|
|
| ID |
Date/Time |
EC/Citation Key |
Table |
Field |
Changed From |
Changed To |
| 288486 |
2024-05-03 10:16:55 |
4.2.3.185 |
entry |
diagram |
For diagram of biosynthesis of diterpenoids from <em>ent</em>-copalyl diphosphate, {terp/entcop} and for diagram of mechanism for <em>ent</em>-atiserene, <em>ent</em>-kaurene and <em>ent</em>-isokaurene, {terp/kaurene} |
For diagram of biosynthesis of diterpenoids from <em>ent</em>-copalyl diphosphate, {terp/entcop} and for diagram of <em>ent</em>-atiserene, <em>ent</em>-kaurene and <em>ent</em>-isokaurene, {terp/kaurene} |
| 288479 |
2024-05-03 10:16:55 |
4.2.3.185 |
entry |
diagram |
For diagram of biosynthesis of diterpenoids from <em>ent</em>-copalyl diphosphate, {terp/entcop} and for diagram of <em>ent</em>-atiserene, <em>ent</em>-kaurene and <em>ent</em>-isokaurene, {terp/kaurene} |
For diagram of biosynthesis of diterpenoids from <em>ent</em>-copalyl diphosphate, {terp/entcop} and for diagram of mechanism for <em>ent</em>-atiserene, <em>ent</em>-kaurene and <em>ent</em>-isokaurene, {terp/kaurene} |
| 288477 |
2024-05-03 10:16:55 |
4.2.3.185 |
entry |
comments |
Isolated from the plant Isodon rubescens. |
Isolated from the plant Isodon rubescens and several species of Aconitum as well as species of Streptomyces. |
| 288476 |
2024-05-03 10:16:55 |
4.2.3.185 |
entry |
other_names |
IrKSL4 |
IrKSL4; AcKSL1; ApKSL1; AtKSL1; AsKSL1 |
| 288459 |
2024-05-03 10:16:54 |
4.2.1.182 |
entry |
glossary |
trans-anhydromevalonate 5-phosphate = (2E)-3-methyl-5-phosphooxypent-2-enoate |
(2E)-3-methyl-5-phosphooxypent-2-enoate = trans-anhydromevalonate 5-phosphate |
| 288454 |
2024-05-03 10:16:54 |
4.2.1.182 |
entry |
sys_name |
R-5-phosphomevalonate hydro-lyase |
(R)-5-phosphomevalonate hydro-lyase |
| 288453 |
2024-05-03 10:16:54 |
4.2.1.182 |
entry |
reaction |
(R)-5-phosphomevalonate = trans-anhydromevalonate 5-phosphate + H2O |
(R)-5-phosphomevalonate = (2E)-3-methyl-5-phosphooxypent-2-enoate + H2O |
| 288448 |
2024-05-03 10:16:53 |
4.1.1.126 |
entry |
glossary |
trans-anhydromevalonate 5-phosphate = (2E)-3-methyl-5-phosphooxypent-2-enoate
3-methylbut-3-en-1-yl phosphate = isopentenyl phosphate |
(2E)-3-methyl-5-phosphooxypent-2-enoate = trans-anhydromevalonate 5-phosphate
3-methylbut-3-en-1-yl phosphate = isopentenyl phosphate |
| 288442 |
2024-05-03 10:16:53 |
4.1.1.126 |
entry |
sys_name |
trans-anhydromevalonate 5-phosphate carboxy-lyase |
(2E)-3-methyl-5-phosphooxypent-2-enoate carboxy-lyase |
| 288441 |
2024-05-03 10:16:53 |
4.1.1.126 |
entry |
reaction |
trans-anhydromevalonate 5-phosphate = 3-methylbut-3-en-1-yl phosphate + CO2 |
(2E)-3-methyl-5-phosphooxypent-2-enoate = 3-methylbut-3-en-1-yl phosphate + CO2 |
| 288421 |
2024-05-03 10:16:52 |
3.4.26.2 |
entry |
comments |
The enzyme, isolated from the fungus Scytalidium lignicola and found in several other fungi, has a low pH optimum, being most active at pH 2 with casein as substrate. It differs from the pepsins (EC 3.4.23.1 and EC 3.4.23.2) in being insensitive to inhibition by pepstatin. It also differs from mammalian pepsins in showing a preference for a positively charged residue ( Lys or Arg) at the P3 position. In addition to the catalytic Glu residue, a Gln residue appears to play an important role in the hydrolytic mechanism. A member of peptidase family G01, the "eqolisin" family of glutamic peptidases (G01.0001). |
The enzyme, isolated from the fungus Scytalidium lignicola and found in several other fungi, has a low pH optimum, being most active at pH 2 with casein as substrate. It differs from the pepsins (EC 3.4.23.1 and EC 3.4.23.2) in being insensitive to inhibition by pepstatin. It also differs from mammalian pepsins in showing a preference for a positively charged residue (Lys or Arg) at the P3 position. In addition to the catalytic Glu residue, a Gln residue appears to play an important role in the hydrolytic mechanism. A member of peptidase family G01, the "eqolisin" family of glutamic peptidases (G01.0001). |
| 288412 |
2024-05-03 10:16:50 |
3.4.26.1 |
entry |
other_names |
CaaX prenyl protease 2; prenyl protein-specific endoprotease 2; PPSEP 2; alpha-factor-converting enzyme RCE1; ras converting enzyme; RACE; glutamic-type intramembrane endopeptidase Rce1; type II CAAX protease. |
CaaX prenyl protease 2; prenyl protein-specific endoprotease 2; PPSEP 2; alpha-factor-converting enzyme RCE1; ras converting enzyme; RACE; glutamic-type intramembrane endopeptidase Rce1; type II CAAX protease |
| 288411 |
2024-05-03 10:16:50 |
3.4.26.1 |
entry |
reaction |
Hydrolyses the peptide bond -P2-(S-farnesyl or geranylgeranyl)C-P1'-P2'-P3'-COOH where where P1' and P2' are amino acids with aliphatic sidechains and P3' is any C-terminal residue. |
Hydrolyses the peptide bond -P2-(S-farnesyl or geranylgeranyl)C-P1'-P2'-P3'-COOH where where P1' and P2' are amino acids with aliphatic sidechains and P3' is any C-terminal residue |
| 288403 |
2024-05-03 10:16:49 |
3.4.21.123 |
entry |
comments |
This bacterial pepstatin-insensitive carboxyl proteinase has been isolated and characterized from Bacillus sp. MN-32 and from several Burkholderia spp. Kumamolysin from Bacillus sp. MN-32 exhibits a Ser278/Glu78/Asp82 catalytic triad. The enzyme is a type example of peptidase family S53 in the MEROPS Peptidas Database. |
This bacterial pepstatin-insensitive carboxyl proteinase has been isolated and characterized from Bacillus sp. MN-32 and from several Burkholderia spp. Kumamolysin from Bacillus sp. MN-32 exhibits a Ser278/Glu78/Asp82 catalytic triad. The enzyme is a type example of peptidase family S53 in the MEROPS Peptidase Database. |
| 288394 |
2024-05-03 10:16:48 |
3.2.1.223 |
entry |
comments |
The enzyme, characterized from the bacterium Bifidobacterium pseudocatenulatum, specifically hydrolyses beta;-L-Arap-(1->3)-L-Araf disaccharides from the non-reducing terminal of arabinogalactan using an exo mode of action. It is active with arabinogalactan-proteins (AGPs) containing type II arabinogalactans such as gum arabic AGP and larch AGP. The enzyme can also hydrolyse alpha-D-Galp-(1->3)-L-Araf disaccharides (cf. EC 3.2.1.215) with a much lower activity. |
The enzyme, characterized from the bacterium Bifidobacterium pseudocatenulatum, specifically hydrolyses beta-L-Arap-(1->3)-L-Araf disaccharides from the non-reducing terminal of arabinogalactan using an exo mode of action. It is active with arabinogalactan-proteins (AGPs) containing type II arabinogalactans such as gum arabic AGP and larch AGP. The enzyme can also hydrolyse alpha-D-Galp-(1->3)-L-Araf disaccharides (cf. EC 3.2.1.215) with a much lower activity. |
| 288389 |
2024-05-03 10:16:47 |
3.2.1.222 |
entry |
glossary |
funoran = [-3)-beta-D-galactopyranose-6-sulfate-(1-4)-3,6-anhydro-alpha-L-galactopyranose-(1-] |
funoran = [->3)-beta-D-galactopyranose-6-sulfate-(1->4)-3,6-anhydro-alpha-L-galactopyranose-(1->] |
| 288384 |
2024-05-03 10:16:47 |
3.2.1.222 |
entry |
comments |
The enzyme is an endo hydrolase that hydrolyses the beta(1,4) bond in funoran, a polysaccharide produced by red algae of the genus Gloiopeltis. The enzyme from the marine bacterium Wenyingzhuangia aestuarii OF219 acts on agarose with a higher efficiency (cf. EC 3.2.1.81, beta-agarase), but binds funoran preferentially. |
The enzyme is an endo hydrolase that hydrolyses the beta(1->4) bond in funoran, a polysaccharide produced by red algae of the genus Gloiopeltis. The enzyme from the marine bacterium Wenyingzhuangia aestuarii OF219 acts on agarose with a higher efficiency (cf. EC 3.2.1.81, beta-agarase), but binds funoran preferentially. |
| 288377 |
2024-05-03 10:16:45 |
2.4.1.11 |
entry |
comments |
The accepted name varies according to the source of the enzyme and the nature of its synthetic product (cf. EC 2.4.1.1, phosphorylase). Glycogen synthase from animal tissues is a complex of a catalytic subunit and the protein glycogenin. The enzyme requires glucosylated glycogenin as a primer; this is the reaction product of EC 2.4.1.186 (glycogenin glucosyltransferase). A similar enzyme utilizes ADP-glucose (EC 2.4.1.21, starch synthase). |
The accepted name varies according to the source of the enzyme and the nature of its synthetic product (cf. EC 2.4.1.1, glycogen phosphorylase). Glycogen synthase from animal tissues is a complex of a catalytic subunit and the protein glycogenin. The enzyme requires glucosylated glycogenin as a primer; this is the reaction product of EC 2.4.1.186 (glycogenin glucosyltransferase). A similar enzyme utilizes ADP-glucose [EC 2.4.1.21, starch synthase (glycosyl-transferring)]. |
| 288370 |
2024-05-03 10:16:44 |
1.8.7.1 |
entry |
comments |
An iron protein. The enzyme participates in sulfate assimilation. While it is usually found in cyanobacteria, plants and algae, it has also been reported in bacteria [4]. Different from EC 1.8.99.5, dissimilatory sulfite reductase, which is involved in prokaryotic sulfur-based energy metabolism. cf. EC 1.8.1.2, assimilatory sulfite reductase (NADPH). |
An iron protein. The enzyme participates in sulfate assimilation. While it is usually found in cyanobacteria, plants and algae, it has also been reported in bacteria [4]. Different from EC 1.8.1.22, dissimilatory sulfite reductase system, which is involved in prokaryotic sulfur-based energy metabolism. cf. EC 1.8.1.2, assimilatory sulfite reductase (NADPH). |
| 288362 |
2024-05-03 10:16:43 |
1.8.2.5 |
entry |
comments |
The enzyme is found in sulfate-reducing bacteria. The source of the electrons is molecular hydrogen, via EC 1.12.2.1, cytochrome-c3 hydrogenase. The organisms utilize the sulfite that is produced for energy generation by EC 1.8.99.5, dissimilatory sulfite reductase. |
The enzyme is found in sulfate-reducing bacteria. The source of the electrons is molecular hydrogen, via EC 1.12.2.1, cytochrome-c3 hydrogenase. The organisms utilize the sulfite that is produced for energy generation by EC 1.8.1.22, dissimilatory sulfite reductase system. |
| 288354 |
2024-05-03 10:16:42 |
1.8.1.2 |
entry |
comments |
Contains siroheme, [4Fe-4S] cluster, FAD and FMN. The enzyme, which catalyses the six-electron reduction of sulfite to sulfide, is involved in sulfate assimilation in bacteria and yeast. Different from EC 1.8.99.5, dissimilatory sulfite reductase, which is involved in prokaryotic sulfur-based energy metabolism. cf. EC 1.8.7.1, assimilatory sulfite reductase (ferredoxin). |
Contains siroheme, [4Fe-4S] cluster, FAD and FMN. The enzyme, which catalyses the six-electron reduction of sulfite to sulfide, is involved in sulfate assimilation in bacteria and yeast. Different from EC 1.8.1.22, dissimilatory sulfite reductase system, which is involved in prokaryotic sulfur-based energy metabolism. cf. EC 1.8.7.1, assimilatory sulfite reductase (ferredoxin). |
| 288351 |
2024-04-11 12:26:23 |
4.2.3.229 |
entry |
diagram |
|
For diagram of <em>ent</em>-atiserene, <em>ent</em>-kaurene and <em>ent</em>-isokaurene, {terp/kaurene} |
| 288349 |
2024-04-11 12:26:00 |
4.2.3.228 |
entry |
diagram |
|
For diagram of acyclic monoterpenoid biosynthesis, {terp/acyclicM} |
| 288347 |
2024-04-11 12:25:43 |
4.2.3.218 |
entry |
diagram |
|
For diagram of miscellaneous diterpenoid biosynthesis, {terp/miscdi} |
| 288345 |
2024-04-11 12:25:30 |
4.2.3.212 |
entry |
diagram |
|
For diagram of <em>ent</em>-cadinane sesquiterpenoid biosynthesis, {terp/entcad} |
| 288343 |
2024-04-11 12:24:28 |
4.1.99.29 |
entry |
diagram |
|
For diagram of the futalosine pathway, {misc/futal} |
| 288341 |
2024-04-11 12:24:12 |
2.5.1.159 |
entry |
diagram |
|
For diagram of hapalindole/fischerindole biosynthesis, {alkaloid/hapal} |
| 288337 |
2024-04-08 06:56:21 |
3.1.3.67 |
entry |
diagram |
For diagram of 1-phosphatidyl-<em>myo</em>-inositol metabolism (part 2), {inositol/PtdIns2} |
For diagram of 1-phosphatidyl-<em>myo</em>-inositol metabolism, {inositol/PtdIns2} |
| 288336 |
2024-04-08 06:56:21 |
3.1.3.67 |
entry |
other_names |
PTEN; MMAC1; phosphatidylinositol-3,4,5-trisphosphate 3-phosphohydrolase |
PTEN (gene name); MMAC1 (gene name); phosphatidylinositol-3,4,5-trisphosphate 3-phosphohydrolase |
| 288265 |
2024-04-04 11:16:33 |
2.7.11.37 |
entry |
comments |
MAST (Microtubule Associated Serine/Threonine) kinases are eukaryotic-wide kinases with roles in microtubule function, PTEN regulation and a variety of neuronal functions. They are found in most eukaryotes, though lost from most fungi and ciliates. MAST kinases associate with their substrates via their PDZ domains. Substrates include the PTEN phosphatase (EC 3.1.3.67) in human and nematodes, and Dlic (Dynein light intermediate chain) in Drosophila. The latter is phosphorylated on Ser401. |
Requires Mg2+. MAST (Microtubule Associated Serine/Threonine) kinases are eukaryotic-wide kinases with roles in microtubule function, PTEN regulation and a variety of neuronal functions. They are found in most eukaryotes, though lost from most fungi and ciliates. MAST kinases associate with their substrates via their PDZ domains. Substrates include the PTEN phosphatase (EC 3.1.3.67) in human and nematodes, and Dlic (Dynein light intermediate chain) in Drosophila. The latter is phosphorylated on Ser401. |
| 288262 |
2024-04-04 11:15:53 |
2.7.11.37 |
entry |
accepted_name |
MAST-subfamily kinase |
MAST-subfamily protein kinase |
| 288256 |
2024-03-30 15:12:38 |
2.4.1.397 |
entry |
comments |
This enzyme is the cyclization domain of cyclic beta-1,2-glucan synthase. Enzymes from Brucella abortus and Thermoanaerobacter italicus were characterized. The cyclization domain of cyclic beta-1,2-glucan synthase is flanked by an N-terminal beta-1,2-glucosyltransferase domain (UDP-alpha-D-glucose-dependent synthase, not EC 2.4.1.391) and a C-terminal beta-1,2-glucoside phosphorylase domain (cf. EC 2.4.1.333), with the former responsible for elongation and the latter for chain length control. The cyclization domain of Thermoanaerobacter italicus cyclizes linear oligosaccharides with a degree of polymerization (DP) of 21 or higher to produce cyclic glucans with DP 17 or higher. The cyclization domain also disproportionates linear beta-1,2-glucooligosaccharides without cycling. The entire cyclic beta-1,2-glucan synthase from Brucella abortus synthesizes cyclic beta-1,2-glucans with DP 17-22. |
This enzyme is the cyclization domain of cyclic beta-1,2-glucan synthase. Enzymes from Brucella abortus and Thermoanaerobacter italicus were characterized. The cyclization domain of cyclic beta-1,2-glucan synthase is flanked by an N-terminal beta-1,2-glucosyltransferase domain (a UDP-alpha-D-glucose-dependent synthase, not EC 2.4.1.391) and a C-terminal beta-1,2-glucoside phosphorylase domain (cf. EC 2.4.1.333), with the former responsible for elongation and the latter for chain length control. The cyclization domain of Thermoanaerobacter italicus cyclizes linear oligosaccharides with a degree of polymerization (DP) of 21 or higher to produce cyclic glucans with DP 17 or higher. The cyclization domain also disproportionates linear beta-1,2-glucooligosaccharides without cycling. The entire cyclic beta-1,2-glucan synthase from Brucella abortus synthesizes cyclic beta-1,2-glucans with DP 17-22. |
| 288251 |
2024-03-23 20:32:09 |
2.4.1.397 |
entry |
comments |
This enzyme is the cyclization domain of cyclic beta-1,2-glucan synthase. Enzymes from Brucella abortus and Thermoanaerobacter italicus were characterized. The cyclization domain of cyclic beta-1,2-glucan synthase is flanked by an N-terminal beta-1,2-glucosyltransferase domain (cf. EC 2.4.1.391) and a C-terminal beta-1,2-glucoside phosphorylase domain (cf. EC 2.4.1.333), with the former responsible for elongation and the latter for chain length control. The cyclization domain of Thermoanaerobacter italicus cyclizes linear oligosaccharides with a degree of polymerization (DP) of 21 or higher to produce cyclic glucans with DP 17 or higher. The cyclization domain also disproportionates linear beta-1,2-glucooligosaccharides without cycling. The entire cyclic beta-1,2-glucan synthase from Brucella abortus synthesizes cyclic beta-1,2-glucans with DP 17-22. |
This enzyme is the cyclization domain of cyclic beta-1,2-glucan synthase. Enzymes from Brucella abortus and Thermoanaerobacter italicus were characterized. The cyclization domain of cyclic beta-1,2-glucan synthase is flanked by an N-terminal beta-1,2-glucosyltransferase domain (UDP-alpha-D-glucose-dependent synthase, not EC 2.4.1.391) and a C-terminal beta-1,2-glucoside phosphorylase domain (cf. EC 2.4.1.333), with the former responsible for elongation and the latter for chain length control. The cyclization domain of Thermoanaerobacter italicus cyclizes linear oligosaccharides with a degree of polymerization (DP) of 21 or higher to produce cyclic glucans with DP 17 or higher. The cyclization domain also disproportionates linear beta-1,2-glucooligosaccharides without cycling. The entire cyclic beta-1,2-glucan synthase from Brucella abortus synthesizes cyclic beta-1,2-glucans with DP 17-22. |
