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
 228050  2018-07-18 03:38:37  1.14.14.140  entry  comments  A cytochrome P-450 (heme-thiolate) protein. The immediate product is likely 2-hydroxyliquiritigenin, which spontaneously rearranges to form licodione.  A cytochrome P-450 (heme-thiolate) protein isolated from licorice plants (Glycyrrhiza echinata L.). The immediate product is likely 2-hydroxyliquiritigenin, which spontaneously rearranges to form licodione.
 228042  2018-07-16 16:00:04  1.14.15.23  entry  comments  The enzyme, characterized from the bacterium Sphingomonas sp. DC-6, initiates the degradation of several chloroacetanilide herbicides, including alachlor, acetochlor, and butachlor. The enzyme is a Rieske non-heme iron oxygenase, and requires a ferredoxin and EC 1.18.1.3, ferredoxin-NAD+ reductase, for activity.  The enzyme, characterized from the bacterium Sphingomonas sp. DC-6, initiates the degradation of several chloroacetanilide herbicides, including alachlor, acetochlor, and butachlor. The enzyme is a Rieske non-heme iron oxygenase, and requires a ferredoxin and EC 1.18.1.3, ferredoxin---NAD+ reductase, for activity.
 228041  2018-07-16 16:00:04  1.14.15.23  entry  reaction  butachlor + 2 reduced ferredoxin [iron-sulfur] cluster + O2 = 2-chloro-N-(2,6-diethylphenyl)acetamide + butyl formate + 2 reduced ferredoxin [iron-sulfur] cluster + H2O  butachlor + 2 reduced ferredoxin [iron-sulfur] cluster + O2 = 2-chloro-N-(2,6-diethylphenyl)acetamide + butyl formate + 2 oxidized ferredoxin [iron-sulfur] cluster + H2O
 228039  2018-07-16 04:32:52  1.14.14.154  entry  other_names  obtusufoliol 14-demethylase; lanosterol 14-demethylase; lanosterol 14alpha-demethylase; sterol 14-demethylase  obtusufoliol 14-demethylase; lanosterol 14-demethylase; lanosterol 14alpha-demethylase; sterol 14-demethylase; CYP51
 228037  2018-07-13 10:03:32  1.14.14.153  entry  reaction  indole + [reduced NADPH---hemoprotein reductase] + O2 = indolin-2-one + [reduced NADPH---hemoprotein reductase] + H2O  indole + [reduced NADPH---hemoprotein reductase] + O2 = indolin-2-one + [oxidized NADPH---hemoprotein reductase] + H2O
 228034  2018-07-13 09:20:25  1.13.12.24  entry  comments  Ca2+-regulated photoproteins are found in a variety of bioluminescent marine organisms, mostly coelenterates, and are responsible for their light emission. The best studied enzyme is from the jellyfish Aequorea victoria. The enzyme tightly binds the imidazolopyrazinone derivative coelenterazine, which is then peroxidized by oxygen. The hydroperoxide is stably bound until three Ca2+ ions bind to the protein, inducing a structural change that results in the formation of a 1,2-dioxetan-3-one ring, followed by decarboxylation and generation of a protein-bound coelenteramide in an excited state. The calcium-bound protein-product complex is known as a blue fluorescent protein. In vivo the energy is transferred to a green fluorescent protein (GFP) by Förster resonance energy transfer. In vitro, in the absence of GFP, coelenteramide emits a photon of blue light while returning to its ground state.  Ca2+-regulated photoproteins are found in a variety of bioluminescent marine organisms, mostly coelenterates, and are responsible for their light emission. The best studied enzyme is from the jellyfish Aequorea victoria. The enzyme tightly binds the imidazolopyrazinone derivative coelenterazine, which is then peroxidized by oxygen. The hydroperoxide is stably bound until three Ca2+ ions bind to the protein, inducing a structural change that results in the formation of a 1,2-dioxetan-3-one ring, followed by decarboxylation and generation of a protein-bound coelenteramide in an excited state. The calcium-bound protein-product complex is known as a blue fluorescent protein. In vivo the energy is transferred to a green fluorescent protein (GFP) by Forster resonance energy transfer. In vitro, in the absence of GFP, coelenteramide emits a photon of blue light while returning to its ground state.
 228032  2018-07-12 03:57:43  1.14.19.70  entry  other_names  CYP121; rv2276 (gene name)  CYP121; rv2276 (locus name)
 228030  2018-07-12 03:30:43  1.14.19.62  entry  comments  A P-450 (heme-thiolate) protein. Secologanin is the precursor of the monoterpenoid indole alkaloids and ipecac alkaloids.  A cytochrome P-450 (heme-thiolate) protein. Secologanin is the precursor of the monoterpenoid indole alkaloids and ipecac alkaloids.
 228028  2018-07-10 03:26:08  1.14.19.65  entry  other_names  CYP719A14 (gene name); (S)-scoulerine oxidase (methylenedioxy-bridge-forming) (ambiguous); (S)-scoulerine,NADPH:oxygen oxidoreductase (methylenedioxy-bridge-forming) (ambiguous)  CYP719A14 (gene name); (S)-scoulerine oxidase (methylenedioxy-bridge-forming) (ambiguous)
 228027  2018-07-09 15:09:30  7.6.2  class  heading    Linked to the hydrolysis of a nucleoside triphosphate
 228026  2018-07-09 15:09:30  7.6.2  class  subsubclass    2
 228025  2018-07-09 15:09:30  7.6.2  class  subclass    6
 228024  2018-07-09 15:09:30  7.6.2  class  class    7
 228023  2018-07-09 13:06:41  7.5.2  class  heading    Linked to the hydrolysis of a nucleoside triphosphate
 228022  2018-07-09 13:06:41  7.5.2  class  subsubclass    2
 228021  2018-07-09 13:06:41  7.5.2  class  subclass    5
 228020  2018-07-09 13:06:41  7.5.2  class  class    7
 228019  2018-07-09 13:06:06  7.4.2  class  heading    Linked to the hydrolysis of a nucleoside triphosphate
 228018  2018-07-09 13:06:06  7.4.2  class  subsubclass    2
 228017  2018-07-09 13:06:06  7.4.2  class  subclass    4
 228016  2018-07-09 13:06:06  7.4.2  class  class    7
 228015  2018-07-09 13:05:39  7.3.2  class  heading    Linked to the hydrolysis of a nucleoside triphosphate
 228014  2018-07-09 13:05:39  7.3.2  class  subsubclass    2
 228013  2018-07-09 13:05:39  7.3.2  class  subclass    3
 228012  2018-07-09 13:05:39  7.3.2  class  class    7
 228011  2018-07-09 13:05:23  7.2.4  class  heading    Linked to decarboxylation
 228010  2018-07-09 13:05:23  7.2.4  class  subsubclass    4
 228009  2018-07-09 13:05:23  7.2.4  class  subclass    2
 228008  2018-07-09 13:05:23  7.2.4  class  class    7
 228007  2018-07-09 13:04:15  7.2.3  class  heading    Hydron translocation linked to the hydrolysis of diphosphate
 228006  2018-07-09 13:04:15  7.2.3  class  subsubclass    3
 228005  2018-07-09 13:04:15  7.2.3  class  subclass    2
 228004  2018-07-09 13:04:15  7.2.3  class  class    7
 228003  2018-07-09 13:03:56  7.2.2  class  heading    Linked to the hydrolysis of a nucleoside triphosphate
 228002  2018-07-09 13:03:56  7.2.2  class  subsubclass    2
 228001  2018-07-09 13:03:56  7.2.2  class  subclass    2
 228000  2018-07-09 13:03:56  7.2.2  class  class    7
 227999  2018-07-09 13:03:39  7.2.1  class  heading    Linked to oxidoreductase reactions
 227998  2018-07-09 13:03:39  7.2.1  class  subsubclass    1
 227997  2018-07-09 13:03:39  7.2.1  class  subclass    2
 227996  2018-07-09 13:03:39  7.2.1  class  class    7
 227995  2018-07-09 13:03:12  7.1.3  class  heading    Hydron translocation linked to the hydrolysis of diphosphate
 227994  2018-07-09 13:03:12  7.1.3  class  subsubclass    3
 227993  2018-07-09 13:03:12  7.1.3  class  subclass    1
 227992  2018-07-09 13:03:12  7.1.3  class  class    7
 227991  2018-07-09 13:02:53  7.1.2  class  heading    Hydron translocation linked to the hydrolysis of a nucleoside triphosphate
 227990  2018-07-09 13:02:53  7.1.2  class  subsubclass    2
 227989  2018-07-09 13:02:53  7.1.2  class  subclass    1
 227988  2018-07-09 13:02:53  7.1.2  class  class    7
 227987  2018-07-09 13:02:27  7.1.1  class  heading    Hydron translocation or charge separation linked to oxidoreductase reactions
 227986  2018-07-09 13:02:27  7.1.1  class  subsubclass    1
 227985  2018-07-09 13:02:27  7.1.1  class  subclass    1
 227984  2018-07-09 13:02:27  7.1.1  class  class    7
 227982  2018-07-09 13:00:41  7.6.0  class  heading    Catalysing the translocation of other compounds
 227981  2018-07-09 13:00:41  7.6.0  class  subclass    6
 227980  2018-07-09 13:00:41  7.6.0  class  class    7
 227978  2018-07-09 12:52:37  7.5.0  class  heading    Catalysing the translocation carbohydrates and their derivatives
 227977  2018-07-09 12:52:37  7.5.0  class  subclass    5
 227976  2018-07-09 12:52:37  7.5.0  class  class    7
 227974  2018-07-09 12:49:51  7.4.0  class  heading    Catalysing the translocation amino acids and peptides
 227973  2018-07-09 12:49:51  7.4.0  class  subclass    4
 227972  2018-07-09 12:49:51  7.4.0  class  class    7
 227970  2018-07-09 12:48:47  7.3.0  class  heading    Catalysing the translocation of inorganic anions and their chelates
 227969  2018-07-09 12:48:47  7.3.0  class  subclass    3
 227968  2018-07-09 12:48:47  7.3.0  class  class    7
 227966  2018-07-09 12:48:12  7.2.0  class  heading    Catalysing the translocation of inorganic cations
 227965  2018-07-09 12:48:12  7.2.0  class  subclass    2
 227964  2018-07-09 12:48:12  7.2.0  class  class    7
 227962  2018-07-09 06:00:25  7.0.0  class  heading    Translocases
 227961  2018-07-09 06:00:25  7.0.0  class  class    7
 227960  2018-07-09 05:59:53  7.1.0  class  heading    Catalysing the translocation of hydrons

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