Showing metabocard for Nickel (BMDB0002457)

IdentificationTaxonomyPhysical propertiesPathwaysSpectraConcentrationsLinksReferencesenzymes (5) Show 5 proteinsXML
Show more...Show more...
Record Information
Version1.0
Creation Date2016-09-30 22:55:28 UTC
Update Date2020-06-04 20:43:48 UTC
BMDB IDBMDB0002457
Secondary Accession Numbers
  • BMDB02457
Metabolite Identification
Common NameNickel
DescriptionNickel, also known as ni2+ or nickel (ii) 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. Nickel exists as a solid, possibly soluble (in water), and possibly neutral molecule. Nickel exists in all living organisms, ranging from bacteria to humans. Nickel is a potentially toxic compound.
Structure
Thumb
MOLSDFPDBSMILESInChI
Synonyms
Chemical FormulaNi
Average Molecular Weight58.6934
Monoisotopic Molecular Weight57.935347922
IUPAC Namenickel(2+) ion
Traditional Namenickel(2+) ion
CAS Registry Number7440-02-0
SMILES
[Ni++]
InChI Identifier
InChI=1S/Ni/q+2
InChI KeyVEQPNABPJHWNSG-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 Parents
Substituents
  • Homogeneous transition metal
  • Inorganic nickel compound
Molecular FrameworkNot Available
External Descriptors
Ontology
StatusDetected and Quantified
OriginNot Available
BiofunctionNot Available
ApplicationNot Available
Cellular locationsNot Available
Physical Properties
StateSolid
Experimental Properties
PropertyValueReference
Melting Point1455 °CNot Available
Boiling PointNot AvailableNot Available
Water SolubilityNot AvailableNot Available
LogPNot AvailableNot Available
Predicted Properties
PropertyValueSource
logP0.16ChemAxon
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-9000000000-08256b3c9e2cc1750f60View in MoNA
Predicted LC-MS/MSPredicted LC-MS/MS Spectrum - 20V, Positivesplash10-0a4i-9000000000-08256b3c9e2cc1750f60View in MoNA
Predicted LC-MS/MSPredicted LC-MS/MS Spectrum - 40V, Positivesplash10-0a4i-9000000000-08256b3c9e2cc1750f60View in MoNA
Predicted LC-MS/MSPredicted LC-MS/MS Spectrum - 10V, Negativesplash10-0a4i-9000000000-4648ffc6f53552c41503View in MoNA
Predicted LC-MS/MSPredicted LC-MS/MS Spectrum - 20V, Negativesplash10-0a4i-9000000000-4648ffc6f53552c41503View in MoNA
Predicted LC-MS/MSPredicted LC-MS/MS Spectrum - 40V, Negativesplash10-0a4i-9000000000-4648ffc6f53552c41503View in MoNA
Biological Properties
Cellular LocationsNot Available
Biospecimen Locations
  • Milk
  • Ruminal Fluid
Pathways
Normal Concentrations
Abnormal Concentrations
Not Available
HMDB IDHMDB0002457
DrugBank IDNot Available
Phenol Explorer Compound IDNot Available
FooDB IDFDB013444
KNApSAcK IDNot Available
Chemspider ID909
KEGG Compound IDC19609
BioCyc IDNot Available
BiGG IDNot Available
Wikipedia LinkNickel
METLIN IDNot Available
PubChem Compound934
PDB IDNot Available
ChEBI ID49786
References
Synthesis ReferenceLightner, David A.; Crist, B. Vincent; Kalyanam, Nagabushanam; May, Leslie M.; Jackman, Dennis E. The octant rule. 15. Antioctant effects: synthesis and circular dichroism of 2-exo- and 2-endo-alkylbicyclo[2.2.1]heptan-7-ones and bicyclo[3.2.1]octan-8-one. J. Org. Chem. 1985,50, 3867-3878. DOI: 10.1021/jo00220a037
Material Safety Data Sheet (MSDS)Not Available
General References
  1. 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.
  2. Fooddata+, The Technical University of Denmark (DTU) [Link]

Enzymes

Enzyme Details
1. 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
2. Polyribonucleotide 5'-hydroxyl-kinase Clp1
General function:
Involved in ATP binding
Specific function:
Polynucleotide kinase that can phosphorylate the 5'-hydroxyl groups of double-stranded RNA (dsRNA), single-stranded RNA (ssRNA), double-stranded DNA (dsDNA) and double-stranded DNA:RNA hybrids. dsRNA is phosphorylated more efficiently than dsDNA, and the RNA component of a DNA:RNA hybrid is phosphorylated more efficiently than the DNA component. Plays a key role in both tRNA splicing and mRNA 3'-end formation. Component of the tRNA splicing endonuclease complex: phosphorylates the 5'-terminus of the tRNA 3'-exon during tRNA splicing; this phosphorylation event is a prerequisite for the subsequent ligation of the two exon halves and the production of a mature tRNA. Its role in tRNA splicing and maturation is required for cerebellar development. Component of the pre-mRNA cleavage complex II (CF-II), which seems to be required for mRNA 3'-end formation. Also phosphorylates the 5'-terminus of exogenously introduced short interfering RNAs (siRNAs), which is a necessary prerequisite for their incorporation into the RNA-induced silencing complex (RISC). However, endogenous siRNAs and microRNAs (miRNAs) that are produced by the cleavage of dsRNA precursors by DICER1 already contain a 5'-phosphate group, so this protein may be dispensible for normal RNA-mediated gene silencing (By similarity).
Gene Name:
CLP1
Uniprot ID:
A2VE01
Molecular weight:
47630.0
Enzyme Details
3. 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
4. 1,2-dihydroxy-3-keto-5-methylthiopentene dioxygenase
General function:
Involved in nickel ion binding
Specific function:
Catalyzes the formation of formate and 2-keto-4-methylthiobutyrate (KMTB) from 1,2-dihydroxy-3-keto-5-methylthiopentene (DHK-MTPene). Also down-regulates cell migration mediated by MMP14.
Gene Name:
ADI1
Uniprot ID:
Q3ZBL1
Molecular weight:
21487.0
Enzyme Details
5. Alpha-fetoprotein
General function:
Involved in copper ion binding
Specific function:
Binds copper, nickel, and fatty acids as well as, and bilirubin less well than, serum albumin.
Gene Name:
AFP
Uniprot ID:
Q3SZ57
Molecular weight:
68588.0