Indication Type	Indication	Combined Product Details	Approval Level	Patient Characteristics
Used in combination to prevent	Folic acid deficiency	Combination Product in combination with: Folic acid (DB00158)	••• •••	••••••••••••• •••••••••
Used in combination to prevent	Iron deficiency	Combination Product in combination with: Folic acid (DB00158)	••• •••	••••••••••••• •••••••••
Treatment of	Iron deficiency anemia		••••••••••••
Prevention of	Iron deficiency anemia		••••••••••••

Associated Therapies

Oral Contraceptives

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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.

Target	Actions	Organism
UTransferrin receptor protein 1	Not Available	Humans
UEgl nine homolog 1	Not Available	Humans
UHistone deacetylase 8	Not Available	Humans
UAlpha-hemoglobin-stabilizing protein	Not Available	Humans
UHemoglobin subunit alpha	Not Available	Humans
UFrataxin, mitochondrial	Not Available	Humans
UFerritin heavy chain	Not Available	Humans
UFlap endonuclease 1	Not Available	Humans
UEndonuclease 8-like 1	Not Available	Humans
UEndonuclease 8-like 2	Not Available	Humans
UDNA polymerase beta	Not Available	Humans
UCeruloplasmin	Not Available	Humans
USerotransferrin	Not Available	Humans

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

Not Available

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.

Drug	Interaction
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Alendronic acid	Ferrous fumarate can cause a decrease in the absorption of Alendronic acid resulting in a reduced serum concentration and potentially a decrease in efficacy.
Almasilate	Almasilate can cause a decrease in the absorption of Ferrous fumarate resulting in a reduced serum concentration and potentially a decrease in efficacy.
Aluminium phosphate	Aluminium phosphate can cause a decrease in the absorption of Ferrous fumarate resulting in a reduced serum concentration and potentially a decrease in efficacy.
Aluminum hydroxide	Aluminum hydroxide can cause a decrease in the absorption of Ferrous fumarate resulting in a reduced serum concentration and potentially a decrease in efficacy.
Asenapine	Asenapine can cause a decrease in the absorption of Ferrous fumarate resulting in a reduced serum concentration and potentially a decrease in efficacy.

Food Interactions

Avoid milk and dairy products. Take ferrous fumarate at least 2 hours before or after milk.
Limit caffeine intake. Food and beverages containing caffeine may reduce iron absorption.
Take at least 2 hours before or after calcium supplements.
Take separate from antacids. Take ferrous fumarate at least 2 hours before or after antacids.
Take with food. This reduces gastric irritation.
Take with foods containing vitamin C. Foods rich in vitamin C increase the absorption of iron.

Products

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Active Moieties

Name	Kind	UNII	CAS	InChI Key
Iron	unknown	E1UOL152H7	7439-89-6	XEEYBQQBJWHFJM-UHFFFAOYSA-N
Ferrous cation	ionic	GW89581OWR	15438-31-0	CWYNVVGOOAEACU-UHFFFAOYSA-N

Product Images

Over the Counter Products

Name	Dosage	Strength	Route	Labeller	Marketing Start	Marketing End
DYNA FERROUS FUMARATE TABLET	Tablet	200 mg	Oral	DYNAPHARM (M) SDN. BHD.	2020-09-08	Not applicable
FEFUR TABLET (FILM-COATED) 100MG	Tablet, film coated		Oral	Hovid Berhad	2020-09-08	Not applicable
Ferion Tab	Tablet	65 mg / tab	Oral	Pharmetics (2011) Inc.	1981-12-31	2000-08-21
Ferrocite	Tablet, film coated	106 mg/1	Oral	Breckenridge Pharmaceutical, Inc.	2003-07-01	2011-12-31
FERROMAX TABLET 200MG	Tablet	200 MG	Oral	ZONTRON PHARMACEUTICALS SDN. BHD.	2020-09-08	Not applicable

Mixture Products

Name	Ingredients	Dosage	Route	Labeller	Marketing Start	Marketing End
24 Multivitamins + Minerals	Ferrous fumarate (15 mg) + Ascorbic acid (150 mg) + Beta carotene (10000 unit) + Biotin (25 mcg) + Calcium (130 mg) + Cholecalciferol (400 unit) + Choline bitartrate (25 mg) + Chromium (20 mcg) + Copper (1 mg) + Cyanocobalamin (25 mcg) + Folic acid (.8 mg) + Inositol (25 mg) + Magnesium (65 mg) + Manganese cation (2 mg) + Molybdenum (20 mcg) + Niacin (25 mg) + Calcium pantothenate (25 mg) + Potassium (15 mg) + Potassium Iodide (.1 mg) + Pyridoxine hydrochloride (25 mg) + Racemethionine (25 mg) + Riboflavin (25 mg) + Selenium (20 mcg) + Thiamine hydrochloride (25 mg) + Vanadium (20 mcg) + Vitamin A palmitate (5000 unit) + Vitamin E (50 unit) + Zinc (10 mg)	Tablet	Oral	Stanley Pharmaceuticals, A Division Of Vita Health Products Inc.	1997-04-30	2002-07-31
ANDALAN FE	Ferrous fumarate (75 mg) + Ethinylestradiol (0.03 mg) + Levonorgestrel (0.15 mg)	Tablet, sugar coated	Oral	Harsen	2018-07-30	2025-07-19
Appedrine	Ferrous fumarate (3.33 mg) + Benzocaine (3 mg) + Nicotinamide (3.33 mg) + Riboflavin (.4 mg) + Sodium ascorbate (10 mg) + Thiamine hydrochloride (.33 mg) + Vitamin A acetate (1333 unit) + Vitamin D (133 unit)	Tablet	Oral	Chattem, Inc.	1975-12-31	2004-07-08
Appeton Essentials Teengrow	Ferrous fumarate (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 hydrochloride (4 mg) + Riboflavin (3 mg) + Thiamine (3 mg) + Vitamin A (2500 IU) + Vitamin E (15 Iu) + Zinc (25 mg)	Tablet	Oral	KOTRA PHARMA (M) SDN. BHD.	2020-09-08	Not applicable
Aurovela 24 Fe	Ferrous fumarate (75 mg/1) + Ethinylestradiol (20 ug/1) + Norethisterone acetate (1 mg/1)	Kit; Tablet	Oral	Aurobindo Pharma Limited	2017-06-15	Not applicable

Unapproved/Other Products

Name	Ingredients	Dosage	Route	Labeller	Marketing Start	Marketing End
Bacmin	Ferrous fumarate (27 mg/1) + Ascorbic acid (500 mg/1) + Biotin (150 ug/1) + Chromium Cr-51 chloride (0.1 mg/1) + Cupric oxide (3 mg/1) + Cyanocobalamin (50 ug/1) + Flavone (50 mg/1) + Folic acid (1 mg/1) + Magnesium oxide (50 mg/1) + Manganese gluconate (5 mg/1) + Nicotinamide (100 mg/1) + Calcium pantothenate (25 mg/1) + Pyridoxine hydrochloride (25 mg/1) + Riboflavin (20 mg/1) + Selenomethionine (50 ug/1) + Thiamine mononitrate (20 mg/1) + Vitamin A acetate (2000 [iU]/1) + Zinc oxide (22.5 mg/1) + alpha-Tocopherol acetate (30 [iU]/1)	Tablet, coated	Oral	Marnel Pharmaceuticals, Llc	2000-04-01	Not applicable
C-Nate DHA	Ferrous fumarate (28 mg/1) + Ascorbic acid (100 mg/1) + Cholecalciferol (400 [iU]/1) + Cupric sulfate pentahydrate (1 mg/1) + Cyanocobalamin (15 ug/1) + Folic acid (1 mg/1) + Magnesium (30 mg/1) + Omega-3 fatty acids (200 mg/1) + Pyridoxine hydrochloride (20 mg/1) + Riboflavin (3 mg/1) + Thiamine mononitrate (3 mg/1) + Vitamin E (30 [iU]/1) + Zinc oxide (20 mg/1)	Capsule, gelatin coated	Oral	Centurion Labs, LLC	2013-01-01	Not applicable
Cavan Folate DHA	Ferrous fumarate (65 mg/1) + Ferrous fumarate (65 mg/1) + Ascorbic acid (70 mg/1) + Ascorbic acid (70 mg/1) + Beta carotene (2700 [iU]/1) + Beta carotene (2700 [iU]/1) + Calcium carbonate (100 mg/1) + Calcium carbonate (100 mg/1) + Cholecalciferol (400 [iU]/1) + Cholecalciferol (400 [iU]/1) + Cupric oxide (2 mg/1) + Cupric oxide (2 mg/1) + Cyanocobalamin (12 ug/1) + Cyanocobalamin (12 ug/1) + DL-alpha tocopheryl acetate (30 [iU]/1) + DL-alpha tocopheryl acetate (30 [iU]/1) + Doconexent (250 mg/1) + Doconexent (250 mg/1) + Folic acid (1 mg/1) + Folic acid (1 mg/1) + Magnesium oxide (25 mg/1) + Magnesium oxide (25 mg/1) + Nicotinamide (18 mg/1) + Nicotinamide (18 mg/1) + Pyridoxine hydrochloride (2.5 mg/1) + Pyridoxine hydrochloride (2.5 mg/1) + Riboflavin (1.8 mg/1) + Riboflavin (1.8 mg/1) + Thiamine mononitrate (1.6 mg/1) + Thiamine mononitrate (1.6 mg/1) + Zinc oxide (25 mg/1) + Zinc oxide (25 mg/1)	Kit	Oral	Seton Pharmaceuticals	2010-06-04	2012-03-31
Cavan Folate DHA	Ferrous fumarate (65 mg/1) + Ferrous fumarate (65 mg/1) + Ascorbic acid (70 mg/1) + Ascorbic acid (70 mg/1) + Beta carotene (2700 [iU]/1) + Beta carotene (2700 [iU]/1) + Calcium carbonate (100 mg/1) + Calcium carbonate (100 mg/1) + Cholecalciferol (400 [iU]/1) + Cholecalciferol (400 [iU]/1) + Cupric oxide (2 mg/1) + Cupric oxide (2 mg/1) + Cyanocobalamin (12 ug/1) + Cyanocobalamin (12 ug/1) + DL-alpha tocopheryl acetate (30 [iU]/1) + DL-alpha tocopheryl acetate (30 [iU]/1) + Doconexent (250 mg/1) + Doconexent (250 mg/1) + Folic acid (1 mg/1) + Folic acid (1 mg/1) + Magnesium oxide (25 mg/1) + Magnesium oxide (25 mg/1) + Nicotinamide (18 mg/1) + Nicotinamide (18 mg/1) + Pyridoxine hydrochloride (2.5 mg/1) + Pyridoxine hydrochloride (2.5 mg/1) + Riboflavin (1.8 mg/1) + Riboflavin (1.8 mg/1) + Thiamine mononitrate (1.6 mg/1) + Thiamine mononitrate (1.6 mg/1) + Zinc oxide (25 mg/1) + Zinc oxide (25 mg/1)	Kit	Oral	Seton Pharmaceuticals	2010-06-04	2012-03-31
Cavan Folate OB	Ferrous fumarate (65 mg/1) + Ascorbic acid (70 mg/1) + Beta carotene (2700 [iU]/1) + Calcium carbonate (100 mg/1) + Cholecalciferol (400 [iU]/1) + Cupric oxide (2 mg/1) + Cyanocobalamin (12 ug/1) + DL-alpha tocopheryl acetate (30 [iU]/1) + Folic acid (1 mg/1) + Magnesium oxide (25 mg/1) + Nicotinamide (18 mg/1) + Pyridoxine hydrochloride (2.5 mg/1) + Riboflavin (1.8 mg/1) + Thiamine mononitrate (1.6 mg/1) + Zinc oxide (25 mg/1)	Tablet	Oral	Seton Pharmaceuticals	2010-08-23	2012-05-31

Chemical Identifiers

UNII: R5L488RY0Q
CAS number: 141-01-5
InChI Key: PMVSDNDAUGGCCE-TYYBGVCCSA-L
InChI: InChI=1S/C4H4O4.Fe/c5-3(6)1-2-4(7)8;/h1-2H,(H,5,6)(H,7,8);/q;+2/p-2/b2-1+;
IUPAC Name: lambda2-iron(2+) (2E)-but-2-enedioate
SMILES: [Fe++].[H]\C(=C(\[H])C([O-])=O)C([O-])=O

References

General References

Not Available

External Links

PubChem Compound: 6433164
ChemSpider: 10607713
ChEBI: 31607
ChEMBL: CHEMBL1200640
Wikipedia: Iron(II)_fumarate

Clinical Trials

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Phase	Status	Purpose	Conditions	Count	Start Date	Why Stopped	100+ additional columns
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Not Available	Recruiting	Treatment	Inflammatory Bowel Diseases (IBD)	1	somestatus	stop reason	just information to hide
Not Available	Unknown Status	Prevention	Female Infertility / Pelvic Inflammatory Disease (PID)	1	somestatus	stop reason	just information to hide
4	Recruiting	Diagnostic	Inflammatory Bowel Diseases (IBD) / Iron Deficiency (ID) / Iron Deficiency Anemia (IDA)	1	somestatus	stop reason	just information to hide
4	Unknown Status	Treatment	Iron Deficiency Anemia (IDA) / Pregnancy Related	1	somestatus	stop reason	just information to hide
3	Completed	Prevention	Anemia / Iron Deficiency (ID)	1	somestatus	stop reason	just information to hide

Pharmacoeconomics

Manufacturers

Not Available

Packagers

Not Available

Dosage Forms

Form	Route	Strength
Tablet, sugar coated	Oral	0.15 mg
Bar, chewable	Oral
Tablet, coated	Oral
Capsule	Cutaneous; Oral
Tablet	Oral
Tablet, film coated	Oral
Capsule	Oral
Tablet	Oral	65 mg / tab
Tablet, film coated	Oral	325 mg/1
Kit	Oral
Tablet, film coated	Oral	106 mg/1
Capsule, liquid filled	Oral
Tablet	Oral	300 mg / tab
Tablet	Oral	200 mg / tab
Capsule	Oral	162 mg
Syrup	Oral
Capsule, gelatin coated; kit; tablet	Oral
Kit; tablet	Oral
Tablet	Oral	106 mg/1
Tablet	Oral	30 mg / tab
Tablet	Oral	18 mg / tab
Capsule, coated	Oral
Tablet	Oral	6 mg
Tablet	Oral
Tablet, film coated	Oral	200 mg
Capsule, delayed release	Oral
Tablet, film coated	Oral
Capsule; kit; tablet	Oral
Capsule, liquid filled; kit; tablet	Oral
Capsule, gelatin coated	Oral
Capsule	Oral	100 mg
Liquid	Oral
Tablet, extended release	Oral
Tablet, film coated	Oral	180 mg
Tablet, sugar coated	Oral
Tablet, sugar coated	Oral	60 mg
Tablet, film coated	Oral	60 mg
Capsule	Oral
Tablet, sugar coated	Oral
Powder, for solution	Oral
Tablet	Oral	28 mg / tab
Tablet, chewable	Oral
Suspension	Oral
Powder	Oral
Tablet	Oral	60 mg
Tablet
Tablet, extended release	Oral	18 mg
Tablet, sugar coated	Oral	200 mg
Tablet	Oral	200 mg
Tablet, coated	Oral	200 mg
Suspension	Oral	76 mg/5mL
Solution / drops	Oral	375 mg/5ml
Tablet, film coated

Prices

Not Available

Patents

Patent Number	Pediatric Extension	Approved	Expires (estimated)	Region
US6667050	No	2003-12-23	2019-04-06

Properties

State

Not Available

Experimental Properties

Not Available

Predicted Properties

Property	Value	Source
Water Solubility	13.1 mg/mL	ALOGPS
logP	0.83	ALOGPS
logP	-0.041	Chemaxon
logS	-1.2	ALOGPS
pKa (Strongest Acidic)	3.35	Chemaxon
Physiological Charge	-2	Chemaxon
Hydrogen Acceptor Count	4	Chemaxon
Hydrogen Donor Count	0	Chemaxon
Polar Surface Area	80.26 Å²	Chemaxon
Rotatable Bond Count	2	Chemaxon
Refractivity	46.28 m³·mol^-1	Chemaxon
Polarizability	8.65 Å³	Chemaxon
Number of Rings	0	Chemaxon
Bioavailability	1	Chemaxon
Rule of Five	Yes	Chemaxon
Ghose Filter	No	Chemaxon
Veber's Rule	No	Chemaxon
MDDR-like Rule	No	Chemaxon

Predicted ADMET Features

Not Available

Spectra

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

Targets

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Details1. Transferrin receptor protein 1

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)
Specific Function: Double-stranded rna binding
Gene Name: TFRC
Uniprot ID: P02786
Uniprot Name: Transferrin receptor protein 1
Molecular Weight: 84870.665 Da

References

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]

Details2. Egl nine homolog 1

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

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]

Details3. Histone deacetylase 8

Kind: Protein
Organism: Humans
Pharmacological action: Unknown

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

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]

Details4. Alpha-hemoglobin-stabilizing protein

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

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]

Details5. Hemoglobin subunit alpha

Kind: Protein
Organism: Humans
Pharmacological action: Unknown

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

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]

Details6. Frataxin, mitochondrial

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

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]

Details7. Ferritin heavy chain

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

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]

Details8. Flap endonuclease 1

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

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]

Details9. Endonuclease 8-like 1

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

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]

Details10. Endonuclease 8-like 2

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

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]

Details11. DNA polymerase beta

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

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]

Details12. Ceruloplasmin

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

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]

Details13. Serotransferrin

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: Ferric iron binding
Gene Name: TF
Uniprot ID: P02787
Uniprot Name: Serotransferrin
Molecular Weight: 77049.175 Da

References

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 July 09, 2018 17:49 / Updated at September 20, 2024 01:25

Ferrous fumarate

Identification

Structure for Ferrous fumarate (DB14491)

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Clinical Trials

Clinical Trial & Rare Diseases Add-on Data Package

Pharmacoeconomics

Properties

Spectra

Collision Cross Sections (CCS)

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