Escherichia coli K-12 substr. MG1655 Compound: Cu2+

Synonyms: Cu+2, Cu++, cupric ion, cupric copper, Cu(II)

Superclasses: an iona cationan inorganic cationa divalent inorganic cation
an ionan inorganic ionan inorganic cationa divalent inorganic cation

Component of:
copper sulfate pentahydrate
copper sulfate

Chemical Formula: Cu

Molecular Weight: 63.546 Daltons

Monoisotopic Molecular Weight: 62.9296011 Daltons

SMILES: [Cu++]

InChI: InChI=1S/Cu/q+2


Unification Links: ChEBI:29036, ChemSpider:25221, HMDB:HMDB00657, IAF1260:50600, PubChem:27099

Standard Gibbs Free Energy of Change Formation (ΔfG in kcal/mol): 0.0

Reactions known to produce the compound:

Not in pathways:
2 Cu+[periplasm] + 2 H+[periplasm] + oxygen[periplasm] → 2 Cu2+[periplasm] + 2 H2O[periplasm]

In Reactions of unknown directionality:

Not in pathways:
Cu2+ + NADH = Cu+ + NAD+

In Transport reactions:
an ion[periplasm]an ion[extracellular space]

Enzymes inhibited by Cu2+, sorted by the type of inhibition, are:

Inhibitor (Competitive) of: cytosine deaminase [Porter93, Comment 1] Inhibitor (Mechanism unknown) of: glyoxalase II [Reiger15], glyoxalase II [Reiger15], lipopolysaccharide glucosyltransferase [Qian14], lipoate-AceF ligase [Green95], N-acetyl-β-neuraminate lyase [Aisaka91, Uchida84], glyoxalase [Subedi11], NADPH-dependent curcumin reductase [Hassaninasab11], guanosine kinase [Mori95], inosine kinase [Mori95], glutaminase [Hartman68], 7-α-hydroxysteroid dehydrogenase [Yoshimoto91], L-serine deaminase [Newman80b], S-formylglutathione hydrolase [Gonzalez06], S-formylglutathione hydrolase [Gonzalez06], mannose isomerase [Itoh08], deoxyribose 1,5-phosphomutase [HammerJespersen70], 3'-nucleotidase [Anraku64a], glutamate decarboxylase B [Helmward89], crotonobetainyl-CoA reductase [Roth94], 3-deoxy-D-manno-octulosonate 8-phosphate synthase [Ray80], glycogen phosphorylase [Chen68a, Chen68], N-acetylglutamylphosphate reductase [Vogel74], 3-deoxy-D-manno-octulosonate 8-phosphate phosphatase [Ray80a], methylglyoxal reductase (NADPH-dependent) [Saikusa87], allantoinase [Kim00d], hydrogen:menaquinone oxidoreductase [Ballantine86], acetylornithine deacetylase [Vogel74a], glutamate-5-semialdehyde dehydrogenase [Hayzer82], D-glucuronate isomerase [Ashwell60], D-galacturonate isomerase [Ashwell60], glyoxylate carboligase [Gupta66], N-acetylornithine aminotransferase [Vogel74b], N-acetylneuraminate lyase [Aisaka91, Uchida84], dipeptidyl carboxypeptidase [Chen09b, Henrich93], threonine dehydrogenase [Boylan81, Craig86], tetrahydrodipicolinate succinylase [Simms84], amylomaltase [Wiesmeyer60], polyphosphate kinase [Haeusler92], glutamate decarboxylase A [Helmward89], N-acetylglutamate synthase [Marvil77], lactaldehyde dehydrogenase [Sridhara69, Baldoma87], glycerol dehydrogenase [Tang79], taurine dioxygenase [Eichhorn97], 2',3'-cyclic nucleotide 2'-phosphodiesterase [Anraku64a], D-aminopropanol dehydrogenase [Kelley84, Campbell78], 2-amino-3-ketobutyrate CoA ligase [Mukherjee87]

This compound has been characterized as a cofactor or prosthetic group of the following enzymes: ubiquinol oxidase (H+-transporting), phenylethylamine oxidase, amine oxidase, examinopeptidase, superoxide dismutase

This compound has been characterized as an alternative cofactor or prosthetic group of the following enzymes: NMN adenylyltransferase

This compound has been characterized as an alternative substrate of the following enzymes: Zn2+:H+ antiporter

In Growth Media: MOPS medium with 2% glycerol, MOPS medium with 2% glucose, MOPS medium with 0.4% glucose, MOPS medium base, Neidhardt EZ rich defined medium, trace metal solution, LB enriched


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Please cite the following article in publications resulting from the use of EcoCyc: Nucleic Acids Research 41:D605-12 2013
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