Changes Log

The entries in the log are arranged in chronological order, with the most recent changes at the top. If you wish to search for changes to a particular enzyme, then enter ec:x.y.z.w (repacing x.y.z.w by the relevant EC number) in the search text box at the top of the page. Other terms can be entered in the text box to limit the results obtained.

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ID	Date/Time	EC/Citation Key	Table	Field	Changed From	Changed To
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.
288237	2024-03-21 05:56:10	3.2.1.225	entry	comments	The enzyme hydrolyses alpha-D-arabinofuranosides with (1->3)- and (1->5)-linkages in D-arabinan core structure of lipoarabinomannan and arabinogalactan of mycobacterial cell wall. cf. EC 3.2.1.55, non-reducing end alpha-L-arabinofuranosidase; EC 3.2.1.bi, D-arabinan exo beta-(1,2)-arabinofuranosidase (non-reducing end); and EC 3.2.1.bk, D-arabinan endo alpha-(1,5)-arabinofuranosidase.	The enzyme hydrolyses alpha-D-arabinofuranosides with (1->3)- and (1->5)-linkages in D-arabinan core structure of lipoarabinomannan and arabinogalactan of mycobacterial cell wall. cf. EC 3.2.1.55, non-reducing end alpha-L-arabinofuranosidase; EC 3.2.1.224, D-arabinan exo beta-(1,2)-arabinofuranosidase (non-reducing end); and EC 3.2.1.226, D-arabinan endo alpha-(1,5)-arabinofuranosidase.
288234	2024-03-20 18:07:42	4.1.1.127	entry	comments	A pyridoxal-phosphate protein. The enzyme, characterized from the cyanobacterium Synechocystis sp. PCC 6803, participates in a biosynthetic pathway for spermidine.	A pyridoxal 5'-phosphate protein. The enzyme, characterized from the cyanobacterium Synechocystis sp. PCC 6803, participates in a biosynthetic pathway for spermidine.
288230	2024-03-20 11:38:51	3.5.99.14	entry	other_names	(S)-norlaudanosoline synthase; 4-hydroxyphenylacetaldehyde hydro-lyase (adding dopamine); 4-hydroxyphenylacetaldehyde hydro-lyase [adding dopamine; (S)-norcoclaurine-forming]	(S)-norlaudanosoline synthase; 4-hydroxyphenylacetaldehyde hydro-lyase (adding dopamine); 4-hydroxyphenylacetaldehyde hydro-lyase [adding dopamine, (S)-norcoclaurine-forming]
288227	2024-03-20 07:03:01	3.2.1.226	entry	comments	The enzyme hydrolyses alpha-(1,5)-D-arabinofuranoside bonds in D-arabinan core structure of lipoarabinomannan and arabinogalactan of mycobacterial cell wall. cf. EC 3.2.1.224, D-arabinan exo beta-(1,2)-arabinofuranosidase (non-reducing end); cf. EC 3.2.1.225, D-arabinan exo alpha-(1,3)/(1,5)-arabinofuranosidase (non-reducing end).	The enzyme hydrolyses alpha-(1->5)-D-arabinofuranoside bonds in D-arabinan core structure of lipoarabinomannan and arabinogalactan of mycobacterial cell wall. cf. EC 3.2.1.224, D-arabinan exo beta-(1,2)-arabinofuranosidase (non-reducing end) and EC 3.2.1.225, D-arabinan exo alpha-(1,3)/(1,5)-arabinofuranosidase (non-reducing end).
288226	2024-03-20 07:03:01	3.2.1.226	entry	other_names	endo-D-arabinanase (ambiguous); DgGH4185a; DgGH4185b; MyxoGH4185; PhageGH4185; Mab4185; EndoMA1; EndoMA2.	endo-D-arabinanase (ambiguous); DgGH4185a; DgGH4185b; MyxoGH4185; PhageGH4185; Mab4185; EndoMA1; EndoMA2
288224	2024-03-20 06:58:24	3.2.1.225	entry	comments	The enzyme hydrolyses alpha-D-arabinofuranosides with (1->3)- and (1->5)-linkages in D-arabinan core structure of lipoarabinomannan and arabinogalactan of mycobacterial cell wall. cf. EC 3.2.1.55, non-reducing end alpha-L-arabinofuranosidase; cf. EC 3.2.1.bi, D-arabinan exo beta-(1,2)-arabinofuranosidase (non-reducing end) and EC 3.2.1.bk, D-arabinan endo alpha-(1,5)-arabinofuranosidase.	The enzyme hydrolyses alpha-D-arabinofuranosides with (1->3)- and (1->5)-linkages in D-arabinan core structure of lipoarabinomannan and arabinogalactan of mycobacterial cell wall. cf. EC 3.2.1.55, non-reducing end alpha-L-arabinofuranosidase; EC 3.2.1.bi, D-arabinan exo beta-(1,2)-arabinofuranosidase (non-reducing end); and EC 3.2.1.bk, D-arabinan endo alpha-(1,5)-arabinofuranosidase.
288222	2024-03-20 06:56:53	3.2.1.225	entry	comments	The enzyme hydrolyses alpha-D-arabinofuranosides with (1->3)- and (1->5)-linkages in D-arabinan core structure of lipoarabinomannan and arabinogalactan of mycobacterial cell wall. cf. EC 3.2.1.55, non-reducing end alpha-L-arabinofuranosidase; cf. EC 3.2.1.bi, D-arabinan exo beta-(1,2)-arabinofuranosidase (non-reducing end); cf. EC 3.2.1.bk, D-arabinan endo alpha-(1,5)-arabinofuranosidase.	The enzyme hydrolyses alpha-D-arabinofuranosides with (1->3)- and (1->5)-linkages in D-arabinan core structure of lipoarabinomannan and arabinogalactan of mycobacterial cell wall. cf. EC 3.2.1.55, non-reducing end alpha-L-arabinofuranosidase; cf. EC 3.2.1.bi, D-arabinan exo beta-(1,2)-arabinofuranosidase (non-reducing end) and EC 3.2.1.bk, D-arabinan endo alpha-(1,5)-arabinofuranosidase.
288220	2024-03-20 06:55:30	3.2.1.225	entry	comments	The enzyme hydrolyses alpha-D-arabinofuranosides with (1,3)- and (1,5)-linkages in D-arabinan core structure of lipoarabinomannan and arabinogalactan of mycobacterial cell wall. cf. EC 3.2.1.55, non-reducing end alpha-L-arabinofuranosidase; cf. EC 3.2.1.224, D-arabinan exo beta-(1,2)-arabinofuranosidase (non-reducing end); cf. EC 3.2.1.226, D-arabinan endo alpha-(1,5)-arabinofuranosidase.	The enzyme hydrolyses alpha-D-arabinofuranosides with (1->3)- and (1->5)-linkages in D-arabinan core structure of lipoarabinomannan and arabinogalactan of mycobacterial cell wall. cf. EC 3.2.1.55, non-reducing end alpha-L-arabinofuranosidase; cf. EC 3.2.1.bi, D-arabinan exo beta-(1,2)-arabinofuranosidase (non-reducing end); cf. EC 3.2.1.bk, D-arabinan endo alpha-(1,5)-arabinofuranosidase.
288218	2024-03-20 04:03:28	2.7.11.36	entry	other_names	MASTL; gwl; greatwall kinase; RIM15; microtubule-associated (MASTL)-subfamily-protein kinase.	MASTL; gwl; greatwall kinase; RIM15; microtubule-associated (MASTL)-subfamily-protein kinase
288216	2024-03-18 09:44:23	1.14.14.185	entry	comments	The enzyme is active in the biosynthetic pathway of paclitaxel (Taxol) in Taxus species (yew)	The enzyme is active in the biosynthetic pathway of paclitaxel (Taxol) in Taxus species (yew).
288214	2024-03-14 08:16:10	1.1.1.438	entry	comments	The enzyme from Corynebacterium cyclohexanicum is highly specific for the cis-4-hydroxy derivative. cf. EC 1.1.1.226, trans-4-hydroxycyclohexanecarboxylate dehydrogenase	The enzyme from Corynebacterium cyclohexanicum is highly specific for the cis-4-hydroxy derivative. cf. EC 1.1.1.226, trans-4-hydroxycyclohexanecarboxylate dehydrogenase.
288209	2024-03-01 14:15:55	4.1.2.66	entry	comments	The enzyme has been purified from vanilla pods of the orchid Vanilla planifolia. It is higly specific for 4-coumarate. Similar compounds such as cinnamate, caffeate, sinapate and o-coumarate are not substrates.	The enzyme has been purified from vanilla pods of the orchid Vanilla planifolia. It is highly specific for 4-coumarate. Similar compounds such as cinnamate, caffeate, sinapate and o-coumarate are not substrates.
288203	2024-03-01 14:08:28	2.5.1.159	entry	comments	Requires Mg2+. The enzyme, characterized from the cyanobacterium Fischerella ambigua UTEX 1903, is involved in the biosynthesis of hapalindole-type alkaloids. When acting on hapalindole U, the enzyme forms ambiguine H.	Requires Mg2+. The enzyme, characterized from the cyanobacterium Fischerella ambigua UTEX 1903, is involved in the biosynthesis of hapalindole-type alkaloids.
288137	2024-02-29 13:25:47	2.5.1.159	entry	glossary	prenyl diphosphate = dimethylallyl diphosphate hapalindole G = (6aS,8R,9R,10R,10aS)-8-chloro-10-isocyano-6,6,9-trimethyl-9-vinyl-2,6,6a,7,8,9,10,10a-octahydronaphtho[1,2,3-cd]indole ambiguine A = (6aS,8R,9R,10R,10aS)-8-chloro-10-isocyano-6,6,9-trimethyl-1-(2-methylbut-3-en-2-yl)-9-vinyl-2,6,6a,7,8,9,10,10a-octahydronaphtho[1,2,3-cd]indole	prenyl diphosphate = dimethylallyl diphosphate hapalindole G = (6aS,8R,9R,10R,10aS)-8-chloro-10-isocyano-6,6,9-trimethyl-9-vinyl-2,6,6a,7,8,9,10,10a-octahydronaphtho[1,2,3-cd]indole ambiguine A = (6aS,8R,9R,10R,10aS)-8-chloro-10-isocyano-6,6,9-trimethyl-1-(2-methylbut-3-en-2-yl)-9-vinyl-2,6,6a,7,8,9,10,10a-octahydronaphtho[1,2,3-cd]indole hapalindole U = (6aS,9R,10R,10aS)-10-isocyano-6,6,9-trimethyl-9-vinyl-2,6,6a,7,8,9,10,10a-octahydronaphtho[1,2,3-cd]indole ambiguine H = (6aS,9R,10R,10aS)-9-ethenyl-10-isocyano-6,6,9-trimethyl-1-(2-methylbut-3-en-2-yl)-2,6,6a,7,8,9,10,10a-octahydronaphtho[1,2,3-cd]indole
288135	2024-02-29 13:25:47	2.5.1.159	entry	reaction	prenyl diphosphate + hapalindole G = ambiguine A + diphosphate	(1) prenyl diphosphate + hapalindole G = ambiguine A + diphosphate;;(2) prenyl diphosphate + hapalindole U = ambiguine H + diphosphate
288132	2024-02-29 06:50:50	3.5.99.12	entry	glossary	(R)-salsolinol = (+)-salsolinol = (R)-1,2,3,4-tetrahydro-1-methylisoquinoline-6,7-diol	(R)-salsolinol = (+)-salsolinol = (1R)-1,2,3,4-tetrahydro-1-methylisoquinoline-6,7-diol