Lead (CED0000002)

Record Information

Version

1.0

Creation Date

2009-03-06 18:57:54 UTC

Update Date

2026-04-06 04:22:59 UTC

Accession Number

CHEM000002

Identification

Common Name

Lead

Class

Small Molecule

Description

Lead belongs to the homogeneous post-transition metal compounds, a class of homogeneous metal compounds within the inorganic compounds. It is an exogenous solid with the formula Pb and an average molecular weight of 207.20 g/mol. Industrial applications include its use as a lubricating agent and as a degradant or impurity. In the context of plastics, lead is used in polyurethane, polyamide, acrylonitrile butadiene styrene, expanded polystyrene, low-density polyethylene, and high-density polyethylene; it is present in polyvinyl chloride and high impact polystyrene, and is released in polycarbonate, polystyrene, polyethylene, and polyethylene terephthalate. Lead is a biological neurotoxin associated with cancer (PMC11827045). Exposure occurs through inhalation, touch, and oral routes, with recorded sources including food contact materials, food processing and cookware (such as the processing of meats and fish, and fermentation processes for molasses and beer), and electrical and electronic equipment (including antennas, amplifiers, contacts, electric switches, and discharge lamps). The compound interacts with 26 recorded protein targets. It binds to sodium/potassium-transporting ATPases (ATP1A1, ATP1A2, ATP1A3, ATP1A4, and four others). It competitively inhibits calcium at protein kinase C (including PRKCA, PRKCB, PRKCD, PRKCI, and two others), which alters the blood-brain barrier and impairs brain microvascular function. Lead exhibits competitive inhibition at the NMDA receptor (including GRIN1, GRIN2A, GRIN2B, GRIN3B, and three others), affecting neurotransmitter release. It also inhibits ferrochelatase, mitochondrial (FECH) and delta-aminolevulinic acid dehydratase (ALAD), preventing the biosynthesis of heme. Additionally, lead binds to ACBP, thymosin beta-4, and calmodulin; the latter interference with calcium binding alters cAMP messenger pathways and neurotransmitter release.

Contaminant Type

Cigarette Toxin
Food Toxin
Household Toxin
Human Neurotoxin
Industrial/Workplace Toxin
Inorganic Compound
Lead Compound
Metabolite
Metal
Natural Compound
Pollutant

Chemical Structure

MOL SDF PDB SMILES InChI

Synonyms

Value	Source
LEAD (II) ion	ChEBI
Lead, ion (PB2+)	ChEBI
Pb	ChEBI
PB(2+)	ChEBI
PB2+	ChEBI
Glover	HMDB
haro Mix MH-204	HMDB
Lead ion (PB2+)	HMDB
Lead(2+) ion	HMDB
Omaha	HMDB
Plumbum	HMDB, ChEBI
Methyl 2-bromo-6-(((2-(5,6-dihydro-1,4,2-dioxazin-3-yl)-2-((4-(4-nitrophenyl)-1,3-thiazol-2-yl)amino)ethyl)sulfanyl)-methyl)-5-hydroxy-3-methoxybenzoate	MeSH, HMDB
82PB	ChEBI
Blei	ChEBI
Plomb	ChEBI
Plomo	ChEBI

Chemical Formula

Average Molecular Mass

207.200 g/mol

Monoisotopic Mass

207.977 g/mol

CAS Registry Number

7439-92-1

IUPAC Name

λ²-lead(2+) ion

Traditional Name

λ²-lead(2+) ion

SMILES

[Pb++]

InChI Identifier

InChI=1S/Pb/q+2

InChI Key

RVPVRDXYQKGNMQ-UHFFFAOYSA-N

Chemical Taxonomy

Description

Belongs to the class of inorganic compounds known as homogeneous post-transition metal compounds. These are inorganic compounds containing only metal atoms,with the largest atom being a post-transition metal atom.

Kingdom

Inorganic compounds

Super Class

Homogeneous metal compounds

Class

Homogeneous post-transition metal compounds

Sub Class

Not Available

Direct Parent

Homogeneous post-transition metal compounds

Alternative Parents

Not Available

Substituents

Homogeneous post-transition metal

Molecular Framework

Not Available

External Descriptors

monoatomic dication (CHEBI:49807 )
divalent metal cation (CHEBI:49807 )
lead cation (CHEBI:49807 )
a cation (PB+2 )

Biological Properties

Status

Detected and Not Quantified

Origin

Exogenous

Cellular Locations

Cytoplasm
Extracellular

Biofluid Locations

Not Available

Tissue Locations

Not Available

Applications

Not Available

Biological Roles

neurotoxin

Chemical Roles

Not Available

Organoleptic Effects

Not Available

Physical Properties

State

Solid

Appearance

Bluish-white metallic solid, turns grey when exposed to air.

Experimental Properties

Property	Value
Melting Point	327.5°C
Boiling Point	1740 °C
Solubility	Not Available

Predicted Properties

Property	Value	Source
logP	0.03	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	Yes	ChemAxon
Rule of Five	Yes	ChemAxon
Ghose Filter	No	ChemAxon
Veber's Rule	Yes	ChemAxon
MDDR-like Rule	No	ChemAxon

Spectra

Spectrum Type	Description	Splash Key	Deposition Date	View
Predicted LC-MS/MS	Predicted LC-MS/MS Spectrum	splash10-014i-0090000000-123b547ace2c14730ca1	Not Available	View Spectrum
Predicted LC-MS/MS	Predicted LC-MS/MS Spectrum	splash10-014i-0090000000-123b547ace2c14730ca1	Not Available	View Spectrum
Predicted LC-MS/MS	Predicted LC-MS/MS Spectrum	splash10-014i-0090000000-123b547ace2c14730ca1	Not Available	View Spectrum
Predicted LC-MS/MS	Predicted LC-MS/MS Spectrum	splash10-03di-0090000000-5199439513f6f28b5c21	Not Available	View Spectrum
Predicted LC-MS/MS	Predicted LC-MS/MS Spectrum	splash10-03di-0090000000-5199439513f6f28b5c21	Not Available	View Spectrum
Predicted LC-MS/MS	Predicted LC-MS/MS Spectrum	splash10-03di-0090000000-5199439513f6f28b5c21	Not Available	View Spectrum

Toxicity Profile

Mechanism of Toxicity

Lead mimics other biologically important metals, such as zinc, calcium, and iron, competing as cofactors for many of their respective enzymatic reactions. For example, lead has been shown to competitively inhibit calcium's binding of calmodulin, interferring with neurotransmitter release. It exhibits similar competitive inhibition at the NMDA receptor and protein kinase C, which impairs brain microvascular formation and function, as well as alters the blood-brain barrier. Lead also affects the nervous system by impairing regulation of dopamine synthesis and blocking evoked release of acetylcholine. However, it's main mechanism of action occurs by inhibiting delta-aminolevulinic acid dehydratase, an enzyme vital in the biosynthesis of heme, which is a necesssary cofactor of hemoglobin. (11, 2, 4, 10) At blood lead levels between 25 and 60 μg/dL, neuropsychiatric effects such as delayed reaction times, irritability, and difficulty concentrating, as well as slowed motor nerve conduction and headache can occur. Anemia may appear at blood lead levels higher than 50 μg/dL. In adults, Abdominal colic, involving paroxysms of pain, may appear at blood lead levels greater than 80 μg/dL.

Carcinogenicity (IARC Classification)

2B, possibly carcinogenic to humans. (9)

Minimum Risk Level

Chronic Inhalation: 0.05 mg/m3 (8)

Symptoms

Symptoms of chronic lead poisoning include reduced cognitive abilities, nausea, abdominal pain, irritability, insomnia, metal taste in the mouth, excess lethargy or hyperactivity, chest pain, headache and, in extreme cases, seizures, comas, and death. There are also associated gastrointestinal problems, such as constipation, diarrhea, vomiting, poor appetite, weight loss, which are common in acute poisoning. (1, 7)

Treatment

Lead poisoning is usually treated with chelation therapy using DMSA, EDTA, or dimercaprol. (7)

Toxicity Values

Not Available

Health Effects

Health Effect	Relationship	Direction	Reference
cancer	associated_with	Not Available	PMC11827045

Exposure Sources

Source ID	Source	Sector	Reference
494	Food contact materials	Food, food processing & cookware	Not Available
505	Amplifiers	Electrical & Electronic Equipment	Not Available
506	Antennas	Electrical & Electronic Equipment	Not Available
512	Contacts	Electrical & Electronic Equipment	Not Available
514	Discharge Lamps	Electrical & Electronic Equipment	Not Available
517	Electric Switches	Electrical & Electronic Equipment	Not Available
520	Emergency Protective Devices	Electrical & Electronic Equipment	Not Available
527	Magnets	Electrical & Electronic Equipment	Not Available
529	Power Cables	Electrical & Electronic Equipment	Not Available
530	Radio Transmission Systems	Electrical & Electronic Equipment	Not Available
536	Superconductive Or Hyperconductive Conductors Cables Or Transmission Lines	Electrical & Electronic Equipment	Not Available
537	Television Systems	Electrical & Electronic Equipment	Not Available
538	Thin Magnetic Films	Electrical & Electronic Equipment	Not Available
544	Fermentation Processes For Beer	Food, food processing & cookware	Not Available
546	Molasses And Treatment Of Molasses	Food, food processing & cookware	Not Available
551	Processing Fish	Food, food processing & cookware	Not Available
552	Processing Meats	Food, food processing & cookware	Not Available
553	Treatment Of Hops	Food, food processing & cookware	Not Available
579	Manufacture Of Iron Or Steel	Industrial manufacturing & chemical processing	Not Available
581	Paper Making Machines	Industrial manufacturing & chemical processing	Not Available
584	Buoys	Marine, shipping & aquaculture	Not Available
592	Marine Propulsion Or Steering	Marine, shipping & aquaculture	Not Available
597	Chemosterilants	Agriculture & land management	Not Available
602	Molluscicides	Agriculture & land management	Not Available
604	Pest Attractants	Agriculture & land management	Not Available
607	Rodenticides(1)	Agriculture & land management	Not Available
608	Rodenticides	Agriculture & land management	Not Available
638	Decorating Textiles	Textiles, leather & furnishings	Not Available
643	Headwear	Textiles, leather & furnishings	Not Available
653	Sewing	Textiles, leather & furnishings	Not Available

Pathways

0 pathways

No pathways found

No metabolic pathways have been associated with this synthetic chemical

Targets

Structure	Protein	UniProt ID	Organism	Relationship	Details
Click to view 3D structure	Acyl-CoA-binding protein	P07108	Humans	Known	Lead is known to bind ACBP, which is responsible for the regulation of various processes such as acyl-CoA metabolism, GABA-A/benzodiazepine receptor modulation, steroidogenesis, intestinal cholecystokinin release, and insulin secretion. (A21)
Click to view 3D structure	Ceruloplasmin	P00450	Humans	Known	Not Available
Click to view 3D structure	Delta-aminolevulinic acid dehydratase	P13716	Humans	Known	Lead inhibition of ALAD prevents the biosynthesis of heme, which is a necesssary cofactor of hemoglobin. (L21)
Click to view 3D structure	Ferrochelatase, mitochondrial	P22830	Humans	Known	Lead inhibition of ferrochelatase prevents the biosynthesis of heme, which is a necesssary cofactor of hemoglobin. (L21)
Click to view 3D structure	Glutamate receptor ionotropic, NMDA 1	Q05586	Humans	Known	Lead exhibits competitive inhibition at the NMDA receptor, affecting neurotransmitter release. (A22)
Click to view 3D structure	Glutamate receptor ionotropic, NMDA 2A	Q12879	Humans	Known	Lead exhibits competitive inhibition at the NMDA receptor, affecting neurotransmitter release. (A22)
Click to view 3D structure	Glutamate receptor ionotropic, NMDA 2B	Q13224	Humans	Known	Lead exhibits competitive inhibition at the NMDA receptor, affecting neurotransmitter release. (A22)
Click to view 3D structure	Glutamate receptor ionotropic, NMDA 2C	Q14957	Humans	Known	Lead exhibits competitive inhibition at the NMDA receptor, affecting neurotransmitter release. (A22)
Click to view 3D structure	Glutamate receptor ionotropic, NMDA 2D	O15399	Humans	Known	Lead exhibits competitive inhibition at the NMDA receptor, affecting neurotransmitter release. (A22)
Click to view 3D structure	Glutamate receptor ionotropic, NMDA 3A	Q8TCU5	Humans	Known	Lead exhibits competitive inhibition at the NMDA receptor, affecting neurotransmitter release. (A22)
Click to view 3D structure	Glutamate receptor ionotropic, NMDA 3B	O60391	Humans	Known	Lead exhibits competitive inhibition at the NMDA receptor, affecting neurotransmitter release. (A22)
Click to view 3D structure	Protein kinase C alpha type	P17252	Humans	Known	Lead exhibits competitive inhibition with calcium at protein kinase C, which impairs brain microvascular formation and function, as well as alters the blood-brain barrier. (L136)
Click to view 3D structure	Protein kinase C beta type	P05771	Humans	Known	Lead exhibits competitive inhibition with calcium at protein kinase C, which impairs brain microvascular formation and function, as well as alters the blood-brain barrier. (L136)
Click to view 3D structure	Protein kinase C delta type	Q05655	Humans	Known	Lead exhibits competitive inhibition with calcium at protein kinase C, which impairs brain microvascular formation and function, as well as alters the blood-brain barrier. (L136)
Click to view 3D structure	Protein kinase C epsilon type	Q02156	Humans	Known	Lead exhibits competitive inhibition with calcium at protein kinase C, which impairs brain microvascular formation and function, as well as alters the blood-brain barrier. (L136)
Click to view 3D structure	Protein kinase C iota type	P41743	Humans	Known	Lead exhibits competitive inhibition with calcium at protein kinase C, which impairs brain microvascular formation and function, as well as alters the blood-brain barrier. (L136)
Click to view 3D structure	Protein kinase C theta type	Q04759	Humans	Known	Lead exhibits competitive inhibition with calcium at protein kinase C, which impairs brain microvascular formation and function, as well as alters the blood-brain barrier. (L136)
Click to view 3D structure	Serotransferrin	P02787	Humans	Known	Not Available
Click to view 3D structure	Sodium/potassium-transporting ATPase subunit alpha-1	P05023	Humans	Known	Lead binds to sodium/potassium-transporting ATPases. (A24)
Click to view 3D structure	Sodium/potassium-transporting ATPase subunit alpha-2	P50993	Humans	Known	Lead binds to sodium/potassium-transporting ATPases. (A24)
Click to view 3D structure	Sodium/potassium-transporting ATPase subunit alpha-3	P13637	Humans	Known	Lead binds to sodium/potassium-transporting ATPases. (A24)
Click to view 3D structure	Sodium/potassium-transporting ATPase subunit alpha-4	Q13733	Humans	Known	Lead binds to sodium/potassium-transporting ATPases. (A24)
Click to view 3D structure	Sodium/potassium-transporting ATPase subunit beta-1	P05026	Humans	Known	Lead binds to sodium/potassium-transporting ATPases. (A24)
Click to view 3D structure	Sodium/potassium-transporting ATPase subunit beta-2	P14415	Humans	Known	Lead binds to sodium/potassium-transporting ATPases. (A24)
Click to view 3D structure	Sodium/potassium-transporting ATPase subunit beta-3	P54709	Humans	Known	Lead binds to sodium/potassium-transporting ATPases. (A24)
Click to view 3D structure	Sodium/potassium-transporting ATPase subunit gamma	P54710	Humans	Known	Lead binds to sodium/potassium-transporting ATPases. (A24)