|
ID |
Date/Time |
EC/Citation Key |
Table |
Field |
Changed From |
Changed To |
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 |
287835 |
2024-02-24 18:02:49 |
5.6.2.7 |
entry |
serial |
|
7 |
287834 |
2024-02-24 18:02:49 |
5.6.2.7 |
entry |
subsubclass |
|
2 |
287833 |
2024-02-24 18:02:49 |
5.6.2.7 |
entry |
subclass |
|
6 |
287832 |
2024-02-24 18:02:49 |
5.6.2.7 |
entry |
class |
|
5 |
287831 |
2024-02-24 18:02:49 |
5.6.2.7 |
entry |
links |
|
BRENDA, EXPASY, IUBMB, KEGG |
287830 |
2024-02-24 18:02:49 |
5.6.2.7 |
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. While most RNA helicases utilize a mechanism known as canonical duplex unwinding and translocate along the RNA (cf. EC 5.6.2.5, RNA 5\'-3\' helicase and EC 5.6.2.6, RNA 3\'-5\' helicase), DEAD-box RNA helicases differ by unwinding RNA via the local strand separation mechanism, which does not involve translocation. These helicases load directly on the duplex region, aided by single stranded or structured nucleic acid regions. Upon loading, the DEAD-box protein locally opens the duplex strands. This step requires binding of ATP, which is not hydrolysed. The local helix opening causes the remaining basepairs to dissociate without further action from the enzyme. Unwinding occurs without apparent polarity, and is limited to relatively short distances. ATP hydrolysis is required for release of the DEAD-box protein from the RNA. The name originates from the sequence D-E-A-D, which is found in Motif II of these proteins. |
287829 |
2024-02-24 18:02:49 |
5.6.2.7 |
entry |
sys_name |
|
RNA helicase (non-translocating) |
287828 |
2024-02-24 18:02:49 |
5.6.2.7 |
entry |
other_names |
|
Dbp2; DDX3; DDX4; DDX5; DDX17; DDX3Y; RM62; hDEAD1; RNA helicase Hera; DED1 |
287827 |
2024-02-24 18:02:49 |
5.6.2.7 |
entry |
reaction |
|
ATP + H2O + wound RNA = ADP + phosphate + unwound RNA |
287826 |
2024-02-24 18:02:49 |
5.6.2.7 |
entry |
accepted_name |
|
DEAD-box RNA helicase |
287825 |
2024-02-24 18:02:49 |
5.6.2.7 |
entry |
ec_num |
|
5.6.2.7 |