Ferrous succinate

Identification

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Name
Ferrous succinate
Accession Number
DB14489  (DBSALT000083)
Type
Small Molecule
Groups
Approved
Description
Not Available
Structure
Thumb
Synonyms
  • Iron succinate
Categories
UNII
818ZYK7N91
CAS number
10030-90-7
Weight
Average: 171.917
Monoisotopic: 171.945895
Chemical Formula
C4H4FeO4
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

Pharmacology

Indication

Used in preventing and treating iron-deficiency anemia.

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
UTransferrin receptor protein 1Not AvailableHumans
UEgl nine homolog 1Not AvailableHumans
UHistone deacetylase 8Not AvailableHumans
UAlpha-hemoglobin-stabilizing proteinNot AvailableHumans
UHemoglobin subunit alphaNot 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
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.

Affected organisms
Not Available
Pathways
Not Available
Pharmacogenomic Effects/ADRs
Not Available

Interactions

Drug Interactions
DrugInteraction
3-Aza-2,3-Dihydrogeranyl DiphosphateFerrous succinate can cause a decrease in the absorption of 3-Aza-2,3-Dihydrogeranyl Diphosphate resulting in a reduced serum concentration and potentially a decrease in efficacy.
Alendronic acidFerrous succinate can cause a decrease in the absorption of Alendronic acid resulting in a reduced serum concentration and potentially a decrease in efficacy.
AlmasilateAlmasilate can cause a decrease in the absorption of Ferrous succinate resulting in a reduced serum concentration and potentially a decrease in efficacy.
AloglutamolAloglutamol can cause a decrease in the absorption of Ferrous succinate resulting in a reduced serum concentration and potentially a decrease in efficacy.
AluminiumAluminium can cause a decrease in the absorption of Ferrous succinate resulting in a reduced serum concentration and potentially a decrease in efficacy.
Aluminium acetoacetateAluminium acetoacetate can cause a decrease in the absorption of Ferrous succinate resulting in a reduced serum concentration and potentially a decrease in efficacy.
Aluminium glycinateAluminium glycinate can cause a decrease in the absorption of Ferrous succinate resulting in a reduced serum concentration and potentially a decrease in efficacy.
Aluminium phosphateAluminium phosphate can cause a decrease in the absorption of Ferrous succinate resulting in a reduced serum concentration and potentially a decrease in efficacy.
Aluminum hydroxideAluminum hydroxide can cause a decrease in the absorption of Ferrous succinate resulting in a reduced serum concentration and potentially a decrease in efficacy.
AsenapineAsenapine can cause a decrease in the absorption of Ferrous succinate resulting in a reduced serum concentration and potentially a decrease in efficacy.
Additional Data Available
  • Extended Description
    Extended Description

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  • Severity
    Severity

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  • Evidence Level
    Evidence Level

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  • Action
    Action

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Food Interactions
Not Available

References

General References
Not Available
External Links
PubChem Compound
159252
ChemSpider
8640173
Wikipedia
Iron_supplement
ATC Codes
B03AA06 — Ferrous succinate

Clinical Trials

Clinical Trials
PhaseStatusPurposeConditionsCount
2Not Yet RecruitingTreatmentCerebral Infarctions / Dementia, Vascular / Iron-Deficiency / Transient Ischaemic Attack (TIA) / Vascular Cognitive Impairment1

Pharmacoeconomics

Manufacturers
Not Available
Packagers
Not Available
Dosage forms
Not Available
Prices
Not Available
Patents
Not Available

Properties

State
Not Available
Experimental Properties
Not Available
Predicted Properties
PropertyValueSource
Water Solubility31.8 mg/mLALOGPS
logP0.53ALOGPS
logP-0.4ChemAxon
logS-0.85ALOGPS
pKa (Strongest Acidic)3.55ChemAxon
Physiological Charge-2ChemAxon
Hydrogen Acceptor Count4ChemAxon
Hydrogen Donor Count0ChemAxon
Polar Surface Area80.26 Å2ChemAxon
Rotatable Bond Count3ChemAxon
Refractivity45.21 m3·mol-1ChemAxon
Polarizability9.33 Å3ChemAxon
Number of Rings0ChemAxon
Bioavailability1ChemAxon
Rule of FiveYesChemAxon
Ghose FilterNoChemAxon
Veber's RuleNoChemAxon
MDDR-like RuleNoChemAxon
Predicted ADMET features
Not Available

Spectra

Mass Spec (NIST)
Not Available
Spectra
Not Available

Taxonomy

Classification
Not classified

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
  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. [PubMed:16564538]
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
  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. [PubMed:16649251]
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
  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. [PubMed:16681389]
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. [PubMed:16901899]
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
  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. [PubMed:16901899]
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
  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. [PubMed:16911956]
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
  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. [PubMed:17070541]
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
  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. [PubMed:20622253]
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
  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. [PubMed:20622253]
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
  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. [PubMed:20622253]
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
  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. [PubMed:20622253]
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
  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. [PubMed:21049900]
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
  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. [PubMed:21049900]

Drug created on July 09, 2018 11:43 / Updated on May 01, 2019 11:59