| Version |
2.5 |
| Creation Date |
2007-07-06 20:30:59 |
| Update Date |
2008-08-26 21:07:37 |
| Primary Accession Number |
DB01378 |
| Secondary Accession Number |
Not Available |
| Name |
Magnesium |
| Drug Type |
- Experimental
- Small Molecule
|
| Description |
Magnesium hydroxide is used primarily in "Milk of Magnesia", a white aqueous, mildly alkaline suspension of magnesium hydroxide formulated at about 8%w/v. Milk of magnesia is primarily used to alleviate constipation, but can also be used to relieve indigestion and heartburn. When taken internally by mouth as a laxative, the osmotic force of the magnesia suspension acts to draw fluids from the body and to retain those already within the lumen of the intestine, serving to distend the bowel, thus stimulating nerves within the colon wall, inducing peristalsis and resulting in evacuation of colonic contents. |
| Synonyms |
Not Available |
| Brand Names |
Not Available |
| Brand Mixtures |
Not Available |
| Chemical IUPAC Name |
magnesium(+2) cation |
| Chemical Formula |
Mg |
| Chemical Structure |
 |
| CAS Registry Number |
7439-95-4 |
| InChI Identifier |
InChI=1/Mg/q+2 |
| InChI Key |
JLVVSXFLKOJNIY-UHFFFAOYAC |
| KEGG Drug |
Not Available |
| KEGG Compound |
C00305  |
| PubChem Compound |
888  |
| PubChem Substance |
22394505  |
| ChEBI ID |
25107  |
| PharmGKB ID |
PA450287  |
| HET ID |
Not Available |
| GenBank ID |
Not Available |
| Drug ID Number [DIN] |
00013838  |
| RxList Link |
Not Available |
| PDRhealth Link |
Not Available |
| Wikipedia Link |
http://en.wikipedia.org/wiki/Magnesium  |
| FDA Label |
Not Available |
| Material Safety Data Sheet (MSDS) |
|
| Synthesis Reference |
Not Available |
| Average Molecular Weight |
24.3050 |
| Monoisotopic Molecular Weight |
23.9850 |
| State |
Solid |
| Melting Point |
651 oC |
| Experimental Water Solubility |
Not Available
Source: PhysProp
|
| Predicted Water Solubility |
Not Available
Calculated using ALOGPS
|
| Experimental LogP/Hydrophobicity |
Not Available
Source: PhysProp
|
| Predicted LogP |
Not Available
Calculated using ALOGPS
|
| Experimental LogS |
Not Available |
| Predicted LogS |
Not Available
Calculated using ALOGPS
|
| Experimental Caco2 Permeability |
Not Available |
| pKa/Isoelectric Point |
Not Available |
| Mass Spectrum |
Not Available
|
| MOL File |
Show | Download  |
| SDF File |
Show | Download  |
| PDB File |
Show | Download  |
| 2D Structure |
|
| 3D Structure |
|
| Experimental PDB ID |
Not Available |
| Isomeric SMILES |
[Mg++] |
| Canonical SMILES |
[Mg++] |
| Drug Category |
Not Available |
| ATC Codes |
|
| AHFS Codes |
- 28:08.04.24
- 28:12.92
- 40:12.00
- 40:34.00*
- 56:04.00
- 56:12.00
- 84:24.00
- 84:92.00
- 88:29.00*
- 92:02.00*
|
| Indication |
Not Available |
| Pharmacology |
Not Available |
| Mechanism of Action |
Not Available |
| Absorption |
Not Available |
| Toxicity |
Not Available |
| Protein Binding |
Not Available |
| Biotransformation |
Not Available |
| Half Life |
Not Available |
| Dosage Forms |
| Form |
Route |
| Aerosol |
Oral |
| Capsule |
Oral |
| Liquid |
Intramuscular |
| Liquid |
Intravenous |
| Liquid |
Oral |
| Ointment |
Topical |
| Pellet |
Oral |
| Powder |
Oral |
| Solution |
Intramuscular |
| Solution |
Intravenous |
| Solution |
Oral |
| Solution / drops |
Oral |
| Suspension |
Oral |
| Syrup |
Oral |
| Tablet |
Oral |
|
| Patient Information |
Not Available |
| Contraindications |
Not Available |
| Interactions |
Not Available |
| Drug Interactions |
| Drug |
Interaction |
| Alendronate |
Formation of non-absorbable complexes |
| Amprenavir |
The antiacid decreases the absorption of amprenavir |
| Atazanavir |
This gastric pH modifier decreases the levels/effects of atazanavir |
| Chloroquine |
The antiacid decreases the absorption of chloroquine |
| Ciprofloxacin |
Formation of non-absorbable complexes |
| Clodronate |
Formation of non-absorbable complexes |
| Delavirdine |
The antiacid decreases the absorption of delavirdine |
| Demeclocycline |
Formation of non-absorbable complexes |
| Dihydroquinidine barbiturate |
The antiacid decreases the absorption of quinidine |
| Doxycycline |
Formation of non-absorbable complexes |
| Enoxacin |
Formation of non-absorbable complexes |
| Etidronic acid |
Formation of non-absorbable complexes |
| Fosamprenavir |
The antiacid decreases the absorption of amprenavir |
| Gatifloxacin |
Formation of non-absorbable complexes |
| Gemifloxacin |
Formation of non-absorbable complexes |
| Grepafloxacin |
Formation of non-absorbable complexes |
| Ibandronate |
Formation of non-absorbable complexes |
| Indinavir |
The antiacid decreases the absorption of indinavir |
| Levofloxacin |
Formation of non-absorbable complexes |
| Lomefloxacin |
Formation of non-absorbable complexes |
| Methacycline |
Formation of non-absorbable complexes |
| Minocycline |
Formation of non-absorbable complexes |
| Moxifloxacin |
Formation of non-absorbable complexes |
| Norfloxacin |
Formation of non-absorbable complexes |
| Ofloxacin |
Formation of non-absorbable complexes |
| Oxytetracycline |
Formation of non-absorbable complexes |
| Pefloxacin |
Formation of non-absorbable complexes |
| Polystyrene sulfonate |
Risk of alkalosis in renal impairment |
| Quinidine |
The antiacid decreases the absorption of quindine |
| Quinidine barbiturate |
The antiacid decreases the absorption of quinidine |
| Risedronate |
Formation of non-absorbable complexes |
| Rosuvastatin |
The antiacid decreases the absorption of rosuvastatin |
| Temafloxacin |
Formation of non-absorbable complexes |
| Tetracycline |
Formation of non-absorbable complexes |
| Trovafloxacin |
Formation of non-absorbable complexes |
|
| Food Interactions |
Not Available
|
| Pathways |
Not Available
|
| General References |
- Wikipedia

|
| Organisms Affected |
Not Available |
| Targets |
- Sodium/potassium-transporting ATPase alpha-1 chain
|
|
Drug Target 1
[top]
|
| Target 1 ID |
806 |
| Target 1 Name |
Sodium/potassium-transporting ATPase alpha-1 chain |
| Target 1 Synonyms |
- EC 3.6.3.9
- Na(+)/K(+) ATPase alpha-1 subunit
- Sodium pump subunit alpha 1
- Sodium/potassium-transporting ATPase alpha-1 chain precursor
|
| Target 1 Gene Name |
ATP1A1 |
| Target 1 Protein Sequence |
>Sodium/potassium-transporting ATPase alpha-1 chain precursor
MGKGVGRDKYEPAAVSEQGDKKGKKGKKDRDMDELKKEVSMDDHKLSLDELHRKYGTDLS
RGLTSARAAEILARDGPNALTPPPTTPEWIKFCRQLFGGFSMLLWIGAILCFLAYSIQAA
TEEEPQNDNLYLGVVLSAVVIITGCFSYYQEAKSSKIMESFKNMVPQQALVIRNGEKMSI
NAEEVVVGDLVEVKGGDRIPADLRIISANGCKVDNSSLTGESEPQTRSPDFTNENPLETR
NIAFFSTNCVEGTARGIVVYTGDRTVMGRIATLASGLEGGQTPIAAEIEHFIHIITGVAV
FLGVSFFILSLILEYTWLEAVIFLIGIIVANVPEGLLATVTVCLTLTAKRMARKNCLVKN
LEAVETLGSTSTICSDKTGTLTQNRMTVAHMWFDNQIHEADTTENQSGVSFDKTSATWLA
LSRIAGLCNRAVFQANQENLPILKRAVAGDASESALLKCIELCCGSVKEMRERYAKIVEI
PFNSTNKYQLSIHKNPNTSEPQHLLVMKGAPERILDRCSSILLHGKEQPLDEELKDAFQN
AYLELGGLGERVLGFCHLFLPDEQFPEGFQFDTDDVNFPIDNLCFVGLISMIDPPRAAVP
DAVGKCRSAGIKVIMVTGDHPITAKAIAKGVGIISEGNETVEDIAARLNIPVSQVNPRDA
KACVVHGSDLKDMTSEQLDDILKYHTEIVFARTSPQQKLIIVEGCQRQGAIVAVTGDGVN
DSPALKKADIGVAMGIAGSDVSKQAADMILLDDNFASIVTGVEEGRLIFDNLKKSIAYTL
TSNIPEITPFLIFIIANIPLPLGTVTILCIDLGTDMVPAISLAYEQAESDIMKRQPRNPK
TDKLVNERLISMAYGQIGMIQALGGFFTYFVILAENGFLPIHLLGLRVDWDDRWINDVED
SYGQQWTYEQRKIVEFTCHTAFFVSIVVVQWADLVICKTRRNSVFQQGMKNKILIFGLFE
ETALAAFLSYCPGMGVALRMYPLKPTWWFCAFPYSLLIFVYDEVRKLIIRRRPGGWVEKE
TYY
|
| Target 1 Number of Residues |
1040 |
| Target 1 Molecular Weight |
112897 |
| Target 1 Theoretical pI |
5.15 |
| Target 1 GO Classification |
|
Function
|
hydrolase activity
hydrolase activity, acting on acid anhydrides
hydrolase activity, acting on acid anhydrides, catalyzing transmembrane movement of substances
catalytic activity
binding
nucleotide binding
purine nucleotide binding
adenyl nucleotide binding
ATP binding
monovalent inorganic cation transporter activity
transporter activity
ion transporter activity
cation transporter activity
ATPase activity, coupled to transmembrane movement of ions, phosphorylative mechanism |
|
Process
|
metabolism
monovalent inorganic cation transport
physiological process
cellular physiological process
transport
ion transport
cation transport |
|
Component
|
intrinsic to membrane
integral to membrane
cell
membrane |
|
| Target 1 General Function |
Inorganic ion transport and metabolism |
| Target 1 Specific Function |
This is the catalytic component of the active enzyme, which catalyzes the hydrolysis of ATP coupled with the exchange of sodium and potassium ions across the plasma membrane. This action creates the electrochemical gradient of sodium and potassium ions, providing the energy for active transport of various nutrients |
| Target 1 Pathways |
Not Available
|
| Target 1 Reactions |
- ATP + H2O + Na+in + K+out = ADP + phosphate + Na+out + K+in
|
| Target 1 Pfam Domain Function |
|
| Target 1 Signals |
|
| Target 1 Transmembrane Regions |
- 88-108
- 132-152
- 289-308
- 321-338
- 773-792
- 803-823
- 844-866
- 919-938
- 952-970
- 986-1006
|
| Target 1 Essentiality |
Non-Essential |
| Target 1 GenBank ID Protein |
219942  |
| Target 1 UniProtKB/Swiss-Prot ID |
P05023  |
| Target 1 UniProtKB/Swiss-Prot Entry Name |
AT1A1_HUMAN  |
| Target 1 PDB ID |
1MO8  |
| Target 1 PDB File |
Show |
| Target 1 3D Structure |
|
| Target 1 Cellular Location |
- Membrane
- multi-pass membrane protein
|
| Target 1 Gene Sequence |
>3072 bp
ATGGGGAAGGGGGTTGGACGTGATAAGTATGAGCCTGCAGCTGTTTCAGAACAAGGTGAT
AAAAAGGGCAAAAAGGGCAAAAAAGACAGGGACATGGATGAACTGAAGAAAGAAGTTTCT
ATGGATGATCATAAACTTAGCCTTGATGAACTTCATCGTAAATATGGAACAGACTTGAGC
CGGGGATTAACATCTGCTCGTGCAGCTGAGATCCTGGCGCGAGATGGTCCCAACGCCCTC
ACTCCCCCTCCCACTACTCCTGAATGGATCAAGTTTTGTCGGCAGCTCTTTGGGGGGTTC
TCAATGTTACTGTGGATTGGAGCGATTCTTTGTTTCTTGGCTTATAGCATCCAAGCTGCT
ACAGAAGAGGAACCTCAAAACGATAATCTGTACCTGGGTGTGGTGCTATCAGCCGTTGTA
ATCATAACTGGTTGCTTCTCCTACTATCAAGAAGCTAAAAGTTCAAAGATCATGGAATCC
TTCAAAAACATGGTCCCTCAGCAAGCCCTTGTGATTCGAAATGGTGAGAAAATGAGCATA
AATGCGGAGGAAGTTGTGGTTGGGGATCTGGTGGAAGTAAAAGGAGGAGACCGAATTCCT
GCTGACCTCAGAATCATATCTGCAAATGGCTGCAAGGTGGATAACTCCTCGCTCACTGGT
GAATCAGAACCCCAGACTAGGTCTCCAGATTTCACAAATGAAAACCCCCTGGAGACGAGG
AACATTGCCTTCTTTTCAACAAATTGTGTTGAAGGCACCGCACGTGGTATTGTTGTCTAC
ACTGGGGATCGCACTGTGATGGGAAGAATTGCCACACTTGCTTCTGGGCTGGAAGGAGGC
CAGACCCCCATTGCTGCAGAAATTGAACATTTTATCCACATCATCACGGGTGTGGCTGTG
TTCCTGGGTGTGTCTTTCTTCATCCTTTCTCTCATCCTTGAGTACACCTGGCTTGAGGCT
GTCATCTTCCTCATCGGTATCATCGTAGCCAATGTGCCGGAAGGTTTGCTGGCCACTGTC
ACGGTCTGTCTGACACTTACTGCCAAACGCATGGCAAGGAAAAACTGCTTAGTGAAGAAC
TTAGAAGCTGTGGAGACCTTGGGGTCCACGTCCACCATCTGCTCTGATAAAACTGGAACT
CTGACTCAGAACCGGATGACAGTGGCCCACATGTGGTTTGACAATCAAATCCATGAAGCT
GATACGACAGAGAATCAGAGTGGTGTCTCTTTTGACAAGACTTCAGCTACCTGGCTTGCT
CTGTCCAGAATTGCAGGTCTTTGTAACAGGGCAGTGTTTCAGGCTAACCAGGAAAACCTA
CCTATTCTTAAGCGGGCAGTTGCAGGAGATGCCTCTGAGTCAGCACTCTTAAAGTGCATA
GAGCTGTGCTGTGGTTCCGTGAAGGAGATGAGAGAAAGATACGCCAAAATCGTCGAGATA
CCCTTCAACTCCACCAACAAGTACCAGTTGTCTATTCATAAGAACCCCAACACATCGGAG
CCCCAACACCTGTTGGTGATGAAGGGCGCCCCAGAAAGGATCCTAGACCGTTGCAGCTCT
ATCCTCCTCCACGGCAAGGAGCAGCCCCTGGATGAGGAGCTGAAAGACGCCTTTCAGAAC
GCCTATTTGGAGCTGGGGGGCCTCGGAGAACGAGTCCTAGGTTTCTGCCACCTCTTTCTG
CCAGATGAACAGTTTCCTGAAGGGTTCCAGTTTGACACTGACGATGTGAATTTCCCTATC
GATAATCTGTGCTTTGTTGGGCTCATCTCCATGATTGACCCTCCACGGGCGGCCGTTCCT
GATGCCGTGGGCAAATGTCGAAGTGCTGGAATTAAGGTCATCATGGTCACAGGAGACCAT
CCAATCACAGCTAAAGCTATTGCCAAAGGTGTGGGCATCATCTCAGAAGGCAATGAGACC
GTGGAAGACATTGCTGCCCGCCTCAACATCCCAGTCAGCCAGGTGAACCCCAGGGATGCC
AAGGCCTGCGTAGTACACGGCAGTGATCTAAAGGACATGACCTCCGAGCAGCTGGATGAC
ATTTTGAAGTACCACACTGAGATAGTGTTTGCCAGGACCTCCCCTCAGCAGAAGCTCATC
ATTGTGGAAGGCTGCCAAAGACAGGGTGCTATCGTGGCTGTGACTGGTGACGGTGTGAAT
GACTCTCCAGCTTTGAAGAAAGCAGACATTGGGGTTGCTATGGGGATTGCTGGCTCAGAT
GTGTCCAAGCAAGCTGCTGACATGATTCTTCTGGATGACAACTTTGCCTCAATTGTGACT
GGAGTAGAGGAAGGTCGTCTGATCTTTGATAACTTGAAGAAATCCATTGCTTATACCTTA
ACCAGTAACATTCCCGAGATCACCCCGTTCCTGATATTTATTATTGCAAACATTCCACTA
CCACTGGGGACTGTCACCATCCTCTGCATTGACTTGGGCACTGACATGGTTCCTGCCATC
TCCCTGGCTTATGAGCAGGCTGAGAGTGACATCATGAAGAGACAGCCCAGAAATCCCAAA
ACAGACAAACTTGTGAATGAGCGGCTGATCAGCATGGCCTATGGGCAGATTGGAATGATC
CAGGCCCTGGGAGGCTTCTTTACTTACTTTGTGATTCTGGCTGAGAACGGCTTCCTCCCA
ATTCACCTGTTGGGCCTCCGAGTGGACTGGGATGACCGCTGGATCAACGATGTGGAAGAC
AGCTACGGGCAGCAGTGGACCTATGAGCAGAGGAAAATCGTGGAGTTCACCTGCCACACA
GCCTTCTTCGTCAGTATCGTGGTGGTGCAGTGGGCCGACTTGGTCATCTGTAAGACCAGG
AGGAATTCGGTCTTCCAGCAGGGGATGAAGAACAAGATCTTGATATTTGGCCTCTTTGAA
GAGACAGCCCTGGCTGCTTTCCTTTCCTACTGCCCTGGAATGGGTGTTGCTCTTAGGATG
TATCCCCTCAAACCTACCTGGTGGTTCTGTGCCTTCCCCTACTCTCTTCTCATCTTCGTA
TATGACGAAGTCAGAAAACTCATCATCAGGCGACGCCCTGGCGGCTGGGTGGAGAAGGAA
ACCTACTATTAG
|
| Target 1 GenBank Gene ID |
|
| Target 1 GeneCard ID |
ATP1A1  |
| Target 1 GenAtlas ID |
ATP1A1  |
| Target 1 HGNC ID |
HGNC:799  |
| Target 1 Chromosome Location |
1 |
| Target 1 Locus |
1p21 |
| Target 1 SNPs |
SNPJam Report  |
| Target 1 General References |
- Shull MM, Pugh DG, Lingrel JB: The human Na, K-ATPase alpha 1 gene: characterization of the 5'-flanking region and identification of a restriction fragment length polymorphism. Genomics. 1990 Mar;6(3):451-60. [PubMed
]
- Kawakami K, Ohta T, Nojima H, Nagano K: Primary structure of the alpha-subunit of human Na,K-ATPase deduced from cDNA sequence. J Biochem (Tokyo). 1986 Aug;100(2):389-97. [PubMed
]
- Chehab FF, Kan YW, Law ML, Hartz J, Kao FT, Blostein R: Human placental Na+,K+-ATPase alpha subunit: cDNA cloning, tissue expression, DNA polymorphism, and chromosomal localization. Proc Natl Acad Sci U S A. 1987 Nov;84(22):7901-5. [PubMed
]
- Shull MM, Lingrel JB: Multiple genes encode the human Na+,K+-ATPase catalytic subunit. Proc Natl Acad Sci U S A. 1987 Jun;84(12):4039-43. [PubMed
]
- Sverdlov ED, Monastyrskaya GS, Broude NE, Ushkaryov YuA, Allikmets RL, Melkov AM, Smirnov YuV, Malyshev IV, Dulobova IE, Petrukhin KE, et al.: The family of human Na+,K+-ATPase genes. No less than five genes and/or pseudogenes related to the alpha-subunit. FEBS Lett. 1987 Jun 15;217(2):275-8. [PubMed
]
- Ruiz A, Bhat SP, Bok D: Characterization and quantification of full-length and truncated Na,K-ATPase alpha 1 and beta 1 RNA transcripts expressed in human retinal pigment epithelium. Gene. 1995 Apr 3;155(2):179-84. [PubMed
]
|
| Target 1 Drug References |
- Buchachenko AL, Kuznetsov DA, Berdinskii VL: [New mechanisms of biological effects of electromagnetic fields] Biofizika. 2006 May-Jun;51(3):545-52. [PubMed
]
- Sirijovski N, Olsson U, Lundqvist J, Al-Karadaghi S, Willows RD, Hansson M: ATPase activity associated with the magnesium chelatase H-subunit of the chlorophyll biosynthetic pathway is an artefact. Biochem J. 2006 Dec 15;400(3):477-84. [PubMed
]
- Balasubramaniyan V, Nalini N: Leptin alters brain adenosine triphosphatase activity in ethanol-mediated neurotoxicity in mice. Singapore Med J. 2006 Oct;47(10):864-8. [PubMed
]
- Yang JL, You JF, Li YY, Wu P, Zheng SJ: Magnesium enhances aluminum-induced citrate secretion in rice bean roots (Vigna umbellata) by restoring plasma membrane H+-ATPase activity. Plant Cell Physiol. 2007 Jan;48(1):66-73. Epub 2006 Nov 27. [PubMed
]
- Nogovitsina OR, Levitina EV: Neurological aspects of the clinical features, pathophysiology, and corrections of impairments in attention deficit hyperactivity disorder. Neurosci Behav Physiol. 2007 Mar;37(3):199-202. [PubMed
]
|