Iron

Identification

Summary

Iron is an essential element commonly used for the treatment of patients with documented iron deficiency.

Brand Names
Citranatal B-calm Kit, Citranatal Harmony, Concept Ob, Ferralet 90, Natafort, Vitafol-one
Generic Name
Iron
DrugBank Accession Number
DB01592
Background

A metallic element found in certain minerals, in nearly all soils, and in mineral waters. It is an essential constituent of hemoglobin, cytochrome, and other components of respiratory enzyme systems. Its chief functions are in the transport of oxygen to tissue (hemoglobin) and in cellular oxidation mechanisms. Depletion of iron stores may result in iron-deficiency anemia. Iron is used to build up the blood in anemia.

Type
Small Molecule
Groups
Approved
Structure
Weight
Average: 55.845
Monoisotopic: 55.934942133
Chemical Formula
Fe
Synonyms
  • Carbonyl iron
  • Eisen
  • Electrolytic iron
  • Fe
  • fer
  • Ferrum
  • Ferrum metallicum
  • Hierro
  • Iron powder
  • Iron, carbonyl
  • Iron, electrolytic
  • Iron, elemental
  • Iron, reduced
  • Reduced iron

Pharmacology

Indication

Used in preventing and treating iron-deficiency anemia.

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Associated Conditions
Indication TypeIndicationCombined Product DetailsApproval LevelAge GroupPatient CharacteristicsDose Form
Used in combination to treatAnemiaCombination Product in combination with: Ascorbic acid (DB00126)••••••••••••••••••• •••••••• •••••••
Used in combination to manageAnemia post chemotherapyRegimen in combination with: Iron sucrose (DB09146)••• ••••••••••••••
Used in combination to treatIron deficiencyCombination Product in combination with: Dextran (DB09255)•••••••••••••••••••••••• •••••••• •• •••• ••••••••••••
Used in combination to treatIron deficiencyCombination Product in combination with: Dextran (DB09255)••••••••••••••••••••••• •• •••• •••• ••••••••••••••••••••
Used in combination to treatIron deficiencyCombination Product in combination with: Dextran (DB09255)••••••••••••••••••••••• ••• ••••• •••• ••••••••••••••••
Associated Therapies
Contraindications & Blackbox Warnings
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Pharmacodynamics

The major activity of supplemental iron is in the prevention and treatment of iron deficiency anemia. Iron has putative immune-enhancing, anticarcinogenic and cognition-enhancing activities.

Mechanism of action

Iron is necessary for the production of hemoglobin. Iron-deficiency can lead to decreased production of hemoglobin and a microcytic, hypochromic anemia.

TargetActionsOrganism
AHemoglobin subunit alpha
activator
Humans
UTransferrin receptor protein 1Not AvailableHumans
UEgl nine homolog 1Not AvailableHumans
UHistone deacetylase 8
cofactor
Humans
UAlpha-hemoglobin-stabilizing proteinNot AvailableHumans
UFrataxin, mitochondrialNot AvailableHumans
UFerritin heavy chainNot AvailableHumans
UFlap endonuclease 1Not AvailableHumans
UEndonuclease 8-like 1Not AvailableHumans
UEndonuclease 8-like 2Not AvailableHumans
UDNA polymerase betaNot AvailableHumans
UCeruloplasminNot AvailableHumans
USerotransferrinNot AvailableHumans
Absorption

The efficiency of absorption depends on the salt form, the amount administered, the dosing regimen and the size of iron stores. Subjects with normal iron stores absorb 10% to 35% of an iron dose. Those who are iron deficient may absorb up to 95% of an iron dose.

Volume of distribution

Not Available

Protein binding

Not Available

Metabolism
Not Available
Route of elimination

Not Available

Half-life

Not Available

Clearance

Not Available

Adverse Effects
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Toxicity

Acute iron overdosage can be divided into four stages. In the first stage, which occurs up to six hours after ingestion, the principal symptoms are vomiting and diarrhea. Other symptoms include hypotension, tachycardia and CNS depression ranging from lethargy to coma. The second phase may occur at 6-24 hours after ingestion and is characterized by a temporary remission. In the third phase, gastrointestinal symptoms recur accompanied by shock, metabolic acidosis, coma, hepatic necrosis and jaundice, hypoglycemia, renal failure and pulmonary edema. The fourth phase may occur several weeks after ingestion and is characterized by gastrointestinal obstruction and liver damage. In a young child, 75 milligrams per kilogram is considered extremely dangerous. A dose of 30 milligrams per kilogram can lead to symptoms of toxicity. Estimates of a lethal dosage range from 180 milligrams per kilogram and upwards. A peak serum iron concentration of five micrograms or more per ml is associated with moderate to severe poisoning in many.

Pathways
PathwayCategory
Nucleotide Sugars MetabolismMetabolic
Cysteine MetabolismMetabolic
Oxidation of Branched-Chain Fatty AcidsMetabolic
Tryptophan MetabolismMetabolic
Lovastatin Action PathwayDrug action
Cerivastatin Action PathwayDrug action
Aromatic L-Aminoacid Decarboxylase DeficiencyDisease
PhenylketonuriaDisease
HypercholesterolemiaDisease
Zellweger SyndromeDisease
Vitamin A DeficiencyDisease
Hereditary Coproporphyria (HCP)Disease
Congenital Erythropoietic Porphyria (CEP) or Gunther DiseaseDisease
Chondrodysplasia Punctata II, X-Linked Dominant (CDPX2)Disease
Smith-Lemli-Opitz Syndrome (SLOS)Disease
Galactosemia IIIDisease
Mevalonic AciduriaDisease
Glucose-6-phosphate Dehydrogenase DeficiencyDisease
Congenital Disorder of Glycosylation CDG-IIdDisease
Cystinosis, Ocular NonnephropathicDisease
The Oncogenic Action of FumarateDisease
Tyrosine MetabolismMetabolic
Inositol MetabolismMetabolic
Catecholamine BiosynthesisMetabolic
Taurine and Hypotaurine MetabolismMetabolic
Porphyrin MetabolismMetabolic
Pentose Phosphate PathwayMetabolic
Galactose MetabolismMetabolic
Pyrimidine MetabolismMetabolic
Simvastatin Action PathwayDrug action
Pharmacogenomic Effects/ADRs
Not Available

Interactions

Drug Interactions
This information should not be interpreted without the help of a healthcare provider. If you believe you are experiencing an interaction, contact a healthcare provider immediately. The absence of an interaction does not necessarily mean no interactions exist.
DrugInteraction
AlmasilateAlmasilate can cause a decrease in the absorption of Iron resulting in a reduced serum concentration and potentially a decrease in efficacy.
Aluminium phosphateAluminium phosphate can cause a decrease in the absorption of Iron resulting in a reduced serum concentration and potentially a decrease in efficacy.
Aluminum hydroxideAluminum hydroxide can cause a decrease in the absorption of Iron resulting in a reduced serum concentration and potentially a decrease in efficacy.
BenazeprilThe risk or severity of adverse effects can be decreased when Iron is combined with Benazepril.
Calcium phosphate dihydrateIron can cause a decrease in the absorption of Calcium phosphate dihydrate resulting in a reduced serum concentration and potentially a decrease in efficacy.
Food Interactions
  • Take with or without food. Many different products contain iron; refer to the product monograph for more specific instruction. Taking iron with food may reduce gastric irritation.

Products

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Active Moieties
NameKindUNIICASInChI Key
Ferrous cationionicGW89581OWR15438-31-0CWYNVVGOOAEACU-UHFFFAOYSA-N
Product Images
International/Other Brands
Ed-In-Sol / Fe-40 / Feosol (GlaxoSmithkline) / Feostat / Fer-In-Sol / Feratab (Upsher-Smith) / Ferate / Fergon / Ferralet / Ferretts / Ferro sanol / Ferro-Caps / Ferro-Time / Ferrousal / Siderol / Simron / Slow Fe / Vitedyn-Slo / Yieronia
Brand Name Prescription Products
NameDosageStrengthRouteLabellerMarketing StartMarketing EndRegionImage
Iron ChewsTablet, chewable15 mg/1OralMayne Pharma Inc.2009-01-012016-12-31US flag
Over the Counter Products
NameDosageStrengthRouteLabellerMarketing StartMarketing EndRegionImage
Chelated Iron 25mg - CapletTablet25 mgOralHealth Wise Nutrition Inc.1995-12-312002-07-18Canada flag
Chelated Iron Supplement - TabTablet18 mgOralAlbion1996-09-062002-09-30Canada flag
Chelated Iron Tab 25mgTablet25 mgOralGahler Enterprises Ltd.1984-12-312008-07-17Canada flag
Fe-chelate TabTablet28 mgOralNutri West Products Ltd.1994-12-311997-08-05Canada flag
Fera Liq 16.7mg/15mlLiquid16.7 mg / 15 mLOralInno Vite Incorporated1987-12-312007-07-31Canada flag
Mixture Products
NameIngredientsDosageRouteLabellerMarketing StartMarketing EndRegionImage
ActyformIron (4.18 mg) + Copper (1 mg) + Magnesium (61.15 mg) + Zinc (9 mg)CapsuleOralTechnodiet S.E.N.C.1999-10-262008-08-13Canada flag
Advanced B & T FormulaIron (1.67 mg) + Ascorbic acid (33.3 mg) + Calcium (200 mg) + Chromium (33.33 mcg) + Copper (0.5 mg) + Cyanocobalamin (6.67 mcg) + Folic acid (0.133 mg) + Magnesium (83.3 mg) + Manganese cation (3.33 mg) + Nicotinamide (6.67 mg) + Calcium pantothenate (5 mg) + Phosphorus (100 mg) + Potassium (16.67 mg) + Pyridoxine hydrochloride (6.67 mg) + Riboflavin (2.67 mg) + Selenium (33.33 mcg) + Silicon (0.333 mg) + Sodium molybdate (16.67 mcg) + Thiamine (2.67 mg) + Vanadium (8.33 mg) + Vitamin D (66.67 unit) + Zinc (5 mg)CapsuleOralNutraceutical CorporationNot applicableNot applicableCanada flag
APPETON TEENGROWIron (10 mg) + Ascorbic acid (100 mg) + Calcium (150 mg) + Cholecalciferol (200 IU) + Copper (0.7 mg) + Cyanocobalamin (6 mcg) + Folic acid (0.4 mg) + Iodine (0.749 mcg) + Magnesium (6.13 mg) + Manganese cation (0.56 mg) + Nicotinamide (20 mg) + Potassium (4.98 mg) + Pyridoxine (4 mg) + Riboflavin (3 mg) + Thiamine (3 mg) + Vitamin A (2500 IU) + Vitamin E (15 IU) + Zinc (0.51 mg)CapsuleOralKOTRA PHARMA (M) SDN. BHD.2020-09-082024-06-28Malaysia flag
BiO-LiFE Ginsomin Softgel CapsulesIron (15 mg) + Ascorbic acid (60 mg) + Beta carotene (6 mg) + Calcium phosphate, dibasic (255 mg) + Copper (2 mg) + Cyanocobalamin (2 µg) + Folic acid (200 µg) + Ginseng (50 mg) + Magnesium (4 mg) + Manganese cation (1 mg) + Nicotinamide (20 mg) + Calcium pantothenate (6 mg) + Potassium (3.5 µg) + Pyridoxine (2 mg) + Riboflavin (1.5 mg) + Selenium (35 µg) + Thiamine (1.5 mg) + Vitamin D (200 IU) + Vitamin E (15 IU) + Zinc (5 mg)CapsuleOralMega Lifesciences Indonesia2020-09-08Not applicableMalaysia flag
BIOGROW BMIron (225 mcg) + Aminobenzoic acid (5 mg) + Biotin (150 mcg) + Choline (20 mg) + Chromium (25 mcg) + Copper (25 mcg) + Cyanocobalamin (6 mcg) + Folic acid (250 mcg) + Inositol (20 mg) + Magnesium (5 mg) + Manganese cation (250 mcg) + Molybdenum (5 mcg) + Nicotinamide (25 mg) + Pantothenic acid (10 mg) + Pyridoxine (12.5 mg) + Riboflavin (5 mg) + Thiamine (5 mg) + Zinc (150 mcg)Tablet, film coatedOralUNISON NUTRACEUTICALS SDN. BHD.2020-09-08Not applicableMalaysia flag
Unapproved/Other Products
NameIngredientsDosageRouteLabellerMarketing StartMarketing EndRegionImage
Active FEIron (75 mg/1) + Ascorbic acid (160 mg/1) + Beta carotene (2100 [iU]/1) + Cholecalciferol (400 [iU]/1) + Cupric oxide (1 mg/1) + Cyanocobalamin (30 ug/1) + DL-alpha tocopheryl acetate (40 [iU]/1) + Folic acid (1250 ug/1) + Magnesium oxide (30 mg/1) + Nicotinamide (20 mg/1) + Pyridoxine hydrochloride (20 mg/1) + Riboflavin (4 mg/1) + Thiamine hydrochloride (4 mg/1) + Zinc oxide (20 mg/1)TabletOralGM Pharmaceuticals, INC2013-11-11Not applicableUS flag
Active OBIron (20 mg/1) + Ascorbic acid (100 mg/1) + Cholecalciferol (400 [iU]/1) + Cupric sulfate pentahydrate (2 mg/1) + Cyanocobalamin (30 ug/1) + D-alpha-Tocopherol acetate (30 [iU]/1) + Doconexent (320 mg/1) + Folic acid (1 mg/1) + Pyridoxine hydrochloride (20 mg/1) + Riboflavin (4 mg/1) + Thiamine mononitrate (2 mg/1) + Zinc oxide (30 mg/1)Capsule, liquid filledOralGM Pharmaceuticals, INC2013-10-282017-03-31US flag
BioFerr 90Iron (88.5 mg/1) + Ascorbic acid (138 mg/1) + Cyanocobalamin (16.8 ug/1) + Docusate sodium (55 mg/1) + Ferrous gluconate dihydrate (13.2 mg/1) + Folic acid (1.4 mg/1)Tablet, film coatedOralBiocomp Pharma, Inc.2014-07-01Not applicableUS flag
BumP DHAIron (15 mg/1) + Cobamamide (500 mg/1) + Flavin adenine dinucleotide (1 mg/1) + Flavin mononucleotide (2 mg/1) + Leucovorin (1 mg/1) + Levomefolate magnesium (1 mg/1) + Magnesium oxide (125 mg/1) + NADH (25 ug/1) + Omega-3 fatty acids (300 mg/1) + Potassium Iodide (250 ug/1) + Pyridoxal phosphate (5 mg/1) + Pyridoxine hydrochloride (20 mg/1) + Zinc glycinate (15 1/1)CapsuleOralCenturion Labs2017-03-242017-04-17US flag
Cavan AlphaIron (27 mg/1) + Ascorbic acid (120 mg/1) + Beta carotene (3000 [iU]/1) + Calcium carbonate (230 mg/1) + Cholecalciferol (800 [iU]/1) + Cupric oxide (2 mg/1) + Cyanocobalamin (12 ug/1) + DL-alpha tocopheryl acetate (3 mg/1) + Folic acid (1 mg/1) + Iodine (220 ug/1) + Magnesium oxide (25 mg/1) + Nicotinamide (20 mg/1) + Omega-3 fatty acids (300 mg/1) + Pyridoxine hydrochloride (50 mg/1) + Riboflavin (4 mg/1) + Thiamine mononitrate (1.8 mg/1) + Zinc oxide (25 mg/1)KitOralSeton Pharmaceuticals2010-07-012013-09-30US flag

Categories

ATC Codes
B03AE02 — Iron, multivitamins and folic acidA11AA01 — Multivitamins and ironB03AE01 — Iron, vitamin b12 and folic acidB03AE04 — Iron, multivitamins and mineralsB03AE03 — Iron and multivitamins
Drug Categories
Chemical TaxonomyProvided by Classyfire
Description
This compound 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.
Kingdom
Inorganic compounds
Super Class
Homogeneous metal compounds
Class
Homogeneous transition metal compounds
Sub Class
Not Available
Direct Parent
Homogeneous transition metal compounds
Alternative Parents
Not Available
Substituents
Homogeneous transition metal
Molecular Framework
Not Available
External Descriptors
elemental iron (CHEBI:82664)
Affected organisms
  • Humans and other mammals

Chemical Identifiers

UNII
E1UOL152H7
CAS number
7439-89-6
InChI Key
XEEYBQQBJWHFJM-UHFFFAOYSA-N
InChI
InChI=1S/Fe
IUPAC Name
iron
SMILES
[Fe]

References

Synthesis Reference

Walter Lugscheider, Paul Mullner, Wilhelm Schiffer, Alois Leutgob, "Arrangement for producing metals, such as molten pig iron, steel pre-material and ferroalloys." U.S. Patent US4617671, issued 0000.

US4617671
General References
Not Available
Human Metabolome Database
HMDB0015531
KEGG Compound
C00023
PubChem Compound
23925
PubChem Substance
46509190
ChemSpider
22368
RxNav
262150
ChEBI
18248
Therapeutic Targets Database
DAP001313
PharmGKB
PA450087
RxList
RxList Drug Page
Drugs.com
Drugs.com Drug Page
PDRhealth
PDRhealth Drug Page
Wikipedia
Iron
FDA label
Download (100 KB)
MSDS
Download (75.6 KB)

Clinical Trials

Clinical Trials
Clinical Trial & Rare Diseases Add-on Data Package
Explore 4,000+ rare diseases, orphan drugs & condition pairs, clinical trial why stopped data, & more. Preview package
PhaseStatusPurposeConditionsCountStart DateWhy Stopped100+ additional columns
Not AvailableActive Not RecruitingNot AvailableAutism Disorder / Iron Deficiency Anemia (IDA) / Neurodevelopmental Abnormality1somestatusstop reasonjust information to hide
Not AvailableActive Not RecruitingNot AvailableDevelopment, Child / Fetal Neurodevelopmental Disorder / Iron Deficiency Anemia (IDA) / Iron Deficiency Anemia of Pregnancy / Iron Deficiency Anemia Treatment / Neurodevelopmental Disorder of Foetus1somestatusstop reasonjust information to hide
Not AvailableActive Not RecruitingPreventionBlood Donation1somestatusstop reasonjust information to hide
Not AvailableActive Not RecruitingTreatmentHypoferritenemia Without Anemia (HWA) / Iron Deficiency Without Anemia)1somestatusstop reasonjust information to hide
Not AvailableAvailableNot AvailableIron Deficiency Anemia of Pregnancy1somestatusstop reasonjust information to hide

Pharmacoeconomics

Manufacturers
Not Available
Packagers
  • Accucaps Industries Ltd.
  • Breckenridge Pharmaceuticals
  • Cardinal Health
  • Centrix Pharmaceuticals
  • Contract Pharm
  • Cypress Pharmaceutical Inc.
  • Dayton Pharmaceuticals
  • Edwards Pharmaceuticals
  • Equipharm Inc.
  • Haupt Pharma
  • Lehigh Valley Technologies Inc.
  • Mallinckrodt Inc.
  • Marlop Pharmaceuticals Inc.
  • Midlothian Labs
  • Nature's Bounty
  • Physicians Total Care Inc.
  • Provident Pharmaceuticals LLC
  • Puretek Corp.
  • Rising Pharmaceuticals
  • River's Edge Pharmaceuticals
  • Roxmar Laboratories
  • Seyer Pharmatec Inc.
Dosage Forms
FormRouteStrength
Injection, solution, concentrateIntravenous
SolutionOral6.66 mg
SolutionOral600 mg
TabletOral60.27 mg
TabletOral25 mg
TabletOral18 mg
Kit; tablet; tablet, film coatedOral
SolutionIntravenous100 mg
SolutionIntravenous10000000 mg
Tablet
Capsule
Capsule, gelatin coated; kit; tabletOral
SolutionIntravenous100 mg/5ml
Tablet, chewableOral
TabletOral350 mcg
SyrupOral1 g
TabletOral28 mg
SolutionOral50 mg
SolutionOral1.5 g
LiquidOral16.7 mg / 15 mL
InjectionIntramuscular100 mg/2ml
CapsuleOral
Tablet, extended releaseOral
Tablet, film coatedOral50 mg
SolutionIntramuscular
SuspensionOral30 mg
SuspensionOral
GelOral
Capsule, delayed releaseOral
Tablet, delayed releaseOral
SolutionIntravenous20 mg
ElixirOral
Tablet, coatedOral
CapsuleOral40 mg
TabletOral37 mg
Tablet, chewableOral15 mg/1
TabletOral25 mg / tab
TabletOral40 mg
Tablet, chewableOral100 mg
Solution / dropsOral50 mg/ml
SolutionOral50 mg/ml
SyrupOral50 mg/5ml
Injection, solutionIntravenous
Solution / dropsOral
SolutionOral
Powder, for solutionOral
LiquidOral
CapsuleOral50 mg/1
LiquidOral15 mg/1mL
SyrupOral
Capsule, liquid filled; kit; tabletOral
Capsule, liquid filled; kit; tablet, film coatedOral
Tablet, coatedOral80 mg
Tablet, coatedOral
CapsuleOral150 mg/1
Capsule, coatedOral
TabletOral
PatchTopical0.76 g/1
Capsule, gelatin coatedOral
Tablet, effervescentOral
SolutionOral40 MG/15ML
Capsule; kit; tablet, coatedOral
Tablet, film coatedOral80 mg
Kit; tablet; tablet, coatedOral
Tablet, chewableOral500 mg
Capsule; kit; tabletOral
InjectionIntravenous100 mg/5ml
Tablet, film coatedOral
Capsule, liquid filled; kitOral
Capsule, liquid filledOral
KitOral
SuspensionOral15 mg/1.25mL
Injection, solutionIntravenous50 mg/1ml
Prices
Unit descriptionCostUnit
Iron chews 15 mg tablet chew0.29USD tablet
Ferrous sulfate 28 mg tablet0.04USD tablet
DrugBank does not sell nor buy drugs. Pricing information is supplied for informational purposes only.
Patents
Patent NumberPediatric ExtensionApprovedExpires (estimated)Region
US6667050No2003-12-232019-04-06US flag

Properties

State
Solid
Experimental Properties
PropertyValueSource
melting point (°C)1538 °CNot Available
Predicted Properties
PropertyValueSource
logP-0.77Chemaxon
Physiological Charge0Chemaxon
Hydrogen Acceptor Count0Chemaxon
Hydrogen Donor Count0Chemaxon
Polar Surface Area0 Å2Chemaxon
Rotatable Bond Count0Chemaxon
Refractivity0 m3·mol-1Chemaxon
Polarizability1.78 Å3Chemaxon
Number of Rings0Chemaxon
Bioavailability1Chemaxon
Rule of FiveYesChemaxon
Ghose FilterNoChemaxon
Veber's RuleYesChemaxon
MDDR-like RuleNoChemaxon
Predicted ADMET Features
PropertyValueProbability
Human Intestinal Absorption+0.9838
Blood Brain Barrier+0.9733
Caco-2 permeable+0.7354
P-glycoprotein substrateNon-substrate0.885
P-glycoprotein inhibitor INon-inhibitor0.9787
P-glycoprotein inhibitor IINon-inhibitor0.9858
Renal organic cation transporterNon-inhibitor0.9108
CYP450 2C9 substrateNon-substrate0.8466
CYP450 2D6 substrateNon-substrate0.8259
CYP450 3A4 substrateNon-substrate0.8158
CYP450 1A2 substrateNon-inhibitor0.8807
CYP450 2C9 inhibitorNon-inhibitor0.9373
CYP450 2D6 inhibitorNon-inhibitor0.9708
CYP450 2C19 inhibitorNon-inhibitor0.9553
CYP450 3A4 inhibitorNon-inhibitor0.988
CYP450 inhibitory promiscuityLow CYP Inhibitory Promiscuity0.882
Ames testNon AMES toxic0.9633
CarcinogenicityCarcinogens 0.664
BiodegradationReady biodegradable0.7326
Rat acute toxicity2.0135 LD50, mol/kg Not applicable
hERG inhibition (predictor I)Weak inhibitor0.9547
hERG inhibition (predictor II)Non-inhibitor0.9746
ADMET data is predicted using admetSAR, a free tool for evaluating chemical ADMET properties. (23092397)

Spectra

Mass Spec (NIST)
Not Available
Spectra
Not Available
Chromatographic Properties
Collision Cross Sections (CCS)
Not Available

Targets

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Kind
Protein
Organism
Humans
Pharmacological action
Yes
Actions
Activator
General Function
Involved in oxygen transport from the lung to the various peripheral tissues
Specific Function
heme binding
Gene Name
HBA1
Uniprot ID
P69905
Uniprot Name
Hemoglobin subunit alpha
Molecular Weight
15257.405 Da
References
  1. Zhou S, Olson JS, Fabian M, Weiss MJ, Gow AJ: Biochemical fates of alpha hemoglobin bound to alpha hemoglobin-stabilizing protein AHSP. J Biol Chem. 2006 Oct 27;281(43):32611-8. Epub 2006 Aug 10. [Article]
  2. Zhou Y, Zhang Y, Zhao D, Yu X, Shen X, Zhou Y, Wang S, Qiu Y, Chen Y, Zhu F: TTD: Therapeutic Target Database describing target druggability information. Nucleic Acids Res. 2024 Jan 5;52(D1):D1465-D1477. doi: 10.1093/nar/gkad751. [Article]
Kind
Protein
Organism
Humans
Pharmacological action
Unknown
General Function
Cellular uptake of iron occurs via receptor-mediated endocytosis of ligand-occupied transferrin receptor into specialized endosomes (PubMed:26214738). Endosomal acidification leads to iron release. The apotransferrin-receptor complex is then recycled to the cell surface with a return to neutral pH and the concomitant loss of affinity of apotransferrin for its receptor. Transferrin receptor is necessary for development of erythrocytes and the nervous system (By similarity). A second ligand, the hereditary hemochromatosis protein HFE, competes for binding with transferrin for an overlapping C-terminal binding site. Positively regulates T and B cell proliferation through iron uptake (PubMed:26642240). Acts as a lipid sensor that regulates mitochondrial fusion by regulating activation of the JNK pathway (PubMed:26214738). When dietary levels of stearate (C18:0) are low, promotes activation of the JNK pathway, resulting in HUWE1-mediated ubiquitination and subsequent degradation of the mitofusin MFN2 and inhibition of mitochondrial fusion (PubMed:26214738). When dietary levels of stearate (C18:0) are high, TFRC stearoylation inhibits activation of the JNK pathway and thus degradation of the mitofusin MFN2 (PubMed:26214738). Mediates uptake of NICOL1 into fibroblasts where it may regulate extracellular matrix production (By similarity)
Specific Function
double-stranded RNA binding
Gene Name
TFRC
Uniprot ID
P02786
Uniprot Name
Transferrin receptor protein 1
Molecular Weight
84870.665 Da
References
  1. Hemadi M, Ha-Duong NT, El Hage Chahine JM: The mechanism of iron release from the transferrin-receptor 1 adduct. J Mol Biol. 2006 May 12;358(4):1125-36. Epub 2006 Mar 13. [Article]
Kind
Protein
Organism
Humans
Pharmacological action
Unknown
General Function
Cellular oxygen sensor that catalyzes, under normoxic conditions, the post-translational formation of 4-hydroxyproline in hypoxia-inducible factor (HIF) alpha proteins. Hydroxylates a specific proline found in each of the oxygen-dependent degradation (ODD) domains (N-terminal, NODD, and C-terminal, CODD) of HIF1A. Also hydroxylates HIF2A. Has a preference for the CODD site for both HIF1A and HIF1B. Hydroxylated HIFs are then targeted for proteasomal degradation via the von Hippel-Lindau ubiquitination complex. Under hypoxic conditions, the hydroxylation reaction is attenuated allowing HIFs to escape degradation resulting in their translocation to the nucleus, heterodimerization with HIF1B, and increased expression of hypoxy-inducible genes. EGLN1 is the most important isozyme under normoxia and, through regulating the stability of HIF1, involved in various hypoxia-influenced processes such as angiogenesis in retinal and cardiac functionality. Target proteins are preferentially recognized via a LXXLAP motif
Specific Function
2-oxoglutarate-dependent dioxygenase activity
Gene Name
EGLN1
Uniprot ID
Q9GZT9
Uniprot Name
Egl nine homolog 1
Molecular Weight
46020.585 Da
References
  1. Davidson TL, Chen H, Di Toro DM, D'Angelo G, Costa M: Soluble nickel inhibits HIF-prolyl-hydroxylases creating persistent hypoxic signaling in A549 cells. Mol Carcinog. 2006 Jul;45(7):479-89. [Article]
Kind
Protein
Organism
Humans
Pharmacological action
Unknown
Actions
Cofactor
General Function
Histone deacetylase that catalyzes the deacetylation of lysine residues on the N-terminal part of the core histones (H2A, H2B, H3 and H4) (PubMed:10748112, PubMed:10922473, PubMed:10926844, PubMed:14701748, PubMed:28497810). Histone deacetylation gives a tag for epigenetic repression and plays an important role in transcriptional regulation, cell cycle progression and developmental events (PubMed:10748112, PubMed:10922473, PubMed:10926844, PubMed:14701748). Histone deacetylases act via the formation of large multiprotein complexes (PubMed:10748112, PubMed:10922473, PubMed:10926844, PubMed:14701748). Also involved in the deacetylation of cohesin complex protein SMC3 regulating release of cohesin complexes from chromatin (PubMed:22885700). May play a role in smooth muscle cell contractility (PubMed:15772115). In addition to protein deacetylase activity, also has protein-lysine deacylase activity: acts as a protein decrotonylase by mediating decrotonylation ((2E)-butenoyl) of histones (PubMed:28497810)
Specific Function
DNA-binding transcription factor binding
Gene Name
HDAC8
Uniprot ID
Q9BY41
Uniprot Name
Histone deacetylase 8
Molecular Weight
41757.29 Da
References
  1. Gantt SL, Gattis SG, Fierke CA: Catalytic activity and inhibition of human histone deacetylase 8 is dependent on the identity of the active site metal ion. Biochemistry. 2006 May 16;45(19):6170-8. [Article]
Kind
Protein
Organism
Humans
Pharmacological action
Unknown
General Function
Acts as a chaperone to prevent the harmful aggregation of alpha-hemoglobin during normal erythroid cell development. Specifically protects free alpha-hemoglobin from precipitation. It is predicted to modulate pathological states of alpha-hemoglobin excess such as beta-thalassemia
Specific Function
hemoglobin binding
Gene Name
AHSP
Uniprot ID
Q9NZD4
Uniprot Name
Alpha-hemoglobin-stabilizing protein
Molecular Weight
11840.325 Da
References
  1. Zhou S, Olson JS, Fabian M, Weiss MJ, Gow AJ: Biochemical fates of alpha hemoglobin bound to alpha hemoglobin-stabilizing protein AHSP. J Biol Chem. 2006 Oct 27;281(43):32611-8. Epub 2006 Aug 10. [Article]
Kind
Protein
Organism
Humans
Pharmacological action
Unknown
General Function
Functions as an activator of persulfide transfer to the scaffoding protein ISCU as component of the core iron-sulfur cluster (ISC) assembly complex and participates to the [2Fe-2S] cluster assembly (PubMed:12785837, PubMed:24971490). Accelerates sulfur transfer from NFS1 persulfide intermediate to ISCU and to small thiols such as L-cysteine and glutathione leading to persulfuration of these thiols and ultimately sulfide release (PubMed:24971490). Binds ferrous ion and is released from FXN upon the addition of both L-cysteine and reduced FDX2 during [2Fe-2S] cluster assembly (PubMed:29576242). The core iron-sulfur cluster (ISC) assembly complex is involved in the de novo synthesis of a [2Fe-2S] cluster, the first step of the mitochondrial iron-sulfur protein biogenesis. This process is initiated by the cysteine desulfurase complex (NFS1:LYRM4:NDUFAB1) that produces persulfide which is delivered on the scaffold protein ISCU in a FXN-dependent manner. Then this complex is stabilized by FDX2 which provides reducing equivalents to accomplish the [2Fe-2S] cluster assembly. Finally, the [2Fe-2S] cluster is transferred from ISCU to chaperone proteins, including HSCB, HSPA9 and GLRX5 (By similarity). May play a role in the protection against iron-catalyzed oxidative stress through its ability to catalyze the oxidation of Fe(2+) to Fe(3+); the oligomeric form but not the monomeric form has in vitro ferroxidase activity (PubMed:15641778). May be able to store large amounts of iron in the form of a ferrihydrite mineral by oligomerization; however, the physiological relevance is unsure as reports are conflicting and the function has only been shown using heterologous overexpression systems (PubMed:11823441, PubMed:12755598). May function as an iron chaperone protein that protects the aconitase [4Fe-4S]2+ cluster from disassembly and promotes enzyme reactivation (PubMed:15247478). May play a role as a high affinity iron binding partner for FECH that is capable of both delivering iron to ferrochelatase and mediating the terminal step in mitochondrial heme biosynthesis (PubMed:15123683, PubMed:16239244)
Specific Function
2 iron, 2 sulfur cluster binding
Gene Name
FXN
Uniprot ID
Q16595
Uniprot Name
Frataxin, mitochondrial
Molecular Weight
23134.895 Da
References
  1. Bencze KZ, Kondapalli KC, Cook JD, McMahon S, Millan-Pacheco C, Pastor N, Stemmler TL: The structure and function of frataxin. Crit Rev Biochem Mol Biol. 2006 Sep-Oct;41(5):269-91. [Article]
Kind
Protein
Organism
Humans
Pharmacological action
Unknown
General Function
Stores iron in a soluble, non-toxic, readily available form. Important for iron homeostasis. Has ferroxidase activity (PubMed:9003196). Iron is taken up in the ferrous form and deposited as ferric hydroxides after oxidation (PubMed:9003196). Also plays a role in delivery of iron to cells (By similarity). Mediates iron uptake in capsule cells of the developing kidney (By similarity). Delivery to lysosomes is mediated by the cargo receptor NCOA4 for autophagic degradation and release of iron (PubMed:24695223, PubMed:26436293)
Specific Function
ferric iron binding
Gene Name
FTH1
Uniprot ID
P02794
Uniprot Name
Ferritin heavy chain
Molecular Weight
21225.47 Da
References
  1. Toussaint L, Bertrand L, Hue L, Crichton RR, Declercq JP: High-resolution X-ray structures of human apoferritin H-chain mutants correlated with their activity and metal-binding sites. J Mol Biol. 2007 Jan 12;365(2):440-52. Epub 2006 Oct 7. [Article]
Kind
Protein
Organism
Humans
Pharmacological action
Unknown
General Function
Structure-specific nuclease with 5'-flap endonuclease and 5'-3' exonuclease activities involved in DNA replication and repair. During DNA replication, cleaves the 5'-overhanging flap structure that is generated by displacement synthesis when DNA polymerase encounters the 5'-end of a downstream Okazaki fragment. It enters the flap from the 5'-end and then tracks to cleave the flap base, leaving a nick for ligation. Also involved in the long patch base excision repair (LP-BER) pathway, by cleaving within the apurinic/apyrimidinic (AP) site-terminated flap. Acts as a genome stabilization factor that prevents flaps from equilibrating into structures that lead to duplications and deletions. Also possesses 5'-3' exonuclease activity on nicked or gapped double-stranded DNA, and exhibits RNase H activity. Also involved in replication and repair of rDNA and in repairing mitochondrial DNA
Specific Function
5'-3' exonuclease activity
Gene Name
FEN1
Uniprot ID
P39748
Uniprot Name
Flap endonuclease 1
Molecular Weight
42592.635 Da
References
  1. Hegde ML, Hegde PM, Holthauzen LM, Hazra TK, Rao KS, Mitra S: Specific Inhibition of NEIL-initiated repair of oxidized base damage in human genome by copper and iron: potential etiological linkage to neurodegenerative diseases. J Biol Chem. 2010 Sep 10;285(37):28812-25. doi: 10.1074/jbc.M110.126664. Epub 2010 Jul 9. [Article]
Kind
Protein
Organism
Humans
Pharmacological action
Unknown
General Function
Involved in base excision repair of DNA damaged by oxidation or by mutagenic agents. Acts as a DNA glycosylase that recognizes and removes damaged bases. Has a preference for oxidized pyrimidines, such as thymine glycol, formamidopyrimidine (Fapy) and 5-hydroxyuracil. Has marginal activity towards 8-oxoguanine. Has AP (apurinic/apyrimidinic) lyase activity and introduces nicks in the DNA strand. Cleaves the DNA backbone by beta-delta elimination to generate a single-strand break at the site of the removed base with both 3'- and 5'-phosphates. Has DNA glycosylase/lyase activity towards mismatched uracil and thymine, in particular in U:C and T:C mismatches. Specifically binds 5-hydroxymethylcytosine (5hmC), suggesting that it acts as a specific reader of 5hmC
Specific Function
class I DNA-(apurinic or apyrimidinic site) endonuclease activity
Gene Name
NEIL1
Uniprot ID
Q96FI4
Uniprot Name
Endonuclease 8-like 1
Molecular Weight
43683.625 Da
References
  1. Hegde ML, Hegde PM, Holthauzen LM, Hazra TK, Rao KS, Mitra S: Specific Inhibition of NEIL-initiated repair of oxidized base damage in human genome by copper and iron: potential etiological linkage to neurodegenerative diseases. J Biol Chem. 2010 Sep 10;285(37):28812-25. doi: 10.1074/jbc.M110.126664. Epub 2010 Jul 9. [Article]
Kind
Protein
Organism
Humans
Pharmacological action
Unknown
General Function
Involved in base excision repair of DNA damaged by oxidation or by mutagenic agents. Has DNA glycosylase activity towards 5-hydroxyuracil and other oxidized derivatives of cytosine with a preference for mismatched double-stranded DNA (DNA bubbles). Has low or no DNA glycosylase activity towards thymine glycol, 2-hydroxyadenine, hypoxanthine and 8-oxoguanine. Has AP (apurinic/apyrimidinic) lyase activity and introduces nicks in the DNA strand. Cleaves the DNA backbone by beta-delta elimination to generate a single-strand break at the site of the removed base with both 3'- and 5'-phosphates
Specific Function
class I DNA-(apurinic or apyrimidinic site) endonuclease activity
Gene Name
NEIL2
Uniprot ID
Q969S2
Uniprot Name
Endonuclease 8-like 2
Molecular Weight
36826.285 Da
References
  1. Hegde ML, Hegde PM, Holthauzen LM, Hazra TK, Rao KS, Mitra S: Specific Inhibition of NEIL-initiated repair of oxidized base damage in human genome by copper and iron: potential etiological linkage to neurodegenerative diseases. J Biol Chem. 2010 Sep 10;285(37):28812-25. doi: 10.1074/jbc.M110.126664. Epub 2010 Jul 9. [Article]
Kind
Protein
Organism
Humans
Pharmacological action
Unknown
General Function
Repair polymerase that plays a key role in base-excision repair (PubMed:10556592, PubMed:9207062, PubMed:9572863). During this process, the damaged base is excised by specific DNA glycosylases, the DNA backbone is nicked at the abasic site by an apurinic/apyrimidic (AP) endonuclease, and POLB removes 5'-deoxyribose-phosphate from the preincised AP site acting as a 5'-deoxyribose-phosphate lyase (5'-dRP lyase); through its DNA polymerase activity, it adds one nucleotide to the 3' end of the arising single-nucleotide gap (PubMed:10556592, PubMed:17526740, PubMed:9556598, PubMed:9572863, PubMed:9614142). Conducts 'gap-filling' DNA synthesis in a stepwise distributive fashion rather than in a processive fashion as for other DNA polymerases. It is also able to cleave sugar-phosphate bonds 3' to an intact AP site, acting as an AP lyase (PubMed:9614142)
Specific Function
5'-deoxyribose-5-phosphate lyase activity
Gene Name
POLB
Uniprot ID
P06746
Uniprot Name
DNA polymerase beta
Molecular Weight
38177.34 Da
References
  1. Hegde ML, Hegde PM, Holthauzen LM, Hazra TK, Rao KS, Mitra S: Specific Inhibition of NEIL-initiated repair of oxidized base damage in human genome by copper and iron: potential etiological linkage to neurodegenerative diseases. J Biol Chem. 2010 Sep 10;285(37):28812-25. doi: 10.1074/jbc.M110.126664. Epub 2010 Jul 9. [Article]
Kind
Protein
Organism
Humans
Pharmacological action
Unknown
General Function
Multifunctional blue, copper-binding (6-7 atoms per molecule) glycoprotein. It has ferroxidase activity oxidizing Fe(2+) to Fe(3+) without releasing radical oxygen species. It is involved in iron transport across the cell membrane (PubMed:16150804). Copper ions provide a large number of enzymatic activites. Oxidizes highly toxic ferrous ions to the ferric state for further incorporation onto apo-transferrins, catalyzes Cu(+) oxidation and promotes the oxidation of biogenic amines such as norepinephrin and serotonin (PubMed:14623105, PubMed:4643313, PubMed:5912351). Provides Cu(2+) ions for the ascorbate-mediated deaminase degradation of the heparan sulfate chains of GPC1 (By similarity). Has glutathione peroxidase-like activity, can remove both hydrogen peroxide and lipid hydroperoxide in the presence of thiols (PubMed:10481051). Also shows NO-oxidase and NO2 synthase activities that determine endocrine NO homeostasis (PubMed:16906150)
Specific Function
copper ion binding
Gene Name
CP
Uniprot ID
P00450
Uniprot Name
Ceruloplasmin
Molecular Weight
122218.48 Da
References
  1. Ha-Duong NT, Eid C, Hemadi M, El Hage Chahine JM: In vitro interaction between ceruloplasmin and human serum transferrin. Biochemistry. 2010 Dec 7;49(48):10261-3. doi: 10.1021/bi1014503. Epub 2010 Nov 9. [Article]
Kind
Protein
Organism
Humans
Pharmacological action
Unknown
General Function
Transferrins are iron binding transport proteins which can bind two Fe(3+) ions in association with the binding of an anion, usually bicarbonate. It is responsible for the transport of iron from sites of absorption and heme degradation to those of storage and utilization. Serum transferrin may also have a further role in stimulating cell proliferation
Specific Function
enzyme binding
Gene Name
TF
Uniprot ID
P02787
Uniprot Name
Serotransferrin
Molecular Weight
77049.175 Da
References
  1. Ha-Duong NT, Eid C, Hemadi M, El Hage Chahine JM: In vitro interaction between ceruloplasmin and human serum transferrin. Biochemistry. 2010 Dec 7;49(48):10261-3. doi: 10.1021/bi1014503. Epub 2010 Nov 9. [Article]

Drug created at August 29, 2007 16:01 / Updated at October 21, 2024 08:50