Showing metabocard for Cobalt (BMDB0000608)

IdentificationTaxonomyPhysical propertiesPathwaysSpectraConcentrationsLinksReferencesenzymes (17) Show 17 proteinsXML
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Record Information
Version1.0
Creation Date2016-09-30 22:33:31 UTC
Update Date2020-06-04 19:34:59 UTC
BMDB IDBMDB0000608
Secondary Accession Numbers
  • BMDB00608
Metabolite Identification
Common NameCobalt
DescriptionCobalt, also known as co(ii) or cobalt(2+) ion, belongs to the class of inorganic compounds known as homogeneous transition metal compounds. These are inorganic compounds containing only metal atoms,with the largest atom being a transition metal atom. Cobalt exists as a solid, possibly soluble (in water), and possibly neutral molecule. Cobalt exists in all living organisms, ranging from bacteria to humans. Cobalt is a potentially toxic compound.
Structure
Thumb
MOLSDFPDBSMILESInChI
Synonyms
ValueSource
Co(II)ChEBI
CO2+ChEBI
Co(2+)ChEBI
COBALT (II) ionChEBI
Cobalt(2+) ionChEBI
Cobalt(II) cationChEBI
Cobaltous ionChEBI
Cobalt(2+)Kegg
AquacatHMDB
CoHMDB
Cobalt-59HMDB
Cobatope-57HMDB
KobaltHMDB
Super cobaltHMDB
Chemical FormulaCo
Average Molecular Weight58.9332
Monoisotopic Molecular Weight58.933200194
IUPAC Namelambda2-cobalt(2+) ion
Traditional Namelambda2-cobalt(2+) ion
CAS Registry Number7440-48-4
SMILES
[Co++]
InChI Identifier
InChI=1S/Co/q+2
InChI KeyXLJKHNWPARRRJB-UHFFFAOYSA-N
Chemical Taxonomy
Description belongs to the class of inorganic compounds known as homogeneous transition metal compounds. These are inorganic compounds containing only metal atoms,with the largest atom being a transition metal atom.
KingdomInorganic compounds
Super ClassHomogeneous metal compounds
ClassHomogeneous transition metal compounds
Sub ClassNot Available
Direct ParentHomogeneous transition metal compounds
Alternative ParentsNot Available
Substituents
  • Homogeneous transition metal
Molecular FrameworkNot Available
External Descriptors
Ontology
StatusDetected and Quantified
Origin
  • Exogenous
BiofunctionNot Available
ApplicationNot Available
Cellular locationsNot Available
Physical Properties
StateSolid
Experimental Properties
PropertyValueReference
Melting Point1495 °CNot Available
Boiling PointNot AvailableNot Available
Water SolubilityNot AvailableNot Available
LogPNot AvailableNot Available
Predicted Properties
PropertyValueSource
logP0.23ChemAxon
pKa (Strongest Acidic)3.09ChemAxon
Physiological Charge2ChemAxon
Hydrogen Acceptor Count0ChemAxon
Hydrogen Donor Count0ChemAxon
Polar Surface Area0 ŲChemAxon
Rotatable Bond Count0ChemAxon
Refractivity0 m³·mol⁻¹ChemAxon
Polarizability1.78 ųChemAxon
Number of Rings0ChemAxon
BioavailabilityYesChemAxon
Rule of FiveYesChemAxon
Ghose FilterYesChemAxon
Veber's RuleYesChemAxon
MDDR-like RuleYesChemAxon
Spectra
Spectra
Spectrum TypeDescriptionSplash Key
Predicted LC-MS/MSPredicted LC-MS/MS Spectrum - 10V, Positivesplash10-0a4i-9000000000-5ec55e9e276ff34b918fView in MoNA
Predicted LC-MS/MSPredicted LC-MS/MS Spectrum - 20V, Positivesplash10-0a4i-9000000000-5ec55e9e276ff34b918fView in MoNA
Predicted LC-MS/MSPredicted LC-MS/MS Spectrum - 40V, Positivesplash10-0a4i-9000000000-5ec55e9e276ff34b918fView in MoNA
Predicted LC-MS/MSPredicted LC-MS/MS Spectrum - 10V, Negativesplash10-0a4i-9000000000-c4eed668d3af388c4a95View in MoNA
Predicted LC-MS/MSPredicted LC-MS/MS Spectrum - 20V, Negativesplash10-0a4i-9000000000-c4eed668d3af388c4a95View in MoNA
Predicted LC-MS/MSPredicted LC-MS/MS Spectrum - 40V, Negativesplash10-0a4i-9000000000-c4eed668d3af388c4a95View in MoNA
Biological Properties
Cellular LocationsNot Available
Biospecimen Locations
  • Epidermis
  • Kidney
  • Liver
  • Longissimus Thoracis Muscle
  • Milk
  • Ruminal Fluid
  • Semimembranosus Muscle
  • Testis
Pathways
Normal Concentrations
Abnormal Concentrations
Not Available
HMDB IDHMDB0000608
DrugBank IDNot Available
Phenol Explorer Compound IDNot Available
FooDB IDFDB003581
KNApSAcK IDNot Available
Chemspider ID94546
KEGG Compound IDC00175
BioCyc IDNot Available
BiGG IDNot Available
Wikipedia LinkCobalt
METLIN IDNot Available
PubChem Compound104729
PDB IDNot Available
ChEBI ID48828
References
Synthesis ReferenceNot Available
Material Safety Data Sheet (MSDS)Not Available
General References
  1. Z. Dobrzañski, R. Ko3acz, H. Górecka, K. Chojnacka, A. Bartkowiak (2005). Z. Dobrzañski et al. The Content of Microelements and Trace Elements in Raw Milk from Cows in the Silesian Region. Polish Journal of Environmental Studies Vol. 14, No 5 (2005), 685-689. Polish Journal of Environmental Studies .
  2. Z. Dobrzański, R. Kołacz, H. Górecka, K. Chojnacka, A. Bartkowiak. (2005). Z. Dobrzański, R. Kołacz, H. Górecka, K. Chojnacka, A. Bartkowiak. 2005. The Content of Microelements and Trace Elements in Raw Milk from Cows in the Silesian Region. Pol. J. Environ. Stud. 14(5):685–689. Polish Journal of Environmental Studies.
  3. A. Foroutan et al. (2019). A. Foroutan et al. The Chemical Composition of Commercial Cow's Milk (in preparation). Journal of Agricultural and Food Chemistry.
  4. Patricia Cava-Montesinos, M. Luisa Cervera Agustín Pastor Miguel de la Guardia (2005). Patricia Cava-Montesinos, M. Luisa Cervera Agustín Pastor Miguel de la Guardia. 2005. Room temperature acid sonication ICP-MS multielemental analysis of milk.Analytica Chimica Acta Volume 531, Issue 1, Pages 111-123. Analytica Chimica Acta.

Enzymes

Enzyme Details
1. S-adenosylmethionine synthase
General function:
Coenzyme transport and metabolism
Specific function:
Catalyzes the formation of S-adenosylmethionine from methionine and ATP.
Gene Name:
MAT2A
Uniprot ID:
A7E3T7
Molecular weight:
43691.0
Enzyme Details
2. Ectonucleotide pyrophosphatase/phosphodiesterase family member 2
General function:
Involved in alkylglycerophosphoethanolamine phosphodies
Specific function:
Hydrolyzes lysophospholipids to produce the signaling molecule lysophosphatidic acid (LPA) in extracellular fluids. Major substrate is lysophosphatidylcholine (PubMed:12119361). Also can act on sphingosylphosphorylcholine producing sphingosine-1-phosphate, a modulator of cell motility. Can hydrolyze, in vitro, bis-pNPP, to some extent pNP-TMP, and barely ATP. Involved in several motility-related processes such as angiogenesis and neurite outgrowth. Acts as an angiogenic factor by stimulating migration of smooth muscle cells and microtubule formation. Stimulates migration of melanoma cells, probably via a pertussis toxin-sensitive G protein. May have a role in induction of parturition. Possible involvement in cell proliferation and adipose tissue development. Tumor cell motility-stimulating factor (By similarity). Required for LPA production in activated platelets, cleaves the sn-1 lysophospholipids to generate sn-1 lysophosphatidic acids containing predominantly 18:2 and 20:4 fatty acids (By similarity). Shows a preference for the sn-1 to the sn-2 isomer of 1-O-alkyl-sn-glycero-3-phosphocholine (lyso-PAF) (By similarity).
Gene Name:
ENPP2
Uniprot ID:
A1A4K5
Molecular weight:
101717.0
Enzyme Details
3. Triokinase/FMN cyclase
General function:
Carbohydrate transport and metabolism
Specific function:
Catalyzes both the phosphorylation of dihydroxyacetone and of glyceraldehyde, and the splitting of ribonucleoside diphosphate-X compounds among which FAD is the best substrate. Represses IFIH1-mediated cellular antiviral response.
Gene Name:
TKFC
Uniprot ID:
Q58DK4
Molecular weight:
59124.0
Enzyme Details
4. S-adenosylmethionine synthase isoform type-1
General function:
Coenzyme transport and metabolism
Specific function:
Catalyzes the formation of S-adenosylmethionine from methionine and ATP. The reaction comprises two steps that are both catalyzed by the same enzyme: formation of S-adenosylmethionine (AdoMet) and triphosphate, and subsequent hydrolysis of the triphosphate.
Gene Name:
MAT1A
Uniprot ID:
Q2KJC6
Molecular weight:
43761.0
Enzyme Details
5. Methionine synthase
General function:
Amino acid transport and metabolism
Specific function:
Catalyzes the transfer of a methyl group from methyl-cobalamin to homocysteine, yielding enzyme-bound cob(I)alamin and methionine. Subsequently, remethylates the cofactor using methyltetrahydrofolate (By similarity).
Gene Name:
MTR
Uniprot ID:
Q4JIJ3
Molecular weight:
140478.0
Enzyme Details
6. cGMP-specific 3',5'-cyclic phosphodiesterase
General function:
Involved in 3',5'-cyclic-GMP phosphodiesterase activity
Specific function:
Plays a role in signal transduction by regulating the intracellular concentration of cyclic nucleotides. This phosphodiesterase catalyzes the specific hydrolysis of cGMP to 5'-GMP (PubMed:8530505). Specifically regulates nitric-oxide-generated cGMP (By similarity).
Gene Name:
PDE5A
Uniprot ID:
Q28156
Molecular weight:
98627.0
Enzyme Details
7. U8 snoRNA-decapping enzyme
General function:
Involved in hydrolase activity
Specific function:
RNA-binding and decapping enzyme that catalyzes the cleavage of the cap structure of snoRNAs and mRNAs in a metal-dependent manner. Part of the U8 snoRNP complex that is required for the accumulation of mature 5.8S and 28S rRNA. Has diphosphatase activity and removes m7G and/or m227G caps from U8 snoRNA and leaves a 5'monophosphate on the RNA. Catalyzes also the cleavage of the cap structure on mRNAs. Does not hydrolyze cap analog structures like 7-methylguanosine nucleoside triphosphate (m7GpppG). Also hydrolysis m7G- and m227G U3-capped RNAs but with less efficiencies. Has broad substrate specificity with manganese or cobalt as cofactor and can act on various RNA species. Binds to the U8 snoRNA; metal is not required for RNA-binding. May play a role in the regulation of snoRNAs and mRNAs degradation. Acts also as a phosphatase; hydrolyzes the non-canonical purine nucleotides inosine diphosphate (IDP) and deoxyinosine diphosphate (dITP) as well as guanosine diphosphate (GDP), deoxyguanosine diphosphate (dGDP), xanthine diphosphate (XDP), inosine triphosphate (ITP) and deoxyinosine triphosphate (ITP) to their respective monophosphate derivatives and does not distinguish between the deoxy- and ribose forms. The order of activity with different substrates is IDP > dIDP >> GDP = dGDP > XDP = ITP = dITP. Binds strongly to GTP, ITP and XTP. Participates in the hydrolysis of dIDP/IDP and probably excludes non-canonical purines from RNA and DNA precursor pools, thus preventing their incorporation into RNA and DNA and avoiding chromosomal lesions.
Gene Name:
NUDT16
Uniprot ID:
A1A4Q9
Molecular weight:
21399.0
Enzyme Details
8. Bis(5'-adenosyl)-triphosphatase
General function:
Nucleotide transport and metabolism
Specific function:
Cleaves P(1)-P(3)-bis(5'-adenosyl) triphosphate (Ap3A) to yield AMP and ADP. Can also hydrolyze P(1)-P(4)-bis(5'-adenosyl) tetraphosphate (Ap4A), but has extremely low activity with ATP. Modulates transcriptional activation by CTNNB1 and thereby contributes to regulate the expression of genes essential for cell proliferation and survival, such as CCND1 and BIRC5. Plays a role in the induction of apoptosis via SRC and AKT1 signaling pathways. Inhibits MDM2-mediated proteasomal degradation of p53/TP53 and thereby plays a role in p53/TP53-mediated apoptosis. Induction of apoptosis depends on the ability of FHIT to bind P(1)-P(3)-bis(5'-adenosyl) triphosphate or related compounds, but does not require its catalytic activity. Functions as tumor suppressor (By similarity).
Gene Name:
FHIT
Uniprot ID:
Q1KZG4
Molecular weight:
16951.0
Enzyme Details
9. Methylmalonyl-CoA mutase, mitochondrial
General function:
Lipid transport and metabolism
Specific function:
Involved in the degradation of several amino acids, odd-chain fatty acids and cholesterol via propionyl-CoA to the tricarboxylic acid cycle.
Gene Name:
MMUT
Uniprot ID:
Q9GK13
Molecular weight:
83235.0
Enzyme Details
10. Methionine aminopeptidase
General function:
Translation, ribosomal structure and biogenesis
Specific function:
Cotranslationally removes the N-terminal methionine from nascent proteins. The N-terminal methionine is often cleaved when the second residue in the primary sequence is small and uncharged (Met-Ala-, Cys, Gly, Pro, Ser, Thr, or Val).
Gene Name:
Not Available
Uniprot ID:
Q862K9
Molecular weight:
20645.0
Enzyme Details
11. Methionine aminopeptidase 1
General function:
Translation, ribosomal structure and biogenesis
Specific function:
Cotranslationally removes the N-terminal methionine from nascent proteins. The N-terminal methionine is often cleaved when the second residue in the primary sequence is small and uncharged (Met-Ala-, Cys, Gly, Pro, Ser, Thr, or Val).
Gene Name:
METAP1
Uniprot ID:
A6QLA4
Molecular weight:
43183.0
Enzyme Details
12. Methionine aminopeptidase
General function:
Translation, ribosomal structure and biogenesis
Specific function:
Cotranslationally removes the N-terminal methionine from nascent proteins. The N-terminal methionine is often cleaved when the second residue in the primary sequence is small and uncharged (Met-Ala-, Cys, Gly, Pro, Ser, Thr, or Val).
Gene Name:
METAP1D
Uniprot ID:
Q2HJ25
Molecular weight:
23806.0
Enzyme Details
13. Methionine aminopeptidase 2
General function:
Translation, ribosomal structure and biogenesis
Specific function:
Cotranslationally removes the N-terminal methionine from nascent proteins. The N-terminal methionine is often cleaved when the second residue in the primary sequence is small and uncharged (Met-Ala-, Cys, Gly, Pro, Ser, Thr, or Val).
Gene Name:
METAP2
Uniprot ID:
Q3ZC89
Molecular weight:
52812.0
Enzyme Details
14. LYR motif-containing protein 4
General function:
Not Available
Specific function:
Required for nuclear and mitochondrial iron-sulfur protein biosynthesis.
Gene Name:
LYRM4
Uniprot ID:
Q0VCG0
Molecular weight:
10711.0
Enzyme Details
15. Transcobalamin-2
General function:
Involved in cobalamin binding
Specific function:
Primary vitamin B12-binding and transport protein. Delivers cobalamin to cells.
Gene Name:
TCN2
Uniprot ID:
Q9XSC9
Molecular weight:
47958.0
Enzyme Details
16. Methylmalonic aciduria and homocystinuria type C protein homolog
General function:
Involved in cobalamin binding
Specific function:
Catalyzes the reductive dealkylation of cyanocobalamin to cob(II)alamin, using FAD or FMN as cofactor and NADPH as cosubstrate. Can also catalyze the glutathione-dependent reductive demethylation of methylcobalamin, and, with much lower efficiency, the glutathione-dependent reductive demethylation of adenosylcobalamin. Under anaerobic conditions cob(I)alamin is the first product; it is highly reactive and is converted to aquocob(II)alamin in the presence of oxygen. Binds cyanocobalamin, adenosylcobalamin, methylcobalamin and other, related vitamin B12 derivatives.
Gene Name:
MMACHC
Uniprot ID:
Q5E9C8
Molecular weight:
31633.0
Enzyme Details
17. Probable lysosomal cobalamin transporter
General function:
Involved in cobalamin binding
Specific function:
Probable lysosomal cobalamin transporter. Required to export cobalamin from lysosomes allowing its conversion to cofactors (By similarity).
Gene Name:
LMBRD1
Uniprot ID:
Q3SYY9
Molecular weight:
62022.0