ECMDB: Zinc (ECMDB01303) (M2MDB000330)

Identification Taxonomy Physical Properties Biological Properties Spectra Concentrations Links References Enzymes (4)Transporters (12)XML

Proteins (13)

Record Information

Version

2.0

Creation Date

2012-05-31 13:49:28 -0600

Update Date

2015-09-18 09:21:20 -0600

Secondary Accession Numbers

ECMDB01303

Identification

Name:

Zinc

Description:

Zinc is an essential element, necessary for sustaining all life. It is an essential trace element, necessary for plants, animals, and microorganisms. Zinc is found in nearly 100 specific enzymes (other sources say 300), serves as structural ions in transcription factors and is stored and transferred in metallothioneins. It is "typically the second most abundant transition metal in organisms" after iron and it is the only metal which appears in all enzyme classes. (Wikipedia)

Structure

MOL SDF PDB SMILES InChI

Synonyms:

Zinc
Zinc ion
Zn
Zn(II)
ZN++
ZN+2
Zn⁺⁺
Zn⁺²

Chemical Formula:

Weight:

Average: 65.409
Monoisotopic: 63.929146578

InChI Key:

HCHKCACWOHOZIP-UHFFFAOYSA-N

InChI:

InChI=1S/Zn

CAS number:

7440-66-6

IUPAC Name:

zinc(2+) ion

Traditional IUPAC Name:

zinc(2+) ion

SMILES:

[Zn]

Chemical Taxonomy

Description

This compound belongs to the class of chemical entities known as homogeneous transition metal compounds. These are inorganic compounds containing only metal atoms,with the largest atom being a transition metal atom.

Kingdom

Chemical entities

Super Class

Inorganic compounds

Class

Homogeneous metal compounds

Sub Class

Homogeneous transition metal compounds

Direct Parent

Homogeneous transition metal compounds

Alternative Parents

Not Available

Substituents

Homogeneous transition metal

Molecular Framework

Not Available

External Descriptors

monoatomic dication (CHEBI:29105 )
divalent metal cation (CHEBI:29105 )
zinc cation (CHEBI:29105 )
a cation (ZN+2 )

Physical Properties

State:

Solid

Charge:

Melting point:

419.5 °C

Experimental Properties:

Property	Value	Source

Predicted Properties

Property	Value	Source
logP	0.16	ChemAxon
Physiological Charge	2	ChemAxon
Hydrogen Acceptor Count	0	ChemAxon
Hydrogen Donor Count	0	ChemAxon
Polar Surface Area	0 Å²	ChemAxon
Rotatable Bond Count	0	ChemAxon
Refractivity	0 m³·mol^-1	ChemAxon
Polarizability	1.78 Å³	ChemAxon
Number of Rings	0	ChemAxon
Bioavailability	1	ChemAxon
Rule of Five	Yes	ChemAxon
Ghose Filter	Yes	ChemAxon
Veber's Rule	Yes	ChemAxon
MDDR-like Rule	Yes	ChemAxon

Biological Properties

Cellular Locations:

Cytoplasm

Reactions:

Adenosine triphosphate + Water + Zinc > ADP + Hydrogen ion + Phosphate + Zinc
Adenosine triphosphate + Water + Zinc > ADP + Hydrogen ion + Phosphate + Zinc
Adenosine triphosphate + Water + Zinc > ADP + Hydrogen ion + Phosphate + Zinc
Adenosine triphosphate + Water + Zinc > ADP + Hydrogen ion + Phosphate + Zinc
Zinc + Water + Adenosine triphosphate > Zinc + ADP + Phosphate + Hydrogen ion
Zinc + Water + Adenosine triphosphate > Zinc + ADP + Phosphate + Hydrogen ion
Zinc + Water + Adenosine triphosphate > Zinc + ADP + Phosphate + Hydrogen ion
Zinc + Water + Adenosine triphosphate > Zinc + ADP + Phosphate + Hydrogen ion
Zinc + Adenosine triphosphate + Water > ADP + Phosphate + Hydrogen ion

SMPDB Pathways:

Collection of Reactions without pathways	PW001891
Porphyrin metabolism	PW000936
Pyrimidine metabolism	PW000942
Secondary Metabolites: Ubiquinol biosynthesis	PW000981
Secondary Metabolites: Ubiquinol biosynthesis 2	PW002036
Secondary metabolites: isoprenoid biosynthesis (nonmevalonate pathway)	PW000975
Secondary metabolites: methylerythritol phosphate and polyisoprenoid biosynthesis	PW000958
inner membrane transport	PW000786
preQ0 metabolism	PW001893
purine nucleotides de novo biosynthesis	PW000910
purine nucleotides de novo biosynthesis 1435709748	PW000960
threonine biosynthesis	PW000817

KEGG Pathways:

ABC transporters ec02010
Pyrimidine metabolism ec00240
Two-component system ec02020

EcoCyc Pathways:

Not Available

Concentrations

Concentration	Strain	Media	Growth Status	Growth System	Temperature	Details
4000± 0 uM	K-12	Not Available	Not Available	Not Available	Not Available	1. Cybercell Database: http://ccdb.wishartlab.com/CCDB/cgi-bin/STAT_NEW.cgi 2. Phillips R., Kondev, J., Theriot, J. (2008) “Physical Biology of the Cell” Garland Science, New York, NY.

Find out more about how we convert literature concentrations.

Spectra

Spectra:

Spectrum Type	Description	Splash Key
Predicted LC-MS/MS	Predicted LC-MS/MS Spectrum - 10V, Positive	splash10-03di-9000000000-0cd08967c771fb645329	View in MoNA
Predicted LC-MS/MS	Predicted LC-MS/MS Spectrum - 20V, Positive	splash10-03di-9000000000-0cd08967c771fb645329	View in MoNA
Predicted LC-MS/MS	Predicted LC-MS/MS Spectrum - 40V, Positive	splash10-03di-9000000000-0cd08967c771fb645329	View in MoNA
Predicted LC-MS/MS	Predicted LC-MS/MS Spectrum - 10V, Negative	splash10-03di-9000000000-29976d3ebd17b2d11a4b	View in MoNA
Predicted LC-MS/MS	Predicted LC-MS/MS Spectrum - 20V, Negative	splash10-03di-9000000000-29976d3ebd17b2d11a4b	View in MoNA
Predicted LC-MS/MS	Predicted LC-MS/MS Spectrum - 40V, Negative	splash10-03di-9000000000-29976d3ebd17b2d11a4b	View in MoNA

References

References:

An WL, Pei JJ, Nishimura T, Winblad B, Cowburn RF: Zinc-induced anti-apoptotic effects in SH-SY5Y neuroblastoma cells via the extracellular signal-regulated kinase 1/2. Brain Res Mol Brain Res. 2005 Apr 27;135(1-2):40-7. Epub 2005 Jan 8. Pubmed: 15857667
Arnold LE, DiSilvestro RA: Zinc in attention-deficit/hyperactivity disorder. J Child Adolesc Psychopharmacol. 2005 Aug;15(4):619-27. Pubmed: 16190793
Batista MN, Cuppari L, de Fatima Campos Pedrosa L, Almeida MG, de Almeida JB, de Medeiros AC, Canziani ME: Effect of end-stage renal disease and diabetes on zinc and copper status. Biol Trace Elem Res. 2006 Jul;112(1):1-12. Pubmed: 16943612
Cominetti C, Garrido AB Jr, Cozzolino SM: Zinc nutritional status of morbidly obese patients before and after Roux-en-Y gastric bypass: a preliminary report. Obes Surg. 2006 Apr;16(4):448-53. Pubmed: 16608609
Cutinha D, Vaja S, Treacher D, Swaminathan R: Erythrocyte zinc content in critically ill patients. Clin Chem Lab Med. 2005;43(9):930-3. Pubmed: 16176172
de Sena KC, Arrais RF, das Gracas Almeida M, de Araujo DM, dos Santos MM, de Lima VT, de Fatima Campos Pedrosa L: Effects of zinc supplementation in patients with type 1 diabetes. Biol Trace Elem Res. 2005 Summer;105(1-3):1-9. Pubmed: 16034148
Gupta SK, Singh SP, Shukla VK: Copper, zinc, and Cu/Zn ratio in carcinoma of the gallbladder. J Surg Oncol. 2005 Sep 1;91(3):204-8. Pubmed: 16118778
Ishikawa Y, Kudo H, Kagawa Y, Sakamoto S: Increased plasma levels of zinc in obese adult females on a weight-loss program based on a hypocaloric balanced diet. In Vivo. 2005 Nov-Dec;19(6):1035-7. Pubmed: 16277018
Kaczmarek A, Robak-Cholubek D, Sowa I, Jakiel G: Comparison of the levels of copper, zinc and iron in cervical mucus and in blood serum of women of childbearing age. Ann Univ Mariae Curie Sklodowska [Med]. 2004;59(1):72-5. Pubmed: 16145958
Kanehisa, M., Goto, S., Sato, Y., Furumichi, M., Tanabe, M. (2012). "KEGG for integration and interpretation of large-scale molecular data sets." Nucleic Acids Res 40:D109-D114. Pubmed: 22080510
Keseler, I. M., Collado-Vides, J., Santos-Zavaleta, A., Peralta-Gil, M., Gama-Castro, S., Muniz-Rascado, L., Bonavides-Martinez, C., Paley, S., Krummenacker, M., Altman, T., Kaipa, P., Spaulding, A., Pacheco, J., Latendresse, M., Fulcher, C., Sarker, M., Shearer, A. G., Mackie, A., Paulsen, I., Gunsalus, R. P., Karp, P. D. (2011). "EcoCyc: a comprehensive database of Escherichia coli biology." Nucleic Acids Res 39:D583-D590. Pubmed: 21097882
Kouremenou-Dona E, Dona A, Papoutsis J, Spiliopoulou C: Copper and zinc concentrations in serum of healthy Greek adults. Sci Total Environ. 2006 Apr 15;359(1-3):76-81. Epub 2005 Jun 13. Pubmed: 15955548
Lukaski HC: Low dietary zinc decreases erythrocyte carbonic anhydrase activities and impairs cardiorespiratory function in men during exercise. Am J Clin Nutr. 2005 May;81(5):1045-51. Pubmed: 15883427
Mankad M, Sathawara NG, Doshi H, Saiyed HN, Kumar S: Seminal plasma zinc concentration and alpha-glucosidase activity with respect to semen quality. Biol Trace Elem Res. 2006 May;110(2):97-106. Pubmed: 16757839
Mocchegiani E, Costarelli L, Giacconi R, Cipriano C, Muti E, Rink L, Malavolta M: Zinc homeostasis in aging: two elusive faces of the same "metal". Rejuvenation Res. 2006 Summer;9(2):351-4. Pubmed: 16706668
Rakicioglu N, Samur G, Topcu A, Topcu AA: The effect of Ramadan on maternal nutrition and composition of breast milk. Pediatr Int. 2006 Jun;48(3):278-83. Pubmed: 16732795
Religa D, Strozyk D, Cherny RA, Volitakis I, Haroutunian V, Winblad B, Naslund J, Bush AI: Elevated cortical zinc in Alzheimer disease. Neurology. 2006 Jul 11;67(1):69-75. Pubmed: 16832080
Santarelli L, Di Lorenzo L, Valentino M, Bracci M, Rapisarda V, Cassano F, Elia G, Martino MG, Neri G, Apostoli P, Soleo L: [Reduced thymulin production during occupational exposure to lead] G Ital Med Lav Ergon. 2005 Jan-Mar;27 Suppl 1:68-72. Pubmed: 15915658
Scheplyagina LA: Impact of the mother's zinc deficiency on the woman's and newborn's health status. J Trace Elem Med Biol. 2005;19(1):29-35. Pubmed: 16240669
Shea-Budgell M, Dojka M, Nimmo M, Lee D, Xu Z: Marginal zinc deficiency increased the susceptibility to acute lipopolysaccharide-induced liver injury in rats. Exp Biol Med (Maywood). 2006 May;231(5):553-8. Pubmed: 16636303
Skarupskiene I, Kuzminskis V, Abdrachmanovas O, Ryselis S, Smalinskiene A: [Zinc and aluminum concentrations in blood of hemodialysis patients and its impact on the frequency of infections] Medicina (Kaunas). 2005;41 Suppl 1:65-8. Pubmed: 15901979
Tsuruoka S, Wakaumi M, Ioka T, Yamamoto H, Ando H, Sugimoto K, Fujimura A: Angiotensin II receptor blocker-induces blunted taste sensitivity: comparison of candesartan and valsartan. Br J Clin Pharmacol. 2005 Aug;60(2):204-7. Pubmed: 16042674

Synthesis Reference:

Not Available

Material Safety Data Sheet (MSDS)

Download (PDF)

Links

External Links:

Resource	Link
CHEBI ID	30185
HMDB ID	HMDB01303
Pubchem Compound ID	23994
Kegg ID	C00038
ChemSpider ID	29723
Wikipedia	Zinc
BioCyc ID	ZN+2
EcoCyc ID	ZN+2
Ligand Expo	ZN2

Enzymes

Protein Details

1. Lead, cadmium, zinc and mercury-transporting ATPase

General function:: Involved in nucleotide binding
Specific function:: Involved in export of lead, cadmium, zinc and mercury
Gene Name:: zntA
Uniprot ID:: P37617
Molecular weight:: 76839

Reactions

ATP + H(2)O + Cd(2+)(In) = ADP + phosphate + Cd(2+)(Out).
ATP + H(2)O + Zn(2+)(In) = ADP + phosphate + Zn(2+)(Out).

Protein Details

2. Zinc import ATP-binding protein ZnuC

General function:: Involved in nucleotide binding
Specific function:: Part of the ABC transporter complex ZnuABC involved in zinc import. Responsible for energy coupling to the transport system
Gene Name:: znuC
Uniprot ID:: P0A9X1
Molecular weight:: 27867

Protein Details

3. High-affinity zinc uptake system membrane protein znuB

General function:: Involved in ATP binding
Specific function:: Involved in the high-affinity zinc uptake transport system
Gene Name:: znuB
Uniprot ID:: P39832
Molecular weight:: 27728

Protein Details

4. High-affinity zinc uptake system protein znuA

General function:: Involved in metal ion binding
Specific function:: Involved in the high-affinity zinc uptake transport system
Gene Name:: znuA
Uniprot ID:: P39172
Molecular weight:: 33777

Transporters

Protein Details

1. Zinc transporter zupT

General function:: Involved in metal ion transmembrane transporter activity
Specific function:: Mediates zinc uptake. May also transport other divalent cations
Gene Name:: zupT
Uniprot ID:: B1XG45
Molecular weight:: 26484

Protein Details

2. Zinc transporter zupT

General function:: Involved in metal ion transmembrane transporter activity
Specific function:: Mediates zinc uptake. May also transport other divalent cations
Gene Name:: zupT
Uniprot ID:: C4ZQV8
Molecular weight:: 26484

Protein Details

3. Zinc transporter zupT

General function:: Involved in metal ion transmembrane transporter activity
Specific function:: Mediates zinc uptake. May also transport other divalent cations such as copper and cadmium ions
Gene Name:: zupT
Uniprot ID:: P0A8H3
Molecular weight:: 26484

Protein Details

4. Zinc transporter zitB

General function:: Involved in cation transmembrane transporter activity
Specific function:: Involved in zinc efflux across the cytoplasmic membrane, thus reducing zinc accumulation in the cytoplasm and rendering bacteria more resistant to zinc. It may contribute to zinc homeostasis at low concentrations of zinc, whereas zntA is required for growth at more toxic concentrations
Gene Name:: zitB
Uniprot ID:: P75757
Molecular weight:: 34678

Protein Details

5. Zinc import ATP-binding protein ZnuC

General function:: Involved in nucleotide binding
Specific function:: Part of the ABC transporter complex ZnuABC involved in zinc import. Responsible for energy coupling to the transport system
Gene Name:: znuC
Uniprot ID:: P0A9X1
Molecular weight:: 27867

Protein Details

6. Outer membrane protein N

General function:: Involved in transporter activity
Specific function:: Non-specific porin
Gene Name:: ompN
Uniprot ID:: P77747
Molecular weight:: 41220

Protein Details

7. Ferrous-iron efflux pump fieF

General function:: Involved in cation transmembrane transporter activity
Specific function:: Iron-efflux transporter responsible for iron detoxification. Also able to transport Zn(2+) in a proton- dependent manner
Gene Name:: fieF
Uniprot ID:: P69380
Molecular weight:: 32927

Protein Details

8. Outer membrane pore protein E

General function:: Involved in transporter activity
Specific function:: Uptake of inorganic phosphate, phosphorylated compounds, and some other negatively charged solutes
Gene Name:: phoE
Uniprot ID:: P02932
Molecular weight:: 38922

Protein Details

9. High-affinity zinc uptake system membrane protein znuB

General function:: Involved in ATP binding
Specific function:: Involved in the high-affinity zinc uptake transport system
Gene Name:: znuB
Uniprot ID:: P39832
Molecular weight:: 27728

Protein Details

10. Outer membrane protein F

General function:: Involved in transporter activity
Specific function:: OmpF is a porin that forms passive diffusion pores which allow small molecular weight hydrophilic materials across the outer membrane. It is also a receptor for the bacteriophage T2
Gene Name:: ompF
Uniprot ID:: P02931
Molecular weight:: 39333

Protein Details

11. High-affinity zinc uptake system protein znuA

General function:: Involved in metal ion binding
Specific function:: Involved in the high-affinity zinc uptake transport system
Gene Name:: znuA
Uniprot ID:: P39172
Molecular weight:: 33777

Protein Details

12. Outer membrane protein C

General function:: Involved in transporter activity
Specific function:: Forms passive diffusion pores which allow small molecular weight hydrophilic materials across the outer membrane
Gene Name:: ompC
Uniprot ID:: P06996
Molecular weight:: 40368

Zinc (ECMDB01303) (M2MDB000330)

Structure for #<Compound:0xabb827b0>

Enzymes

Reactions

Transporters