Ferrous succinate
Identification
- Summary
Ferrous succinate is an iron supplement indicated in the treatment of iron deficiency anemia.
- Generic Name
- Ferrous succinate
- DrugBank Accession Number
- DB14489
- Background
Not Available
- Type
- Small Molecule
- Groups
- Approved
- Structure
- Weight
- Average: 171.917
Monoisotopic: 171.945895 - Chemical Formula
- C4H4FeO4
- Synonyms
- Iron succinate
Pharmacology
- Indication
Used in preventing and treating iron-deficiency anemia.
Reduce drug development failure ratesBuild, train, & validate machine-learning modelswith evidence-based and structured datasets.Build, train, & validate predictive machine-learning models with structured datasets.- Associated Conditions
Indication Type Indication Combined Product Details Approval Level Age Group Patient Characteristics Dose Form Treatment of Iron deficiency ••• ••• •••••• - Contraindications & Blackbox Warnings
- Prevent Adverse Drug Events TodayTap into our Clinical API for life-saving information on contraindications & blackbox warnings, population restrictions, harmful risks, & more.Avoid life-threatening adverse drug events with our Clinical API
- 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
- Improve decision support & research outcomesWith structured adverse effects data, including: blackbox warnings, adverse reactions, warning & precautions, & incidence rates. View sample adverse effects data in our new Data Library!Improve decision support & research outcomes with our structured adverse effects data.
- 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 Integrate drug-drug
interactions in your softwareAlendronic acid Ferrous succinate 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 succinate 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 succinate 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 succinate resulting in a reduced serum concentration and potentially a decrease in efficacy. Asenapine Asenapine can cause a decrease in the absorption of Ferrous succinate resulting in a reduced serum concentration and potentially a decrease in efficacy. - Food Interactions
- Not Available
Products
- Drug product information from 10+ global regionsOur datasets provide approved product information including:dosage, form, labeller, route of administration, and marketing period.Access drug product information from over 10 global regions.
Categories
- ATC Codes
- B03AA06 — Ferrous succinate
- Drug Categories
- Classification
- Not classified
- Affected organisms
- Not Available
Chemical Identifiers
- UNII
- 818ZYK7N91
- CAS number
- 10030-90-7
- InChI Key
- MDXRFOWKIZPNTA-UHFFFAOYSA-L
- InChI
- InChI=1S/C4H6O4.Fe/c5-3(6)1-2-4(7)8;/h1-2H2,(H,5,6)(H,7,8);/q;+2/p-2
- IUPAC Name
- lambda2-iron(2+) butanedioate
- SMILES
- [Fe++].[O-]C(=O)CCC([O-])=O
References
- General References
- DIMDI Product Information: FERRLECIT 2 (iron succinate) tablet [Link]
- External Links
- PubChem Compound
- 159252
- ChemSpider
- 8640173
- Wikipedia
- Iron_supplement
Clinical Trials
- Clinical Trials
Phase Status Purpose Conditions Count 4 Completed Treatment Iron Deficiency Anemia (IDA) 1 4 Not Yet Recruiting Prevention Iron Deficiency Anemia (IDA) 1 4 Not Yet Recruiting Treatment Postpartum Anemia 1 4 Recruiting Treatment Adults / Perioperative Anemia / Spinal Deformities / Surgery 1 4 Unknown Status Treatment Anemia / Hematopoietic Stem Cell Transplantation (SCT) / Lymphoma 1
Pharmacoeconomics
- Manufacturers
- Not Available
- Packagers
- Not Available
- Dosage Forms
Form Route Strength Tablet 280 mg - Prices
- Not Available
- Patents
- Not Available
Properties
- State
- Not Available
- Experimental Properties
- Not Available
- Predicted Properties
Property Value Source Water Solubility 31.8 mg/mL ALOGPS logP 0.53 ALOGPS logP -0.4 Chemaxon logS -0.85 ALOGPS pKa (Strongest Acidic) 3.55 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 3 Chemaxon Refractivity 45.21 m3·mol-1 Chemaxon Polarizability 9.33 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
- Kind
- Protein
- Organism
- Humans
- Pharmacological action
- Unknown
- General Function
- Virus receptor activity
- Specific Function
- Cellular uptake of iron occurs via receptor-mediated endocytosis of ligand-occupied transferrin receptor into specialized endosomes. Endosomal acidification leads to iron release. The apotransferri...
- 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]
- Kind
- Protein
- Organism
- Humans
- Pharmacological action
- Unknown
- General Function
- Peptidyl-proline dioxygenase activity
- Specific 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 prol...
- 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]
- Kind
- Protein
- Organism
- Humans
- Pharmacological action
- Unknown
- General Function
- Transcription factor binding
- Specific Function
- Responsible for the deacetylation of lysine residues on the N-terminal part of the core histones (H2A, H2B, H3 and H4). Histone deacetylation gives a tag for epigenetic repression and plays an impo...
- 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]
- 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]
- Kind
- Protein
- Organism
- Humans
- Pharmacological action
- Unknown
- General Function
- Oxygen transporter activity
- Specific Function
- Involved in oxygen transport from the lung to the various peripheral tissues.
- 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]
- Kind
- Protein
- Organism
- Humans
- Pharmacological action
- Unknown
- General Function
- Promotes the biosynthesis of heme and assembly and repair of iron-sulfur clusters by delivering Fe(2+) to proteins involved in these pathways. 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. 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. Modulates the RNA-binding activity of ACO1.
- 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]
- Kind
- Protein
- Organism
- Humans
- Pharmacological action
- Unknown
- General Function
- Iron ion binding
- Specific Function
- Stores iron in a soluble, non-toxic, readily available form. Important for iron homeostasis. Has ferroxidase activity. Iron is taken up in the ferrous form and deposited as ferric hydroxides after ...
- 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]
- 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 structurs 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]
- Kind
- Protein
- Organism
- Humans
- Pharmacological action
- Unknown
- General Function
- Not Available
- Specific Function
- Not Available
- 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]
- Kind
- Protein
- Organism
- Humans
- Pharmacological action
- Unknown
- General Function
- Zinc ion binding
- Specific 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 preferenc...
- 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]
- Kind
- Protein
- Organism
- Humans
- Pharmacological action
- Unknown
- General Function
- Microtubule binding
- Specific Function
- Repair polymerase that plays a key role in base-excision repair. Has 5'-deoxyribose-5-phosphate lyase (dRP lyase) activity that removes the 5' sugar phosphate and also acts as a DNA polymerase that...
- 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]
- Kind
- Protein
- Organism
- Humans
- Pharmacological action
- Unknown
- General Function
- Ferroxidase activity
- Specific Function
- Ceruloplasmin is a 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 iro...
- Gene Name
- CP
- Uniprot ID
- P00450
- Uniprot Name
- Ceruloplasmin
- Molecular Weight
- 122204.45 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]
- Kind
- Protein
- Organism
- Humans
- Pharmacological action
- Unknown
- General Function
- Transferrin receptor binding
- Specific 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 si...
- Gene Name
- TF
- Uniprot ID
- P02787
- Uniprot Name
- Serotransferrin
- Molecular Weight
- 77063.195 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 17:43 / Updated at May 14, 2021 01:06