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Escherichia coli K-12 substr. MG1655 Compound: Mn2+

Synonyms: manganese ion, Mn(II), Mn+2, Mn++, manganese (II) ion

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

Component of:
manganese chloride
manganese sulfate pentahydrate

Chemical Formula: Mn

Molecular Weight: 54.938 Daltons

Monoisotopic Molecular Weight: 54.9380496 Daltons

SMILES: [Mn++]

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


Unification Links: CAS:7439-96-5, CAS:16397-91-4, ChEBI:29035, ChemSpider:25916, HMDB:HMDB01333, IAF1260:33594, KEGG:C19610, PubChem:27854

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

In Reactions of unknown directionality:

Not in pathways:
MntR + Mn2+ = MntR-Mn2+

In Transport reactions:
Mn2+[periplasm] + H+[periplasm]Mn2+[cytosol] + H+[cytosol],
an ion[periplasm]an ion[extracellular space]

Enzymes activated by Mn2+, sorted by the type of activation, are:

Activator (Mechanism unknown) of: dipeptidyl carboxypeptidase [Chen09a, Henrich93], cysteinylglycine dipeptidase [Suzuki01a], adenosylmethionine decarboxylase [Lu07], cyclic di-GMP phosphodiesterase [Lacey10], D-altronate dehydratase [Dreyer87], glutaminase B [Prusiner76], D-mannonate oxidoreductase [Portalier72], D-mannonate dehydratase [RobertBaudouy73, Dreyer87], threonine dehydrogenase [Comment 1], polyphosphate kinase [Ahn90, Haeusler92, Comment 2], proline aminopeptidase [Yoshimoto89]

Enzymes inhibited by Mn2+, sorted by the type of inhibition, are:

Inhibitor (Mechanism unknown) of: biotin sulfoxide reductase [Del79], methylmalonyl-CoA mutase [Bobik03], glutaminase [Brown08], glutaminase [Brown08], diacylglycerol pyrophosphate phosphatase [Dillon96], N-acetylglutamylphosphate reductase [Vogel74], imidazole glycerol phosphate synthase [Klem93], phosphoglucomutase [Joshi64], Rnase [Goedken01], D-glucarate dehydratase [Comment 3], D-aminopropanol dehydrogenase [Kelley84, Campbell78]

This compound has been characterized as a cofactor or prosthetic group of the following enzymes: PII-UMP deuridylylation, [protein-PII] uridylyltransferase, Xaa-Pro dipeptidase, 1-hydroxy-2-methyl-2-(E)-butenyl 4-diphosphate synthase, cytidine 3'-phosphate phosphohydrolase, dGMP 5'-phosphate phosphohydrolase, adenosine 3'-phosphate phosphohydrolase, UDP-N-acetylmuramate-alanine ligase, monoacetylchitobiose-6-phosphate hydrolase, 6-phospho-β-D-glucosyl-(1,4)-D-glucose glucohydrolase, phosphoribosylglycinamide formyltransferase, 5'-nucleotidase, 3'-nucleotidase, 8-oxo-dGTP diphosphatase, 2-oxopent-4-enoate hydratase, transketolase, 5-phospho-α-D-ribosyl 1,2-cyclic phosphate phosphodiesterase, 2,3-bisphosphoglycerate-independent phosphoglycerate mutase, RNA ligase, L-ascorbate 6-phosphate lactonase, p-aminobenzoyl-glutamate hydrolase, S-ureidoglycine aminohydrolase, allantoate amidohydrolase, coproporphyrinogen III oxidase, diacylglycerol kinase, tRNA nucleotidyltransferase, fructose-1,6-bisphosphatase, peptidoglycan glycosyltransferase, agmatinase, oligoribonuclease, protein kinase, L-arabinose isomerase, L-fucose isomerase, D-arabinose isomerase, ThDP adenylyl transferase, histidinol dehydrogenase, histidinal dehydrogenase, glutamine synthetase, 2C-methyl-D-erythritol 2,4-cyclodiphosphate synthase, 2-succinyl-5-enolpyruvyl-6-hydroxy-3-cyclohexene-1-carboxylate synthase, xylose isomerase, 2-deoxyglucose-6-phosphatase, 3-isopropylmalate dehydrogenase, aminopeptidase, examinopeptidase, proline aminopeptidase, deoxyribose 1,5-phosphomutase, adenine deaminase, L-rhamnose isomerase, 1-deoxy-D-xylulose 5-phosphate reductoisomerase, α-D-ribose 1,5-phosphomutase, pyrimidine nucleotidase, guanylate cyclase, glutamine synthetase deadenylase, transketolase, malate dehydrogenase, NAD-requiring, malate dehydrogenase, ribonuclease, 3-octaprenyl-4-hydroxybenzoate carboxy-lyase, RNase T exonuclease, 2-keto-3-deoxygluconokinase, Rnase, phosphoglycerol transferase, phenylhydantoinase, superoxide dismutase, guanosine-3',5'-bis(diphosphate) 3'-diphosphatase, acyl carrier protein phosphodiesterase, NADH pyrophosphatase, phosphoglycerol transferase, isocitrate dehydrogenase, phosphodiesterase, c-di-GMP-specific, RNase, fructose 1,6-bisphosphatase, RNA 3'-terminal phosphate cyclase, α-galactosidase, 3' to 5' proofreading exonuclease

This compound has been characterized as an alternative cofactor or prosthetic group of the following enzymes: pyruvate kinase, molybdenum cofactor guanylyltransferase, bis(molybdenum cofactor) guanylyltransferase, farnesyl diphosphate synthase, methionine adenosyltransferase, imidazoleglycerol-phosphate dehydratase, aspartate ammonia-lyase, folylpoly-γ-glutamate synthetase, GDP-mannose mannosyl hydrolase, isopentenyl diphosphate isomerase, NAD+ synthetase, NH3-dependent, pyruvate kinase, 4-diphosphocytidyl-2C-methyl-D-erythritol synthase, hypoxanthine phosphoribosyltransferase, isocitrate lyase, nucleoside diphosphate kinase, allantoinase, glycerol kinase, dihydroneopterin triphosphate 2'-epimerase, phosphoenolpyruvate carboxykinase (ATP), ribose-phosphate diphosphokinase, oxidized nucleoside triphosphate pyrophosphohydrolase, adenylylsulfate kinase, bis(molybdenum cofactor) synthase, cytosine deaminase, pantothenate synthetase, geranyl diphosphate synthase, holo-[acyl-carrier-protein] synthase, NMN adenylyltransferase, adenine phosphoribosyltransferase, carbamoyl phosphate synthetase

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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Brown08: Brown G, Singer A, Proudfoot M, Skarina T, Kim Y, Chang C, Dementieva I, Kuznetsova E, Gonzalez CF, Joachimiak A, Savchenko A, Yakunin AF (2008). "Functional and structural characterization of four glutaminases from Escherichia coli and Bacillus subtilis." Biochemistry 47(21);5724-35. PMID: 18459799

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Chen09a: 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.

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Del79: Del Campillo-Campbell, A, Dykhuizen, D, Cleary, PP "Enzymatic reduction of d-biotin d-sulfoxide to d-biotin." Methods in Enzymology 62:379-385 (1979).

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Goedken01: Goedken ER, Marqusee S (2001). "Co-crystal of Escherichia coli RNase HI with Mn2+ ions reveals two divalent metals bound in the active site." J Biol Chem 276(10);7266-71. PMID: 11083878

Haeusler92: Haeusler PA, Dieter L, Rittle KJ, Shepler LS, Paszkowski AL, Moe OA (1992). "Catalytic properties of Escherichia coli polyphosphate kinase: an enzyme for ATP regeneration." Biotechnol Appl Biochem 1992;15(2);125-33. PMID: 1316760

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Klem93: Klem TJ, Davisson VJ (1993). "Imidazole glycerol phosphate synthase: the glutamine amidotransferase in histidine biosynthesis." Biochemistry 1993;32(19);5177-86. PMID: 8494895

Lacey10: Lacey MM, Partridge JD, Green J (2010). "Escherichia coli K-12 YfgF is an anaerobic cyclic di-GMP phosphodiesterase with roles in cell surface remodelling and the oxidative stress response." Microbiology 156(Pt 9);2873-86. PMID: 20522491

Lu07: Lu ZJ, Markham GD (2007). "Metal ion activation of S-adenosylmethionine decarboxylase reflects cation charge density." Biochemistry 46(27);8172-80. PMID: 17567041

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Yoshimoto89: Yoshimoto T, Tone H, Honda T, Osatomi K, Kobayashi R, Tsuru D (1989). "Sequencing and high expression of aminopeptidase P gene from Escherichia coli HB101." J Biochem (Tokyo) 105(3);412-6. PMID: 2659585

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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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