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
 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

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