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
 270932  2021-12-01 07:51:03  2.7.1.16  entry  diagram    For diagram of <small>L</small>-Arabinose catabolism, {polysacc/AraCat}
 270930  2021-12-01 07:51:01  2.7.1.101  entry  diagram    For diagram of tagatose metabolism, {polysacc/tagatose}
 270928  2021-12-01 07:50:59  2.5.1.147  entry  diagram    For diagram of coenzyme F<small><sub>420</sub></small> biosynthesis, {misc/F420}
 270927  2021-12-01 07:50:58  2.4.1.385  entry  diagram    For diagram of <em>all</em>-<em>cis</em>-polyprenyl diphosphate, {terp/withanolide}
 270926  2021-12-01 07:50:56  2.4.1.369  entry  diagram    For diagram of glucosyl enterobactin biosynthesis, {misc/GlcEnterob}
 270925  2021-12-01 07:50:54  2.4.1.367  entry  diagram    For diagram of protopanaxatriol glucoside biosynthesis, {terp/protopanaxT}
 270924  2021-12-01 07:50:52  2.4.1.366  entry  diagram    For diagram of protopanaxatriol glucoside biosynthesis, {terp/protopanaxT}
 270923  2021-12-01 07:50:50  2.4.1.365  entry  diagram    For diagram of protopanaxadiol glucoside biosynthesis, {terp/protopanaxD}
 270922  2021-12-01 07:50:48  2.4.1.364  entry  diagram    For diagram of protopanaxadiol glucoside biosynthesis, {terp/protopanaxD}
 270921  2021-12-01 07:38:24  2.4.1.363  entry  diagram    For diagram of protopanaxadiol glucoside biosynthesis, {terp/protopanaxD}
 270920  2021-12-01 07:38:22  2.4.1.360  entry  diagram    For diagram of vitexin and isovitexin derivatives biosynthesis, {phenol/vitexin}
 270918  2021-12-01 07:38:20  2.4.1.358  entry  diagram    For diagram of phloroisovalerophenone 2-<em>o</em>-glucoside biosynthesis, {phenol/phloroisoval}
 270916  2021-12-01 07:38:17  2.3.1.290  entry  diagram    For diagram of 4-Nitrobenzoyl-CoA antibiotics biosynthesis, {misc/nitrobenz}
 270915  2021-12-01 07:38:15  2.3.1.289  entry  diagram    For diagram of 4-Nitrobenzoyl-CoA antibiotics biosynthesis, {misc/nitrobenz}
 270913  2021-12-01 07:38:13  2.3.1.281  entry  diagram    For diagram of polyketides biosynthesis, {phenol/polyketide}
 270912  2021-12-01 07:38:11  2.1.1.380  entry  diagram    For diagram of cremeomycin biosynthesis, {misc/cremeomycin}
 270911  2021-12-01 07:38:09  2.1.1.353  entry  diagram    For diagram of aureothin catabolism, {misc/aureothin}
 270909  2021-12-01 07:38:06  2.1.1.352  entry  diagram    For diagram of noscapine biosynthesis, {alkaloid/noscapine}
 270907  2021-12-01 07:38:04  2.1.1.350  entry  diagram    For diagram of the vitamin K cycle, {misc/vitKcycle}
 270905  2021-12-01 07:38:00  2.1.1.349  entry  diagram    For diagram of toxoflavin biosynthesis, {misc/toxoflavin}
 270904  2021-12-01 07:37:57  1.5.1.52  entry  diagram    For diagram of staphylopine biosynthesis, {AminoAcid/staphylopine}
 270902  2021-12-01 07:37:55  1.4.7.1  entry  diagram    For diagram of glutamic acid biosynthesis, {AminoAcid/Glu}
 270900  2021-12-01 07:37:53  1.4.1.14  entry  diagram    For diagram of glutamic acid biosynthesis, {AminoAcid/Glu}
 270899  2021-12-01 07:37:51  1.4.1.13  entry  diagram    For diagram of glutamic acid biosynthesis, {AminoAcid/Glu}
 270898  2021-12-01 07:37:47  1.3.5.3  entry  diagram    For diagram of porphyrin biosynthesis (later stages), {tetrapyr/porphyrin2}
 270896  2021-12-01 07:37:45  1.3.1.119  entry  diagram    For diagram of chlorobenzene catabolism, {misc/ClC6H5}
 270893  2021-12-01 07:37:41  1.2.1.26  entry  diagram    For diagram of <small>L</small>-Arabinose catabolism, {polysacc/AraCat} and for diagram of <small>D</small>-Arabinose catabolism, {polysacc/AraCat2}
 270890  2021-12-01 07:37:36  1.2.1.21  entry  diagram    For diagram of <small>L</small>-Arabinose catabolism, {polysacc/AraCat}
 270889  2021-12-01 07:37:34  1.17.99.10  entry  diagram    For diagram of cholic acid biosynthesis (sidechain), {terp/sidechain2}
 270887  2021-12-01 07:37:31  1.14.99.64  entry  diagram    For diagram of astaxanthin biosynthesis, {terp/astaxanthin}
 270886  2021-12-01 07:37:28  1.14.99.46  entry  diagram    For diagram of pyrimidine catabolism, {misc/pyrimcat}
 270884  2021-12-01 07:37:25  1.14.14.159  entry  diagram    For diagram of dolabradiene biosynthesis, {terp/dolabra}
 270883  2021-12-01 07:37:23  1.14.13.249  entry  diagram    For diagram of cremeomycin biosynthesis, {misc/cremeomycin}
 270881  2021-12-01 07:37:01  1.13.11.5  entry  diagram    For diagram of tyrosine catabolism, {AminoAcid/TyrCat}
 270880  2021-11-24 14:12:09  2.7.1.234  cite  cite_key    van-der-heiden-e-2015-106
 270879  2021-11-24 14:12:09  2.7.1.234  cite  ref_num    2
 270878  2021-11-24 14:12:09  2.7.1.234  cite  cite_key    shakeri-garakani-a-2004-717
 270877  2021-11-24 14:12:09  2.7.1.234  cite  ref_num    1
 270872  2021-11-24 14:12:09  2.7.1.234  entry  comments  The enzyme has been pruified from the bacterium Bacillus licheniformis and is part of a D-tagatose catabolic pathway.  The enzyme, which has been purified from the bacteria Klebsiella oxytoca and Bacillus licheniformis, is part of a D-tagatose catabolic pathway. The substrate, which occurs in a pyranose form in solution, undergoes a change to the furanose conformation after binding to the enzyme, in order permit phosphorylation at C6.The enzyme has been pruified from the bacterium Bacillus licheniformis and is part of a D-tagatose catabolic pathway.
 270871  2021-11-24 14:12:09  2.7.1.234  entry  sys_name  ATP:D-tagatose-1-phosphate 6-phosphotransferase  ATP:D-tagatopyranse-1-phosphate 6-phosphotransferase
 270870  2021-11-24 14:12:09  2.7.1.234  entry  reaction  ATP + D-tagatose 1-phosphate = ADP + D-tagatose 1,6-bisphosphate  ATP + D-tagatopyranose 1-phosphate = ADP + D-tagatofuranose 1,6-bisphosphate
 270865  2021-11-22 13:12:53  2.6.1.123  entry  comments  The enzyme, characterized from the bacterium Bacillus subtilis, is a heterodimer. The PabA subunit hydrolyses L-glutamine to L-glutamate and NH3 (cf. EC 3.5.1.2, glutaminase), which is channeled to the PabB active site. PabB catalyses the formation of 4-amino-4-deoxychorismate from chorismate in two steps, via the intermediate 2-amino-4-deoxychorismate. cf. EC 2.6.1.85, aminodeoxychorismate synthase.  The enzyme, characterized from the bacterium Bacillus subtilis, is a heterodimer. The PabA subunit acts successively on two molecules of L-glutamine, hydrolysing each to L-glutamate and ammonia (cf. EC 3.5.1.2, glutaminase). The ammonia molecules are channeled to the active site of PabB, which catalyses the formation of 4-amino-4-deoxychorismate from chorismate in two steps via the intermediate 2-amino-4-deoxychorismate. cf. EC 2.6.1.85, aminodeoxychorismate synthase.
 270864  2021-11-22 13:12:53  2.6.1.123  entry  other_names  ADCS (ambiguous); ADC synthase (ambiguous)  ADCS (ambiguous); ADC synthase (ambiguous); pabAB (gene names)
 270863  2021-11-22 13:12:53  2.6.1.123  entry  reaction  chorismate + 2 L-glutamine + H2O = 4-amino-4-deoxychorismate + 2 L-glutamate + ammonia (overall reaction);;(1a) chorismate + L-glutamine = (2S)-2-amino-4-deoxychorismate + L-glutamate;;(1b) (2S)-2-amino-4-deoxychorismate + L-glutamine + H2O = 4-amino-4-deoxychorismate + L-glutamate + ammonia  chorismate + 2 L-glutamine + H2O = 4-amino-4-deoxychorismate + 2 L-glutamate + ammonia (overall reaction);;(1a) 2 L-glutamine + 2 H2O = 2 L-glutamate + 2 NH3;;(1b) chorismate + NH3 = (2S)-2-amino-4-deoxychorismate + H2O;;(1c) (2S)-2-amino-4-deoxychorismate + NH3 = 4-amino-4-deoxychorismate + NH3
 270861  2021-11-21 14:43:10  2.6.1.123  entry  comments  The enzyme, characterized from the bacterium Bacillus subtilis, is a heterodimer. The PabA component is a glutamine amidotransferase that hydrolyses glutamine to glutamate, forming ammonia, which is channeled to the PabB active site. PabB catalyses the formation of 4-amino-4-deoxychorismate from chorismate in two steps, via the intermediate 2-amino-4-deoxychorismate. cf. EC 2.6.1.85, aminodeoxychorismate synthase.  The enzyme, characterized from the bacterium Bacillus subtilis, is a heterodimer. The PabA subunit hydrolyses L-glutamine to L-glutamate and NH3 (cf. EC 3.5.1.2, glutaminase), which is channeled to the PabB active site. PabB catalyses the formation of 4-amino-4-deoxychorismate from chorismate in two steps, via the intermediate 2-amino-4-deoxychorismate. cf. EC 2.6.1.85, aminodeoxychorismate synthase.
 270857  2021-11-19 11:01:23  5.6.2.4  entry  comments  Helicases are motor proteins that can transiently catalyse the unwinding of energetically stable duplex DNA or RNA molecules by using ATP hydrolysis as the source of energy (although other nucleoside triphosphates can replace ATP in some cases). DNA helicases unwind duplex DNA and are involved in replication, repair, recombination, transcription, pre-rRNA processing, and translation initiation. Mechanistically, DNA helicases are divided into those that can translocate in the 3'-5' direction and those that translocate in the 5'-3' direction with respect to the strand on which they initially bind. This entry describes a number of DNA helicases that translocate in the 3'-5' direction. Many of the enzymes require a 3' single-stranded DNA tail. The Rep protein is a component of the bacterial replisome, providing a replication fork-specific motor. The UvrD enzyme, found in Gram-negative bacteria, is involved in maintenance of chromosomal integrity. The RecQ proteins are a family of eukaryotic helicases that are involved in DNA replication, transcription and repair. The Mer3 helicase, found in fungi and plants, is required for crossover formation during meiosis. cf. EC 5.6.2.c, DNA 5'-3' helicase.  Helicases are motor proteins that can transiently catalyse the unwinding of energetically stable duplex DNA or RNA molecules by using ATP hydrolysis as the source of energy (although other nucleoside triphosphates can replace ATP in some cases). DNA helicases unwind duplex DNA and are involved in replication, repair, recombination, transcription, pre-rRNA processing, and translation initiation. Mechanistically, DNA helicases are divided into those that can translocate in the 3'-5' direction and those that translocate in the 5'-3' direction with respect to the strand on which they initially bind. This entry describes a number of DNA helicases that translocate in the 3'-5' direction. Many of the enzymes require a 3' single-stranded DNA tail. The Rep protein is a component of the bacterial replisome, providing a replication fork-specific motor. The UvrD enzyme, found in Gram-negative bacteria, is involved in maintenance of chromosomal integrity. The RecQ proteins are a family of eukaryotic helicases that are involved in DNA replication, transcription and repair. The Mer3 helicase, found in fungi and plants, is required for crossover formation during meiosis. cf. EC 5.6.2.3, DNA 5'-3' helicase.
 270854  2021-11-18 07:14:01  2.7.1.235  entry  glossary  Lipid A is a lipid component of the lipopolysaccharides (LPS) of Gram-negative bacteria. It usually consists of two glucosamine units connected by a beta(1->6) bond and decorated with four to seven acyl chains and up to two phosphate groups. Hep = L-glycero-beta-D-manno-heptose. Hep I refers to the first heptose added to the lipid, in a reaction catalysed by EC 2.4.99.l, lipopolysaccharide heptosyltransferase I.  Lipid A is a lipid component of the lipopolysaccharides (LPS) of Gram-negative bacteria. It usually consists of two glucosamine units connected by a beta(1->6) bond and decorated with four to seven acyl chains and up to two phosphate groups. Hep = L-glycero-beta-D-manno-heptose
 270852  2021-11-18 07:08:48  5.6.2.4  entry  comments  Helicases are motor proteins that can transiently catalyse the unwinding of energetically stable duplex DNA or RNA molecules by using ATP hydrolysis as the source of energy (although other nucleoside triphosphates can replace ATP in some cases). DNA helicases unwind duplex DNA and are involved in replication, repair, recombination, transcription, pre-rRNA processing, and translation initiation. Mechanistically, DNA helicases are divided into those that can translocate in the 3'-5' direction and those that translocate in the 5'3' direction with respect to the strand on which they initially bind. This entry describes a number of DNA helicases that translocate in the 3'-5' direction. Many of the enzymes require a 3' single-stranded DNA tail. The Rep protein is a component of the bacterial replisome, providing a replication fork-specific motor. The UvrD enzyme, found in Gram-negative bacteria, is involved in maintenance of chromosomal integrity. The RecQ proteins are a family of eukaryotic helicases that are involved in DNA replication, transcription and repair. The Mer3 helicase, found in fungi and plants, is required for crossover formation during meiosis. cf. EC 5.6.2.c, DNA 5'-3' helicase.  Helicases are motor proteins that can transiently catalyse the unwinding of energetically stable duplex DNA or RNA molecules by using ATP hydrolysis as the source of energy (although other nucleoside triphosphates can replace ATP in some cases). DNA helicases unwind duplex DNA and are involved in replication, repair, recombination, transcription, pre-rRNA processing, and translation initiation. Mechanistically, DNA helicases are divided into those that can translocate in the 3'-5' direction and those that translocate in the 5'-3' direction with respect to the strand on which they initially bind. This entry describes a number of DNA helicases that translocate in the 3'-5' direction. Many of the enzymes require a 3' single-stranded DNA tail. The Rep protein is a component of the bacterial replisome, providing a replication fork-specific motor. The UvrD enzyme, found in Gram-negative bacteria, is involved in maintenance of chromosomal integrity. The RecQ proteins are a family of eukaryotic helicases that are involved in DNA replication, transcription and repair. The Mer3 helicase, found in fungi and plants, is required for crossover formation during meiosis. cf. EC 5.6.2.c, DNA 5'-3' helicase.
 270850  2021-11-18 07:08:23  5.6.2.4  entry  comments  Helicases are motor proteins that can transiently catalyse the unwinding of energetically stable duplex DNA or RNA molecules by using ATP hydrolysis as the source of energy (although other nucleoside triphosphates can replace ATP in some cases). DNA helicases unwind duplex DNA and are involved in replication, repair, recombination, transcription, pre-rRNA processing, and translation initiation. Mechanistically, DNA helicases are divided into those that can translocate in the 3'5' direction and those that translocate in the 5'3' direction with respect to the strand on which they initially bind. This entry describes a number of DNA helicases that translocate in the 3'-5' direction. Many of the enzymes require a 3' single-stranded DNA tail. The Rep protein is a component of the bacterial replisome, providing a replication fork-specific motor. The UvrD enzyme, found in Gram-negative bacteria, is involved in maintenance of chromosomal integrity. The RecQ proteins are a family of eukaryotic helicases that are involved in DNA replication, transcription and repair. The Mer3 helicase, found in fungi and plants, is required for crossover formation during meiosis. cf. EC 5.6.2.3, DNA 5'-3' helicase.  Helicases are motor proteins that can transiently catalyse the unwinding of energetically stable duplex DNA or RNA molecules by using ATP hydrolysis as the source of energy (although other nucleoside triphosphates can replace ATP in some cases). DNA helicases unwind duplex DNA and are involved in replication, repair, recombination, transcription, pre-rRNA processing, and translation initiation. Mechanistically, DNA helicases are divided into those that can translocate in the 3'-5' direction and those that translocate in the 5'3' direction with respect to the strand on which they initially bind. This entry describes a number of DNA helicases that translocate in the 3'-5' direction. Many of the enzymes require a 3' single-stranded DNA tail. The Rep protein is a component of the bacterial replisome, providing a replication fork-specific motor. The UvrD enzyme, found in Gram-negative bacteria, is involved in maintenance of chromosomal integrity. The RecQ proteins are a family of eukaryotic helicases that are involved in DNA replication, transcription and repair. The Mer3 helicase, found in fungi and plants, is required for crossover formation during meiosis. cf. EC 5.6.2.c, DNA 5'-3' helicase.
 270843  2021-11-18 07:01:56  2.3.3.21  entry  glossary  (2R)-2-hydroxy-2-methylbutanedioate = (2R)-2-methylmalate = (-)-citramalate 3-methyl-2-oxobutanoate =alpha-ketoisovalerate 2-oxobutanoate = alpha-ketobutyrate 4-methyl-2-oxopentanoate = alpha-ketoisocaproate 2-oxohexanoate = alpha-ketopimelate 2-oxoglutarate = alpha-ketoglutarate  (2R)-2-hydroxy-2-methylbutanedioate = (2R)-2-methylmalate = (-)-citramalate 3-methyl-2-oxobutanoate = alpha-ketoisovalerate 2-oxobutanoate = alpha-ketobutyrate 4-methyl-2-oxopentanoate = alpha-ketoisocaproate 2-oxohexanoate = alpha-ketopimelate 2-oxoglutarate = alpha-ketoglutarate
 270832  2021-11-17 17:52:00  1.16.3.4  entry  comments  The enzyme, characterized from the bacterium Escherichia coli, is involved in copper tolerance under aerobic conditions. The enzyme contains a substrate binding (type 1) copper site and a trinuclear copper center (consisting of type 2 and type 3 copper sites) in which oxygen binding and reduction takes place. It also contains a methionine rich region that can bind additional copper ions. In vitro, if the substrate binding site is occupied by copper(II), the enzyme can function as a laccase (EC 1.10.3.2) -type quinol oxidase. However, in vivo this site is occupied by a copper(I) ion and the enzyme functions as a cuprous oxidase.  The enzyme, characterized from the bacterium Escherichia coli, is involved in copper tolerance under aerobic conditions. The enzyme contains a substrate binding (type 1) copper site and a trinuclear copper center (consisting of type 2 and type 3 copper sites) in which oxygen binding and reduction takes place. It also contains a methionine rich region that can bind additional copper ions. In vitro, if the substrate binding site is occupied by copper(II), the enzyme can function as a laccase-type quinol oxidase (EC 1.10.3.2). However, in vivo this site is occupied by a copper(I) ion and the enzyme functions as a cuprous oxidase.
 270825  2021-11-17 17:41:09  2.1.1.383  entry  sys_name  L-carnitine:[Co(I) quaternary-amine-specifc corrinoid protein] Co-methyltransferase  L-carnitine:[Co(I) quaternary-amine-specific corrinoid protein] Co-methyltransferase
 270824  2021-11-17 17:41:09  2.1.1.383  entry  reaction  L-carnitine + a [Co(I) quaternary-amine-specifc corrinoid protein] = a [methyl-Co(III) quaternary-amine-specifc corrinoid protein] + L-norcarnitine  L-carnitine + a [Co(I) quaternary-amine-specific corrinoid protein] = a [methyl-Co(III) quaternary-amine-specific corrinoid protein] + L-norcarnitine
 270816  2021-11-17 10:43:44  2.6.1.122  entry  sys_name  UDP-3-acetamido-2-amino-2,3-dideoxy-alpha-D-glucopyranose:2-oxoglutarate aminotransferase  UDP-2-acetamido-3-amino-2,3-dideoxy-alpha-D-glucopyranose:2-oxoglutarate aminotransferase
 270815  2021-11-17 10:43:44  2.6.1.122  entry  reaction  UDP-3-acetamido-2-amino-2,3-dideoxy-alpha-D-glucopyranose + 2-oxoglutarate = UDP-N-acetyl-3-dehydro-alpha-D-glucosamine + L-glutamate  UDP-2-acetamido-3-amino-2,3-dideoxy-alpha-D-glucopyranose + 2-oxoglutarate = UDP-N-acetyl-3-dehydro-alpha-D-glucosamine + L-glutamate

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