ExplorEnz: Changes log The Enzyme Database


 

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
 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.
 288245  2024-03-21 11:39:36  3.6.4.13  hist  note  RNA helicase. Now covered by EC 5.6.2.5 (RNA 5′-3′ helicase), EC 5.6.2.6 (RNA 3′-5′ helicase) and EC 5.6.2.7 (DEAD-box RNA helicase)  RNA helicase. Now covered by EC 5.6.2.5, RNA 5′-3′ helicase, EC 5.6.2.6, RNA 3′-5′ helicase and EC 5.6.2.7, DEAD-box RNA helicase
 288244  2024-03-21 11:21:39  3.6.4.13  hist  note  RNA helicase. Now EC 5.6.2.5, RNA 5′-3′ helicase; EC 5.6.2.6, RNA 3′-5′ helicase; and EC 5.6.2.7, DEAD-box RNA helicase  RNA helicase. Now covered by EC 5.6.2.5 (RNA 5′-3′ helicase), EC 5.6.2.6 (RNA 3′-5′ helicase) and EC 5.6.2.7 (DEAD-box RNA helicase)
 288243  2024-03-21 11:17:59  3.6.4.13  hist  note  RNA helicase. Now EC 5.6.2.5, RNA helicase  RNA helicase. Now EC 5.6.2.5, RNA 5′-3′ helicase; EC 5.6.2.6, RNA 3′-5′ helicase; and EC 5.6.2.7, DEAD-box RNA helicase
 288242  2024-03-21 05:58:05  5.6.2.6  hist  note  RNA 3-5 helicase. Now EC 5.6.2.6.  
 288240  2024-03-21 05:56:56  5.6.2.6  hist  note    RNA 3-5 helicase. Now EC 5.6.2.6.
 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
 288084  2024-02-27 06:47:05  1.14.14.185  entry  reaction  5,20-epoxytax-11-en-4alpha-ol + [reduced NADPH---hemoprotein reductase] + O2 = 5,20-epoxytax-11-en-4alpha,9alpha-diol + [oxidized NADPH---hemoprotein reductase] + H2O  5,20-epoxytax-11-en-4alpha-ol + [reduced NADPH---hemoprotein reductase] + O2 = 5,20-epoxytax-11-ene-4alpha,9alpha-diol + [oxidized NADPH---hemoprotein reductase] + H2O
 288080  2024-02-27 06:22:32  1.14.14.185  entry  sys_name  oxotaxadiene-4alpha-ol,[reduced NADPH---hemoprotein reductase]:oxygen oxidoreductase (9alpha-hydroxylating)  5,20-epoxytax-11-en-4alpha-ol,[reduced NADPH---hemoprotein reductase]:oxygen oxidoreductase (9alpha-hydroxylating)
 288079  2024-02-27 06:22:32  1.14.14.185  entry  reaction  oxotaxadiene-4alpha-ol + [reduced NADPH---hemoprotein reductase] + O2 = oxotaxadiene-4alpha,9alpha-diol + [oxidized NADPH---hemoprotein reductase] + H2O  5,20-epoxytax-11-en-4alpha-ol + [reduced NADPH---hemoprotein reductase] + O2 = 5,20-epoxytax-11-en-4alpha,9alpha-diol + [oxidized NADPH---hemoprotein reductase] + H2O
 288077  2024-02-26 14:53:21  4.1.2.66  entry  reaction  4-coumarate + H2O = 4-hydroxybenzaldehyde + acetate (overall reaction);;(a) 4-coumarate + H2O = 3-hydroxy-3-(4-hydroxyphenyl)propanoate;;(b) 3-hydroxy-3-(4-hydroxyphenyl)propanoate = 4-hydroxybenzaldehyde + acetate  4-coumarate + H2O = 4-hydroxybenzaldehyde + acetate (overall reaction);;(1a) 4-coumarate + H2O = 3-hydroxy-3-(4-hydroxyphenyl)propanoate;;(1b) 3-hydroxy-3-(4-hydroxyphenyl)propanoate = 4-hydroxybenzaldehyde + acetate
 288075  2024-02-26 14:50:50  4.1.2.65  entry  reaction  ferulate + H2O = vanillin + acetate (overall reaction);;(a) ferulate + H2O = 3-hydroxy-3-(4-hydroxy-3-methoxyphenyl)propanoate;;(b) 3-hydroxy-3-(4-hydroxy-3-methoxyphenyl)propanoate = vanillin + acetate  ferulate + H2O = vanillin + acetate (overall reaction);;(1a) ferulate + H2O = 3-hydroxy-3-(4-hydroxy-3-methoxyphenyl)propanoate;;(1b) 3-hydroxy-3-(4-hydroxy-3-methoxyphenyl)propanoate = vanillin + acetate
 288073  2024-02-26 14:48:45  3.2.1.226  entry  reaction  Hydrolysis of internal alpha-D-arabinofuranoside bonds in D-arabinans.  Hydrolysis of internal alpha-D-arabinofuranoside bonds in D-arabinans
 288071  2024-02-26 14:48:25  3.2.1.225  entry  reaction  Hydrolysis of terminal non-reducing alpha-D-arabinofuranoside residues in D-arabinans.  Hydrolysis of terminal non-reducing alpha-D-arabinofuranoside residues in D-arabinans
 288069  2024-02-26 14:48:07  3.2.1.224  entry  reaction  Hydrolysis of terminal non-reducing beta-D-arabinofuranoside residues in D-arabinans.  Hydrolysis of terminal non-reducing beta-D-arabinofuranoside residues in D-arabinans
 288066  2024-02-26 12:49:21  3.1.2.33  entry  glossary  glycinebetainyl-CoA = betainyl-CoA = N,N,N-trimethylglycyl-CoA  betaine-CoA = glycinebetainyl-CoA = betainyl-CoA = N,N,N-trimethylglycyl-CoA
 288063  2024-02-26 12:49:21  3.1.2.33  entry  sys_name  glycinebetainyl-CoA hydrolase  betaine-CoA hydrolase
 288062  2024-02-26 12:49:21  3.1.2.33  entry  reaction  glycinebetainyl-CoA + H2O = glycine betaine + CoA  betaine-CoA + H2O = glycine betaine + CoA
 288058  2024-02-26 10:46:58  2.1.1.243  entry  other_names  mrsA (gene name); argN (gene name); 2-ketoarginine methyltransferase  mrsA (gene name); argN (gene name); 2-ketoarginine methyltransferase; S-adenosyl-L-methionine:5-carbamimidamido-2-oxopentanoate S-methyltransferase
 288036  2024-02-24 18:03:19  5.6.2.6  entry  comments  RNA helicases, which participate in nearly all aspects of RNA metabolism, utilize the energy from ATP hydrolysis to unwind RNA. The engine core of helicases is usually made of a pair of RecA-like domains that form an NTP binding cleft at their interface. Changes in the chemical state of the NTP binding cleft (binding of the NTP or its hydrolysis products) alter the relative positions of the RecA-like domains and nucleic acid-binding domains, creating structural motions that disrupt the pairing of the nucleic acid, causing separation and unwinding. Most RNA helicases utilize a mechanism known as canonical duplex unwinding, in which the helicase binds to a single stranded region adjacent to the duplex and then translocates along the bound strand with defined directionality, displacing the complementary strand. Most of these helicases proceed 3' to 5' (type A polarity), but some proceed 5' to 3' (type B polarity - cf. EC 5.6.2.5, RNA 5'-3' helicase), and some are able to catalyse unwinding in either direction [1,3]. Most canonically operating helicases require substrates with single stranded regions in a defined orientation (polarity) with respect to the duplex. A different class of RNA helicases, EC 5.6.2.g, DEAD-box RNA helicase, use a different mechanism and unwind short stretches of RNA with no translocation.  RNA helicases, which participate in nearly all aspects of RNA metabolism, utilize the energy from ATP hydrolysis to unwind RNA. The engine core of helicases is usually made of a pair of RecA-like domains that form an NTP binding cleft at their interface. Changes in the chemical state of the NTP binding cleft (binding of the NTP or its hydrolysis products) alter the relative positions of the RecA-like domains and nucleic acid-binding domains, creating structural motions that disrupt the pairing of the nucleic acid, causing separation and unwinding. Most RNA helicases utilize a mechanism known as canonical duplex unwinding, in which the helicase binds to a single stranded region adjacent to the duplex and then translocates along the bound strand with defined directionality, displacing the complementary strand. Most of these helicases proceed 3' to 5' (type A polarity), but some proceed 5' to 3' (type B polarity - cf. EC 5.6.2.5, RNA 5'-3' helicase), and some are able to catalyse unwinding in either direction [1,3]. Most canonically operating helicases require substrates with single stranded regions in a defined orientation (polarity) with respect to the duplex. A different class of RNA helicases, EC 5.6.2.7, DEAD-box RNA helicase, use a different mechanism and unwind short stretches of RNA with no translocation.
 288031  2024-02-24 18:03:17  5.6.2.5  entry  comments  RNA helicases, which participate in nearly all aspects of RNA metabolism, utilize the energy from ATP hydrolysis to unwind RNA. The engine core of helicases is usually made of a pair of RecA-like domains that form an NTP binding cleft at their interface. Changes in the chemical state of the NTP binding cleft (binding of the NTP or its hydrolysis products) alter the relative positions of the RecA-like domains and nucleic acid-binding domains, creating structural motions that disrupt the pairing of the nucleic acid, causing separation and unwinding. Most RNA helicases utilize a mechanism known as canonical duplex unwinding, in which the helicase binds to a single stranded region adjacent to the duplex and then translocates along the bound strand with defined directionality, displacing the complementary strand. Most of these helicases proceed 3' to 5' (type A polarity - cf. EC 5.6.2.f, RNA 3'-5' helicase), but some proceed 5' to 3' (type B polarity), and some are able to catalyse unwinding in either direction [1,4]. Most canonically operating helicases require substrates with single stranded regions in a defined orientation (polarity) with respect to the duplex. A different class of RNA helicases, EC 5.6.2.g, DEAD-box RNA helicase, use a different mechanism and unwind short stretches of RNA with no translocation.  RNA helicases, which participate in nearly all aspects of RNA metabolism, utilize the energy from ATP hydrolysis to unwind RNA. The engine core of helicases is usually made of a pair of RecA-like domains that form an NTP binding cleft at their interface. Changes in the chemical state of the NTP binding cleft (binding of the NTP or its hydrolysis products) alter the relative positions of the RecA-like domains and nucleic acid-binding domains, creating structural motions that disrupt the pairing of the nucleic acid, causing separation and unwinding. Most RNA helicases utilize a mechanism known as canonical duplex unwinding, in which the helicase binds to a single stranded region adjacent to the duplex and then translocates along the bound strand with defined directionality, displacing the complementary strand. Most of these helicases proceed 3' to 5' (type A polarity - cf. EC 5.6.2.6, RNA 3'-5' helicase), but some proceed 5' to 3' (type B polarity), and some are able to catalyse unwinding in either direction [1,4]. Most canonically operating helicases require substrates with single stranded regions in a defined orientation (polarity) with respect to the duplex. A different class of RNA helicases, EC 5.6.2.7, DEAD-box RNA helicase, use a different mechanism and unwind short stretches of RNA with no translocation.
 288027  2024-02-24 18:03:13  4.2.3.226  entry  comments  The enzyme occurs in plants. The initial cyclization product is a (7R)-beta-bisabolyl cation. The major final product is (+)-2-epi-prezizaene. Other products are (-)-alpha-cedrene (cf. EC 4.2.3.gw, (-)-alpha-cedrene synthase), small amounts of (-)-beta-curcumene, and other sesquiterpenes with less than 10% yield. The enzyme also catalyses the reaction of EC 4.2.3.61, 5-epiaristolochene synthase.  The enzyme occurs in plants. The initial cyclization product is a (7R)-beta-bisabolyl cation. The major final product is (+)-2-epi-prezizaene. Other products are (-)-alpha-cedrene (cf. EC 4.2.3.227, (-)-alpha-cedrene synthase), small amounts of (-)-beta-curcumene, and other sesquiterpenes with less than 10% yield. The enzyme also catalyses the reaction of EC 4.2.3.61, 5-epiaristolochene synthase.
 288023  2024-02-24 18:03:12  4.2.3.223  entry  comments  A diterpene synthase isolated from the bacterium Allokutzneria albata. It also generates allokutznerene (EC 4.2.3.gt, allokutznerene synthase), phomopsene (EC 4.2.3.222, phomopsene synthase) and traces of (-)-spiroviolene (EC 4.2.3.158, (-)-spiroviolene synthase).  A diterpene synthase isolated from the bacterium Allokutzneria albata. It also generates allokutznerene (EC 4.2.3.224, allokutznerene synthase), phomopsene (EC 4.2.3.222, phomopsene synthase) and traces of (-)-spiroviolene (EC 4.2.3.158, (-)-spiroviolene synthase).
 288019  2024-02-24 18:03:11  4.2.3.222  entry  comments  A diterpene synthase from the fungus Diaporthe amygdali. Phomopsene synthase has also been isolated from the bacteria Nocardia testacea, Nocardia rhamnosiphila, and Allokutzneria albata. The Allokutzneria albata enzyme also generates allokutznerene (EC 4.2.3.gt, allokutznerene synthase), bonnadiene (EC 4.2.3.gs, bonnadiene synthase) and traces of (-)-spiroviolene (EC 4.2.3.158, (-)-spiroviolene synthase).  A diterpene synthase from the fungus Diaporthe amygdali. Phomopsene synthase has also been isolated from the bacteria Nocardia testacea, Nocardia rhamnosiphila, and Allokutzneria albata. The Allokutzneria albata enzyme also generates allokutznerene (EC 4.2.3.224, allokutznerene synthase), bonnadiene (EC 4.2.3.223, bonnadiene synthase) and traces of (-)-spiroviolene (EC 4.2.3.158, (-)-spiroviolene synthase).
 288014  2024-02-24 18:03:10  3.5.99.15  entry  comments  The enzyme from the leaves of Alangium lamarckii differs in enantiomeric specificity from EC 3.5.99.i, deacetylipecoside synthase. The product is rapidly converted to demethylisoalangiside.  The enzyme from the leaves of Alangium lamarckii differs in enantiomeric specificity from EC 3.5.99.16, deacetylipecoside synthase. The product is rapidly converted to demethylisoalangiside.
 288010  2024-02-24 18:03:08  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.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 3.2.1.224, D-arabinan exo beta-(1,2)-arabinofuranosidase (non-reducing end); cf. EC 3.2.1.226, D-arabinan endo alpha-(1,5)-arabinofuranosidase.
 288006  2024-02-24 18:03:07  3.2.1.224  entry  comments  The enzyme, characterized from the bacterium Microbacterium arabinogalactanolyticum, hydrolyses beta-D-arabinofuranosides from the non-reducing terminal of 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 3.2.1.185, non-reducing end beta-L-arabinofuranosidase; EC 3.2.1.bj, D-arabinan exo alpha-(1,3)/(1,5)-arabinofuranosidase (non-reducing end); and EC 3.2.1.bk, D-arabinan endo alpha-(1,5)-arabinofuranosidase.  The enzyme, characterized from the bacterium Microbacterium arabinogalactanolyticum, hydrolyses beta-D-arabinofuranosides from the non-reducing terminal of 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 3.2.1.185, non-reducing end beta-L-arabinofuranosidase; EC 3.2.1.225, D-arabinan exo alpha-(1,3)/(1,5)-arabinofuranosidase (non-reducing end); and EC 3.2.1.226, D-arabinan endo alpha-(1,5)-arabinofuranosidase.

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