Escherichia coli K-12 substr. MG1655 Compound: Ni2+

Synonyms: nickel, Ni++, Ni+2

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

Component of:
nickel sulphate
NikR-Ni transcriptional repressor

Chemical Formula: Ni

Molecular Weight: 58.7 Daltons

Monoisotopic Molecular Weight: 57.9353479 Daltons

SMILES: [Ni++]

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


Unification Links: ChEBI:49786, ChemSpider:909, HMDB:HMDB02457, IAF1260:34516, KEGG:C19609, PubChem:934

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

In Reactions of unknown directionality:

Not in pathways:
YqjI + Ni2+ = YqjI-nickel
RcnR + Ni2+ = RcnR-nickel
NikR + Ni2+ = NikR-Ni transcriptional repressor

In Transport reactions:
Ni2+[periplasm] + ATP + H2O → Ni2+[cytosol] + ADP + phosphate + H+,
an ion[periplasm]an ion[extracellular space]

Enzymes activated by Ni2+, sorted by the type of activation, are:

Activator (Mechanism unknown) of: cysteinylglycine dipeptidase [Suzuki01], fructoselysine 3-epimerase [Wiame04], argininosuccinate lyase [Vogel74]

Enzymes inhibited by Ni2+, sorted by the type of inhibition, are:

Inhibitor (Mechanism unknown) of: fructose bisphosphate aldolase [Macomber11], lipopolysaccharide glucosyltransferase [Qian14], GTPase [Sydor13], glutamate-5-semialdehyde dehydrogenase [Hayzer82], N-acetylglutamylphosphate reductase [Vogel74], methylglyoxal reductase (NADPH-dependent) [Saikusa87], acetylornithine deacetylase [Vogel74a], dipeptidyl carboxypeptidase [Chen09, Henrich93], threonine dehydrogenase [Boylan81, Craig86], amylomaltase [Wiesmeyer60], D-aminopropanol dehydrogenase [Kelley84, Campbell78], α-galactosidase [Burstein71]

This compound has been characterized as a cofactor or prosthetic group of the following enzymes: ureidoglycolate lyase, 5'-nucleotidase, 3'-nucleotidase, aminopeptidase, examinopeptidase, glyoxalase I

This compound has been characterized as an alternative cofactor or prosthetic group of the following enzymes: methionine adenosyltransferase, allantoinase, NMN adenylyltransferase, phenylhydantoinase

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


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Burstein71: Burstein C, Kepes A (1971). "The alpha-galactosidase from Escherichia coli K12." Biochim Biophys Acta 1971;230(1);52-63. PMID: 5543331

Campbell78: Campbell RL, Swain RR, Dekker EE (1978). "Purification, separation, and characterization of two molecular forms of D-1-amino-2-propanol:NAD+ oxidoreductase activity from extracts of Escherichia coli K-12." J Biol Chem 253(20);7282-8. PMID: 359547

Chen09: Chen HL, Chang CT, Lin LL, Li TY, Lo HF (2009). "The dipeptidyl carboxypeptidase of Escherichia coli novablue: overproduction and molecular characterization of the recombinant enzyme." World Journal of Microbiology and Biotechnology 25(2);323-330.

Craig86: Craig PA, Dekker EE (1986). "L-threonine dehydrogenase from Escherichia coli K-12: thiol-dependent activation by Mn2+." Biochemistry 1986;25(8);1870-6. PMID: 3518793

Hayzer82: Hayzer DJ, Leisinger T (1982). "Proline biosynthesis in Escherichia coli. Purification and characterisation of glutamate-semialdehyde dehydrogenase." Eur J Biochem 1982;121(3);561-5. PMID: 7035170

Henrich93: Henrich B, Becker S, Schroeder U, Plapp R (1993). "dcp gene of Escherichia coli: cloning, sequencing, transcript mapping, and characterization of the gene product." J Bacteriol 175(22);7290-300. PMID: 8226676

Kelley84: Kelley JJ, Dekker EE (1984). "D-1-amino-2-propanol:NAD+ oxidoreductase. Purification and general properties of the large molecular form of the enzyme from Escherichia coli K12." J Biol Chem 1984;259(4);2124-9. PMID: 6365902

Macomber11: Macomber L, Elsey SP, Hausinger RP (2011). "Fructose-1,6-bisphosphate aldolase (class II) is the primary site of nickel toxicity in Escherichia coli." Mol Microbiol 82(5);1291-300. PMID: 22014167

Qian14: Qian J, Garrett TA, Raetz CR (2014). "In vitro assembly of the outer core of the lipopolysaccharide from Escherichia coli K-12 and Salmonella typhimurium." Biochemistry 53(8);1250-62. PMID: 24479701

Saikusa87: Saikusa T, Rhee H, Watanabe K, Murata K, Kimura A (1987). "Metabolism of 2-oxoaldehydes in bacteria: purification and characterization of methylglyoxal reductase from E. coli." Agricultural and Biological Chemistry 51(7): 1893-1899.

Suzuki01: Suzuki H, Kamatani S, Kumagai H (2001). "Purification and characterization of aminopeptidase B from Escherichia coli K-12." Biosci Biotechnol Biochem 65(7);1549-58. PMID: 11515538

Sydor13: Sydor AM, Jost M, Ryan KS, Turo KE, Douglas CD, Drennan CL, Zamble DB (2013). "Metal binding properties of Escherichia coli YjiA, a member of the metal homeostasis-associated COG0523 family of GTPases." Biochemistry 52(10);1788-1801. PMID: 24449932

Vogel74: Vogel HJ, Vogel RH (1974). "Enzymes of arginine biosynthesis and their repressive control." Adv Enzymol Relat Areas Mol Biol 1974;40(0);65-90. PMID: 4365537

Vogel74a: Vogel, HJ, Vogel, RH "Enzymes of Arginine Biosynthesis." Advances in Enzymology 40:71-72 (1974).

Wiame04: Wiame E, Van Schaftingen E (2004). "Fructoselysine 3-epimerase, an enzyme involved in the metabolism of the unusual Amadori compound psicoselysine in Escherichia coli." Biochem J 378(Pt 3);1047-52. PMID: 14641112

Wiesmeyer60: Wiesmeyer H, Cohn M (1960). "The characterization of the pathway of maltose utilization by Escherichia coli: II. General properties and mechanism of action of amylomaltase." Biochim Biophys Acta 39:427-439. PMID: 13844669

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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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