases.
|
188 |
+
|
189 |
+
2. -. -.- Transferases.
|
190 |
+
2. 1. -.- Transferring one-carbon groups.
|
191 |
+
2. 1. 1.- Methyltransferases.
|
192 |
+
2. 1. 2.- Hydroxymethyl-, formyl- and related transferases.
|
193 |
+
2. 1. 3.- Carboxy- and carbamoyltransferases.
|
194 |
+
2. 1. 4.- Amidinotransferases.
|
195 |
+
2. 1. 5.- Methylenetransferases.
|
196 |
+
2. 2. -.- Transferring aldehyde or ketonic groups.
|
197 |
+
2. 2. 1.- Transketolases and transaldolases.
|
198 |
+
2. 3. -.- Acyltransferases.
|
199 |
+
2. 3. 1.- Transferring groups other than amino-acyl groups.
|
200 |
+
2. 3. 2.- Aminoacyltransferases.
|
201 |
+
2. 3. 3.- Acyl groups converted into alkyl groups on transfer.
|
202 |
+
2. 4. -.- Glycosyltransferases.
|
203 |
+
2. 4. 1.- Hexosyltransferases.
|
204 |
+
2. 4. 2.- Pentosyltransferases.
|
205 |
+
2. 4.99.- Transferring other glycosyl groups.
|
206 |
+
2. 5. -.- Transferring alkyl or aryl groups, other than methyl groups.
|
207 |
+
2. 5. 1.- Transferring alkyl or aryl groups, other than methyl groups.
|
208 |
+
2. 6. -.- Transferring nitrogenous groups.
|
209 |
+
2. 6. 1.- Transaminases.
|
210 |
+
2. 6. 2.- Amidinotransferases.
|
211 |
+
2. 6. 3.- Oximinotransferases.
|
212 |
+
2. 6.99.- Transferring other nitrogenous groups.
|
213 |
+
2. 7. -.- Transferring phosphorus-containing groups.
|
214 |
+
2. 7. 1.- Phosphotransferases with an alcohol group as acceptor.
|
215 |
+
2. 7. 2.- Phosphotransferases with a carboxy group as acceptor.
|
216 |
+
2. 7. 3.- Phosphotransferases with a nitrogenous group as acceptor.
|
217 |
+
2. 7. 4.- Phosphotransferases with a phosphate group as acceptor.
|
218 |
+
2. 7. 5.- Phosphotransferases with regeneration of donors, apparently catalyzing intramolecular transfers.
|
219 |
+
2. 7. 6.- Diphosphotransferases.
|
220 |
+
2. 7. 7.- Nucleotidyltransferases.
|
221 |
+
2. 7. 8.- Transferases for other substituted phosphate groups.
|
222 |
+
2. 7. 9.- Phosphotransferases with paired acceptors.
|
223 |
+
2. 7.10.- Protein-tyrosine kinases.
|
224 |
+
2. 7.11.- Protein-serine/threonine kinases.
|
225 |
+
2. 7.12.- Dual-specificity kinases (those acting on Ser/Thr and Tyr residues).
|
226 |
+
2. 7.13.- Protein-histidine kinases.
|
227 |
+
2. 7.14.- Protein-arginine kinases.
|
228 |
+
2. 7.99.- Other protein kinases.
|
229 |
+
2. 8. -.- Transferring sulfur-containing groups.
|
230 |
+
2. 8. 1.- Sulfurtransferases.
|
231 |
+
2. 8. 2.- Sulfotransferases.
|
232 |
+
2. 8. 3.- CoA-transferases.
|
233 |
+
2. 8. 4.- Transferring alkylthio groups.
|
234 |
+
2. 8. 5.- Thiosulfotransferases.
|
235 |
+
2. 9. -.- Transferring selenium-containing groups.
|
236 |
+
2. 9. 1.- Selenotransferases.
|
237 |
+
2.10. -.- Transferring molybdenum- or tungsten-containing groups.
|
238 |
+
2.10. 1.- Molybdenumtransferases or tungstentransferases with sulfide groups as acceptors.
|
239 |
+
|
240 |
+
3. -. -.- Hydrolases.
|
241 |
+
3. 1. -.- Acting on ester bonds.
|
242 |
+
3. 1. 1.- Carboxylic ester hydrolases.
|
243 |
+
3. 1. 2.- Thiolester hydrolases.
|
244 |
+
3. 1. 3.- Phosphoric monoester hydrolases.
|
245 |
+
3. 1. 4.- Phosphoric diester hydrolases.
|
246 |
+
3. 1. 5.- Triphosphoric monoester hydrolases.
|
247 |
+
3. 1. 6.- Sulfuric ester hydrolases.
|
248 |
+
3. 1. 7.- Diphosphoric monoester hydrolases.
|
249 |
+
3. 1. 8.- Phosphoric triester hydrolases.
|
250 |
+
3. 1.11.- Exodeoxyribonucleases producing 5'-phosphomonoesters.
|
251 |
+
3. 1.12.- Exodeoxyribonucleases producing 3'-phosphomonoesters.
|
252 |
+
3. 1.13.- Exoribonucleases producing 5'-phosphomonoesters.
|
253 |
+
3. 1.14.- Exoribonucleases producing 3'-phosphomonoesters.
|
254 |
+
3. 1.15.- Exonucleases active with either ribo- or deoxyribonucleic acids and producing 5'-phosphomonoesters.
|
255 |
+
3. 1.16.- Exonucleases active with either ribo- or deoxyribonucleic acids and producing 3'-phosphomonoesters.
|
256 |
+
3. 1.21.- Endodeoxyribonucleases producing 5'-phosphomonoesters.
|
257 |
+
3. 1.22.- Endodeoxyribonucleases producing other than 5'-phosphomonoesters.
|
258 |
+
3. 1.23.- Site specific endodeoxyribonucleases: cleavage is sequence specific.
|
259 |
+
3. 1.24.- Site specific endodeoxyribonucleases: cleavage is not sequence specific.
|
260 |
+
3. 1.25.- Site-specific endodeoxyribonucleases specific for altered bases.
|
261 |
+
3. 1.26.- Endoribonucleases producing 5'-phosphomonoesters.
|
262 |
+
3. 1.27.- Endoribonucleases producing other than 5'-phosphomonoesters.
|
263 |
+
3. 1.30.- Endoribonucleases active with either ribo- or deoxyribonucleic acids and producing 5'-phosphomonoesters.
|
264 |
+
3. 1.31.- Endoribonucleases active with either ribo- or deoxyribonucleic acids and producing 3'-phosphomonoesters.
|
265 |
+
3. 2. -.- Glycosylases.
|
266 |
+
3. 2. 1.- Glycosidases, i.e. enzymes hydrolyzing O- and S-glycosyl compounds.
|
267 |
+
3. 2. 2.- Hydrolyzing N-glycosyl compounds.
|
268 |
+
3. 2. 3.- Hydrolyzing S-glycosyl compounds.
|
269 |
+
3. 3. -.- Acting on ether bonds.
|
270 |
+
3. 3. 1.- Thioether and trialkylsulfonium hydrolases.
|
271 |
+
3. 3. 2.- Ether hydrolases.
|
272 |
+
3. 4. -.- Acting on peptide bonds (peptidases).
|
273 |
+
3. 4. 1.- alpha-Amino-acyl-peptide hydrolases.
|
274 |
+
3. 4. 2.- Peptidyl-amino-acid hydrolases.
|
275 |
+
3. 4. 3.- Dipeptide hydrolases.
|
276 |
+
3. 4. 4.- Peptidyl peptide hydrolases.
|
277 |
+
3. 4.11.- Aminopeptidases.
|
278 |
+
3. 4.12.- Peptidylamino-acid hydrolases or acylamino-acid hydrolases.
|
279 |
+
3. 4.13.- Dipeptidases.
|
280 |
+
3. 4.14.- Dipeptidyl-peptidases and tripeptidyl-peptidases.
|
281 |
+
3. 4.15.- Peptidyl-dipeptidases.
|
282 |
+
3. 4.16.- Serine-type carboxypeptidases.
|
283 |
+
3. 4.17.- Metallocarboxypeptidases.
|
284 |
+
3. 4.18.- Cysteine-type carboxypeptidases.
|
285 |
+
3. 4.19.- Omega peptidases.
|
286 |
+
3. 4.21.- Serine endopeptidases.
|
287 |
+
3. 4.22.- Cysteine endopeptidases.
|
288 |
+
3. 4.23.- Aspartic endopeptidases.
|
289 |
+
3. 4.24.- Metalloendopeptidases.
|
290 |
+
3. 4.25.- Threonine endopeptidases.
|
291 |
+
3. 4.99.- Endopeptidases of unknown catalytic mechanism.
|
292 |
+
3. 5. -.- Acting on carbon-nitrogen bonds, other than peptide bonds.
|
293 |
+
3. 5. 1.- In linear amides.
|
294 |
+
3. 5. 2.- In cyclic amides.
|
295 |
+
3. 5. 3.- In linear amidines.
|
296 |
+
3. 5. 4.- In cyclic amidines.
|
297 |
+
3. 5. 5.- In nitriles.
|
298 |
+
3. 5.99.- In other compounds.
|
299 |
+
3. 6. -.- Acting on acid anhydrides.
|
300 |
+
3. 6. 1.- In phosphorus-containing anhydrides.
|
301 |
+
3. 6. 2.- In sulfonyl-containing anhydrides.
|
302 |
+
3. 6. 3.- Acting on acid anhydrides; catalyzing transmembrane movement of substances.
|
303 |
+
3. 6. 4.- Acting on ATP; involved in cellular and subcellular movement.
|
304 |
+
3. 6. 5.- Acting on GTP; involved in cellular and subcellular movement.
|
305 |
+
3. 7. -.- Acting on carbon-carbon bonds.
|
306 |
+
3. 7. 1.- In ketonic substances.
|
307 |
+
3. 8. -.- Acting on halide bonds.
|
308 |
+
3. 8. 1.- In C-halide compounds.
|
309 |
+
3. 8. 2.- In P-halide compounds.
|
310 |
+
3. 9. -.- Acting on phosphorus-nitrogen bonds.
|
311 |
+
3. 9. 1.- Acting on phosphorus-nitrogen bonds.
|
312 |
+
3.10. -.- Acting on sulfur-nitrogen bonds.
|
313 |
+
3.10. 1.- Acting on sulfur-nitrogen bonds.
|
314 |
+
3.11. -.- Acting on carbon-phosphorus bonds.
|
315 |
+
3.11. 1.- Acting on carbon-phosphorus bonds.
|
316 |
+
3.12. -.- Acting on sulfur-sulfur bonds.
|
317 |
+
3.12. 1.- Acting on sulfur-sulfur bonds.
|
318 |
+
3.13. -.- Acting on carbon-sulfur bonds.
|
319 |
+
3.13. 1.- Acting on carbon-sulfur bonds.
|
320 |
+
|
321 |
+
4. -. -.- Lyases.
|
322 |
+
4. 1. -.- Carbon-carbon lyases.
|
323 |
+
4. 1. 1.- Carboxy-lyases.
|
324 |
+
4. 1. 2.- Aldehyde-lyases.
|
325 |
+
4. 1. 3.- Oxo-acid-lyases.
|
326 |
+
4. 1.99.- Other carbon-carbon lyases.
|
327 |
+
4. 2. -.- Carbon-oxygen lyases.
|
328 |
+
4. 2. 1.- Hydro-lyases.
|
329 |
+
4. 2. 2.- Acting on polysaccharides.
|
330 |
+
4. 2. 3.- Acting on phosphates.
|
331 |
+
4. 2.99.- Other carbon-oxygen lyases.
|
332 |
+
4. 3. -.- Carbon-nitrogen lyases.
|
333 |
+
4. 3. 1.- Ammonia-lyases.
|
334 |
+
4. 3. 2.- Lyases acting on amides, amidines, etc.
|
335 |
+
4. 3. 3.- Amine-lyases.
|
336 |
+
4. 3.99.- Other carbon-nitrogen lyases.
|
337 |
+
4. 4. -.- Carbon-sulfur lyases.
|
338 |
+
4. 4. 1.- Carbon-sulfur lyases.
|
339 |
+
4. 5. -.- Carbon-halide lyases.
|
340 |
+
4. 5. 1.- Carbon-halide lyases.
|
341 |
+
4. 6. -.- Phosphorus-oxygen lyases.
|
342 |
+
4. 6. 1.- Phosphorus-oxygen lyases.
|
343 |
+
4. 7. -.- Carbon-phosphorus lyases.
|
344 |
+
4. 7. 1.- Carbon-phosphorus lyases.
|
345 |
+
4.99. -.- Other lyases.
|
346 |
+
4.99. 1.- Other lyases.
|
347 |
+
|
348 |
+
5. -. -.- Isomerases.
|
349 |
+
5. 1. -.- Racemases and epimerases.
|
350 |
+
5. 1. 1.- Acting on amino acids and derivatives.
|
351 |
+
5. 1. 2.- Acting on hydroxy acids and derivatives.
|
352 |
+
5. 1. 3.- Acting on carbohydrates and derivatives.
|
353 |
+
5. 1.99.- Acting on other compounds.
|
354 |
+
5. 2. -.- Cis-trans-isomerases.
|
355 |
+
5. 2. 1.- Cis-trans isomerases.
|
356 |
+
5. 3. -.- Intramolecular oxidoreductases.
|
357 |
+
5. 3. 1.- Interconverting aldoses and ketoses.
|
358 |
+
5. 3. 2.- Interconverting keto- and enol-groups.
|
359 |
+
5. 3. 3.- Transposing C=C bonds.
|
360 |
+
5. 3. 4.- Transposing S-S bonds.
|
361 |
+
5. 3.99.- Other intramolecular oxidoreductases.
|
362 |
+
5. 4. -.- Intramolecular transferases.
|
363 |
+
5. 4. 1.- Transferring acyl groups.
|
364 |
+
5. 4. 2.- Phosphotransferases (phosphomutases).
|
365 |
+
5. 4. 3.- Transferring amino groups.
|
366 |
+
5. 4. 4.- Transferring hydroxy groups.
|
367 |
+
5. 4.99.- Transferring other groups.
|
368 |
+
5. 5. -.- Intramolecular lyases.
|
369 |
+
5. 5. 1.- Intramolecular lyases.
|
370 |
+
5. 6. -.- Isomerases altering macromolecular conformation.
|
371 |
+
5. 6. 1.- Enzymes altering polypeptide conformation or assembly.
|
372 |
+
5. 6. 2.- Enzymes altering nucleic acid conformation.
|
373 |
+
5.99. -.- Other isomerases.
|
374 |
+
5.99. 1.- Other isomerases.
|
375 |
+
|
376 |
+
6. -. -.- Ligases.
|
377 |
+
6. 1. -.- Forming carbon-oxygen bonds.
|
378 |
+
6. 1. 1.- Ligases forming aminoacyl-tRNA and related compounds.
|
379 |
+
6. 1. 2.- Acid--alcohol ligases (ester synthases).
|
380 |
+
6. 1. 3.- Cyclo-ligases.
|
381 |
+
6. 2. -.- Forming carbon-sulfur bonds.
|
382 |
+
6. 2. 1.- Acid--thiol ligases.
|
383 |
+
6. 3. -.- Forming carbon-nitrogen bonds.
|
384 |
+
6. 3. 1.- Acid--ammonia (or amine) ligases (amide synthases).
|
385 |
+
6. 3. 2.- Acid--amino-acid ligases (peptide synthases).
|
386 |
+
6. 3. 3.- Cyclo-ligases.
|
387 |
+
6. 3. 4.- Other carbon--nitrogen ligases.
|
388 |
+
6. 3. 5.- Carbon--nitrogen ligases with glutamine as amido-N-donor.
|
389 |
+
6. 4. -.- Forming carbon-carbon bonds.
|
390 |
+
6. 4. 1.- Forming carbon-carbon bonds.
|
391 |
+
6. 5. -.- Forming phosphoric ester bonds.
|
392 |
+
6. 5. 1.- Forming phosphoric ester bonds.
|
393 |
+
6. 6. -.- Forming nitrogen-metal bonds.
|
394 |
+
6. 6. 1.- Forming coordination complexes.
|
395 |
+
|
396 |
+
7. -. -.- Translocases.
|
397 |
+
7. 1. -.- Catalysing the translocation of hydrons.
|
398 |
+
7. 1. 1.- Hydron translocation or charge separation linked to oxidoreductase reactions.
|
399 |
+
7. 1. 2.- Hydron translocation linked to the hydrolysis of a nucleoside triphosphate.
|
400 |
+
7. 1. 3.- Hydron translocation linked to the hydrolysis of diphosphate.
|
401 |
+
7. 2. -.- Catalysing the translocation of inorganic cations.
|
402 |
+
7. 2. 1.- Linked to oxidoreductase reactions.
|
403 |
+
7. 2. 2.- Linked to the hydrolysis of a nucleoside triphosphate.
|
404 |
+
7. 2. 3.- Linked to the hydrolysis of diphosphate.
|
405 |
+
7. 2. 4.- Linked to decarboxylation.
|
406 |
+
7. 3. -.- Catalysing the translocation of inorganic anions and their chelates.
|
407 |
+
7. 3. 2.- Linked to the hydrolysis of a nucleoside triphosphate.
|
408 |
+
7. 4. -.- Catalysing the translocation amino acids and peptides.
|
409 |
+
7. 4. 2.- Linked to the hydrolysis of a nucleoside triphosphate.
|
410 |
+
7. 5. -.- Catalysing the translocation carbohydrates and their derivatives.
|
411 |
+
7. 5. 2.- Linked to the hydrolysis of a nucleoside triphosphate.
|
412 |
+
7. 6. -.- Catalysing the translocation of other compounds.
|
413 |
+
7. 6. 2.- Linked to the hydrolysis of a nucleoside triphosphate.
|
414 |
+
|
415 |
+
---------------------------------------------------------------------------
|
416 |
+
Copyrighted by the SIB Swiss Institute of Bioinformatics and
|
417 |
+
distributed under the Creative Commons Attribution (CC BY 4.0) License
|
418 |
+
---------------------------------------------------------------------------
|