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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
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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 |
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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 |
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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 |
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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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