|
|
| ID |
Date/Time |
EC/Citation Key |
Table |
Field |
Changed From |
Changed To |
| 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 |
| 288057 |
2024-02-24 18:03:42 |
4.3.3.4 |
hist |
note |
deacetylipecoside synthase. Now EC 3.5.99.i, deacetylipecoside synthase |
deacetylipecoside synthase. Now EC 3.5.99.16, deacetylipecoside synthase |
| 288056 |
2024-02-24 18:03:40 |
4.3.3.3 |
hist |
note |
deacetylisoipecoside synthase. Now EC 3.5.99.h, deacetylisoipecoside synthase |
deacetylisoipecoside synthase. Now EC 3.5.99.15, deacetylisoipecoside synthase |
| 288054 |
2024-02-24 18:03:39 |
4.3.3.2 |
hist |
note |
strictosidine synthase. Now EC 3.5.99.f, strictosidine synthase |
strictosidine synthase. Now EC 3.5.99.13, strictosidine synthase |
| 288053 |
2024-02-24 18:03:38 |
4.2.1.78 |
hist |
note |
(S)-norcoclaurine synthase. Now 3.5.99.g, (S)-norcoclaurine synthase |
(S)-norcoclaurine synthase. Now 3.5.99.14, (S)-norcoclaurine synthase |
| 288052 |
2024-02-24 18:03:37 |
2.1.1.86 |
hist |
note |
tetrahydromethanopterin S-methyltransferase. Now EC 7.2.1.f, tetrahydromethanopterin S-methyltransferase |
tetrahydromethanopterin S-methyltransferase. Now EC 7.2.1.4, tetrahydromethanopterin 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. |
| 288002 |
2024-02-24 18:03:06 |
2.6.1.125 |
entry |
comments |
Requires pyridoxal 5'-phosphate. The enzyme, characterized from several bacterial species, is known to participate in L-arginine degradation and in the biosynthesis of the rare amino acid (3R)-3-methyl-L-arginine. The enzyme from Streptomyces arginensis also catalyses the activity of EC 2.6.1.aq, L-aspartate:5-guanidino-3-methyl-2-oxopentanoate transaminase. |
Requires pyridoxal 5'-phosphate. The enzyme, characterized from several bacterial species, is known to participate in L-arginine degradation and in the biosynthesis of the rare amino acid (3R)-3-methyl-L-arginine. The enzyme from Streptomyces arginensis also catalyses the activity of EC 2.6.1.126, L-aspartate:5-guanidino-3-methyl-2-oxopentanoate transaminase. |
| 287998 |
2024-02-24 18:03:05 |
2.5.1.158 |
entry |
comments |
This activity has been characterized from a number of fungal bifunctional enzymes. Following the formation of hexaprenyl diphosphate, a different domain in the enzymes catalyses its cyclization into a triterpene (see EC 4.2.3.gl, macrophomene synthase and EC 4.2.3.gk, talaropentaene synthase). cf. EC 2.5.1.82, hexaprenyl diphosphate synthase [geranylgeranyl-diphosphate specific]. |
This activity has been characterized from a number of fungal bifunctional enzymes. Following the formation of hexaprenyl diphosphate, a different domain in the enzymes catalyses its cyclization into a triterpene (see EC 4.2.3.221, macrophomene synthase and EC 4.2.3.220, talaropentaene synthase). cf. EC 2.5.1.82, hexaprenyl diphosphate synthase [geranylgeranyl-diphosphate specific]. |
| 287993 |
2024-02-24 18:02:56 |
4.2.3.8 |
entry |
diagram |
For diagram of the biosynthesis of cembrene and casbene, {terp/cembr} |
For diagram of cembrene and related diterpenoids, {terp/cembrene} |
| 287969 |
2024-02-24 18:02:55 |
4.2.2.28 |
entry |
comments |
The enzyme, characterized from the phytopathogenic fungus Fusarium oxysporum, removes the rhamnosyl residue from alpha-L-rhamnosyl-(1->4)-beta-D-glucuronate or from oligosaccharides that contain this motif at the non-reducing end, leaving an unsaturated glucuronate residue. Among its natural substrates is the type II arabinogalactan component of gum arabic. |
The enzyme, characterized from the phytopathogenic fungus Fusarium oxysporum, removes the rhamnosyl residue from alpha-L-rhamnosyl-(1->4)-D-glucuronate or (with lower activity) from oligosaccharides that contain this motif at the non-reducing end, leaving an unsaturated glucuronate residue. Among its natural substrates is the type II arabinogalactan component of gum arabic. |
| 287968 |
2024-02-24 18:02:55 |
4.2.2.28 |
entry |
sys_name |
alpha-L-rhamnosyl-(1->4)-beta-D-glucuronate lyase |
alpha-L-rhamnosyl-(1->4)-D-glucuronate lyase |
| 287967 |
2024-02-24 18:02:55 |
4.2.2.28 |
entry |
reaction |
an alpha-L-rhamnose-(1->4)-beta-D-glucuronide = alpha-L-rhamnopyranose + a 4-deoxy-alpha-L-threo-hex-4-enopyranuronoside |
alpha-L-rhamnosyl-(1->4)-D-glucuronate = L-rhamnopyranose + 4-deoxy-L-threo-hex-4-enopyranuronate |
| 287966 |
2024-02-24 18:02:55 |
4.2.2.28 |
entry |
accepted_name |
alpha-L-rhamnosyl-(1->4)-beta-D-glucuronate lyase |
alpha-L-rhamnosyl-(1->4)-D-glucuronate lyase |
| 287962 |
2024-02-24 18:02:55 |
2.1.1.243 |
entry |
glossary |
5-guanidino-2-oxopentanoate = 2-ketoarginine
5-guanidino-3-methyl-2-oxopentanoate = 5-carbamimidamido-3-methyl-2-oxopentanoate |
5-guanidino-2-oxopentanoate = 2-ketoarginine
(3R)-5-guanidino-3-methyl-2-oxopentanoate = (3R)-5-carbamimidamido-3-methyl-2-oxopentanoate |
| 287953 |
2024-02-24 18:02:55 |
2.1.1.243 |
entry |
comments |
The enzyme is involved in production of the rare amino acid 3-methylarginine, which is used by the epiphytic bacterium Pseudomonas syringae pv. syringae as an antibiotic against the related pathogenic species Pseudomonas syringae pv. glycinea. |
The enzyme is involved in production of the rare amino acid (3R)-3-methyl-L-arginine. The compound is used by the epiphytic bacterium Pseudomonas syringae pv. syringae as an antibiotic against the related pathogenic species Pseudomonas savastanoi pv. glycinea. Other bacteria incorporate the compound into more complex compounds such as the peptidyl nucleoside antibiotic arginomycin. |
| 287952 |
2024-02-24 18:02:54 |
2.1.1.243 |
entry |
sys_name |
S-adenosyl-L-methionine:5-carbamimidamido-2-oxopentanoate S-methyltransferase |
S-adenosyl-L-methionine:5-guanidino-2-oxopentanoate (3R)-methyltransferase |
| 287951 |
2024-02-24 18:02:54 |
2.1.1.243 |
entry |
other_names |
mrsA (gene name) |
mrsA (gene name); argN (gene name); 2-ketoarginine methyltransferase |
| 287950 |
2024-02-24 18:02:54 |
2.1.1.243 |
entry |
reaction |
S-adenosyl-L-methionine + 5-guanidino-2-oxopentanoate = S-adenosyl-L-homocysteine + 5-guanidino-3-methyl-2-oxopentanoate |
S-adenosyl-L-methionine + 5-guanidino-2-oxopentanoate = S-adenosyl-L-homocysteine + (3R)-5-guanidino-3-methyl-2-oxopentanoate |
| 287949 |
2024-02-24 18:02:54 |
2.1.1.243 |
entry |
accepted_name |
2-ketoarginine methyltransferase |
5-guanidino-2-oxopentanoate (3R)-methyltransferase |
| 287945 |
2024-02-24 18:02:53 |
1.1.1.226 |
entry |
glossary |
|
trans-4-hydroxycyclohexane-1-carboxylate = trans-4-hydroxycyclohexanecarboxylate
4-oxocyclohexane-1-carboxylate = 4-oxocyclohexanecarboxylate |
| 287936 |
2024-02-24 18:02:53 |
1.1.1.226 |
entry |
comments |
The enzyme from Corynebacterium cyclohexanicum is highly specific for the trans-4-hydroxy derivative. |
The enzyme from Corynebacterium cyclohexanicum is highly specific for the trans-4-hydroxy derivative. cf. EC 1.1.1.438, cis-4-hydroxycyclohexanecarboxylate dehydrogenase. |
| 287935 |
2024-02-24 18:02:53 |
1.1.1.226 |
entry |
sys_name |
trans-4-hydroxycyclohexanecarboxylate:NAD+ 4-oxidoreductase |
trans-4-hydroxycyclohexane-1-carboxylate:NAD+ 4-oxidoreductase |
| 287934 |
2024-02-24 18:02:53 |
1.1.1.226 |
entry |
other_names |
trans-4-hydroxycyclohexanecarboxylate dehydrogenase |
4-hydroxycyclohexanecarboxylate dehydrogenase (ambiguous); chcB1 (gene name) |
| 287933 |
2024-02-24 18:02:53 |
1.1.1.226 |
entry |
reaction |
trans-4-hydroxycyclohexanecarboxylate + NAD+ = 4-oxocyclohexanecarboxylate + NADH + H+ |
trans-4-hydroxycyclohexane-1-carboxylate + NAD+ = 4-oxocyclohexane-1-carboxylate + NADH + H+ |
| 287932 |
2024-02-24 18:02:53 |
1.1.1.226 |
entry |
accepted_name |
4-hydroxycyclohexanecarboxylate dehydrogenase |
trans-4-hydroxycyclohexanecarboxylate dehydrogenase |
| 287928 |
2024-02-24 18:02:52 |
7.2.1.4 |
entry |
glossary |
|
CoM = {glossary/CoM::coenzyme M} = 2-sulfanylethane-1-sulfonate
{glossary/methanop::tetrahydromethanopterin} = 1-(4-{(1R)-1-[(6S,7S)-2-amino-7-methyl-4-oxo-3,4,5,6,7,8-hexahydropteridin-6-yl]ethylamino}phenyl)-1-deoxy-5-O-{5-O-[(1S)-1,3-dicarboxypropylphosphonato]-alpha-D-ribofuranosyl}-D-ribitol |
| 287919 |
2024-02-24 18:02:52 |
7.2.1.4 |
entry |
cas_num |
|
103406-60-6 |
| 287918 |
2024-02-24 18:02:52 |
7.2.1.4 |
entry |
diagram |
|
For diagram of methane biosynthesis, {misc/methane} |
| 287916 |
2024-02-24 18:02:52 |
7.2.1.4 |
entry |
serial |
|
4 |
| 287915 |
2024-02-24 18:02:52 |
7.2.1.4 |
entry |
subsubclass |
|
1 |
| 287914 |
2024-02-24 18:02:52 |
7.2.1.4 |
entry |
subclass |
|
2 |
| 287913 |
2024-02-24 18:02:52 |
7.2.1.4 |
entry |
class |
|
7 |
| 287912 |
2024-02-24 18:02:52 |
7.2.1.4 |
entry |
links |
|
BRENDA, EAWAG-BBD, EXPASY, KEGG, PDB |
| 287911 |
2024-02-24 18:02:52 |
7.2.1.4 |
entry |
comments |
|
Involved in the formation of methane from CO2 in methanogenic archaea. The reaction involves the export of one or two sodium ions. The enzyme from the archaeon Methanobacterium thermoautotrophicum is a membrane-associated multienzyme complex composed of eight different subunits, and contains a 5\'-hydroxybenzimidazolyl-cobamide cofactor, to which the methyl group is attached during the transfer. A soluble enzyme that is induced by the presence of CO has been reported as well [6]. |
| 287910 |
2024-02-24 18:02:52 |
7.2.1.4 |
entry |
sys_name |
|
5-methyl-5,6,7,8-tetrahydromethanopterin:CoM 2-methyltransferase (Na+-transporting) |
| 287909 |
2024-02-24 18:02:52 |
7.2.1.4 |
entry |
other_names |
|
tetrahydromethanopterin methyltransferase; mtrA-H (gene names); cmtA (gene name); N5-methyltetrahydromethanopterin---coenzyme M methyltransferase; 5-methyl-5,6,7,8-tetrahydromethanopterin:2-mercaptoethanesulfonate 2-methyltransferase |
| 287908 |
2024-02-24 18:02:52 |
7.2.1.4 |
entry |
reaction |
|
5-methyl-5,6,7,8-tetrahydromethanopterin + CoM + 2 Na+[side 1] = 5,6,7,8-tetrahydromethanopterin + 2-(methylsulfanyl)ethane-1-sulfonate + 2 Na+[side 2] |
| 287907 |
2024-02-24 18:02:52 |
7.2.1.4 |
entry |
accepted_name |
|
tetrahydromethanopterin S-methyltransferase |
| 287906 |
2024-02-24 18:02:52 |
7.2.1.4 |
entry |
ec_num |
|
7.2.1.4 |
| 287902 |
2024-02-24 18:02:51 |
6.3.2.64 |
entry |
glossary |
|
bisucaberin B = pre-bisucaberin = 3-[(5-{3-[(5-aminopentyl)(hydroxy)carbamoyl]propanamido}pentyl)(hydroxy)carbamoyl]propanoate
bisucaberin = 1,12-dihydroxy-1,6,12,17-tetrazacyclodocosane-2,5,13,16-tetrone |
| 287892 |
2024-02-24 18:02:51 |
6.3.2.64 |
entry |
serial |
|
64 |
| 287891 |
2024-02-24 18:02:51 |
6.3.2.64 |
entry |
subsubclass |
|
2 |
| 287890 |
2024-02-24 18:02:51 |
6.3.2.64 |
entry |
subclass |
|
3 |
| 287889 |
2024-02-24 18:02:51 |
6.3.2.64 |
entry |
class |
|
6 |
| 287888 |
2024-02-24 18:02:51 |
6.3.2.64 |
entry |
links |
|
BRENDA, EXPASY, IUBMB, KEGG |
| 287887 |
2024-02-24 18:02:51 |
6.3.2.64 |
entry |
comments |
|
Requires Mg2+. The enzyme, characterized from the bacterium Aliivibrio salmonicida, catalyses the last step in the biosynthesis of the siderophore bisucaberin. The enzyme catalyses the reaction in two steps - concatenation of two molecules of N1-hydroxy-N1-succinylcadaverine, followed by cyclization. |
| 287886 |
2024-02-24 18:02:51 |
6.3.2.64 |
entry |
sys_name |
|
N1-hydroxy-N1-succinylcadaverine:N1-hydroxy-N1-succinylcadaverine ligase |
| 287885 |
2024-02-24 18:02:51 |
6.3.2.64 |
entry |
other_names |
|
pubC (gene name); BibC C-terminal domain |
| 287884 |
2024-02-24 18:02:51 |
6.3.2.64 |
entry |
reaction |
|
2 ATP + 2 N1-hydroxy-N1-succinylcadaverine = 2 AMP + 2 diphosphate + bisucaberin (overall reaction);;(1a) ATP + 2 N1-hydroxy-N1-succinylcadaverine = AMP + diphosphate + bisucaberin B;;(1b) ATP + bisucaberin B = AMP + diphosphate + bisucaberin |
| 287883 |
2024-02-24 18:02:51 |
6.3.2.64 |
entry |
accepted_name |
|
bisucaberin synthase |
| 287882 |
2024-02-24 18:02:51 |
6.3.2.64 |
entry |
ec_num |
|
6.3.2.64 |
| 287867 |
2024-02-24 18:02:50 |
6.3.2.63 |
entry |
glossary |
|
putrebactin = 1,11-dihydroxy-1,6,11,16-tetraazacycloicosane-2,5,12,15-tetrone
pre-putrebactin = 4-{[4-({4-[(4-aminobutyl)(hydroxy)amino]-4-oxobutanoyl}amino)butyl](hydroxy)amino}-4-oxobutanoate |
| 287857 |
2024-02-24 18:02:50 |
6.3.2.63 |
entry |
serial |
|
63 |
| 287856 |
2024-02-24 18:02:50 |
6.3.2.63 |
entry |
subsubclass |
|
2 |
| 287855 |
2024-02-24 18:02:50 |
6.3.2.63 |
entry |
subclass |
|
3 |
| 287854 |
2024-02-24 18:02:50 |
6.3.2.63 |
entry |
class |
|
6 |
| 287853 |
2024-02-24 18:02:50 |
6.3.2.63 |
entry |
links |
|
BRENDA, EXPASY, IUBMB, KEGG |
| 287852 |
2024-02-24 18:02:50 |
6.3.2.63 |
entry |
comments |
|
Requires Mg2+. The enzyme, characterized from the bacteria Shewanella spp. MR-4 and MR-7, catalyse the last step in the biosynthesis of the siderophore putrebactin. The enzyme catalyses the reaction in two steps - concatenation of two molecules of N1-hydroxy-N1-succinylputrescine, followed by cyclization. |
| 287851 |
2024-02-24 18:02:50 |
6.3.2.63 |
entry |
sys_name |
|
N1-hydroxy-N1-succinylputrescine:N1-hydroxy-N1-succinylputrescine ligase |
| 287850 |
2024-02-24 18:02:50 |
6.3.2.63 |
entry |
other_names |
|
pubC (gene name) |
| 287849 |
2024-02-24 18:02:50 |
6.3.2.63 |
entry |
reaction |
|
2 ATP + 2 N1-hydroxy-N1-succinylputrescine = 2 AMP + 2 diphosphate + putrebactin (overall reaction);;(1a) ATP + 2 N1-hydroxy-N1-succinylputrescine = AMP + diphosphate + pre-putrebactin;;(1b) ATP + pre-putrebactin = AMP + diphosphate + putrebactin |
| 287848 |
2024-02-24 18:02:50 |
6.3.2.63 |
entry |
accepted_name |
|
putrebactin synthase |
| 287847 |
2024-02-24 18:02:50 |
6.3.2.63 |
entry |
ec_num |
|
6.3.2.63 |
