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Record Information
Version3.6
Creation Date2012-09-06 15:16:51 UTC
Update Date2016-02-11 01:31:49 UTC
HMDB IDHMDB15188
Secondary Accession NumbersNone
Metabolite Identification
Common NameMimosine
DescriptionMimosine is only found in individuals that have used or taken this drug. It is an antineoplastic alanine-substituted pyridine derivative isolated from Leucena glauca. [PubChem]Mimosine causes inhibition of DNA replication, changes in the progression of the cells in the cell cycle, and apoptosis. Mimosine appears to introduce breaks into DNA. Mimosine is an iron/zinc chelator. Iron depletion induces DNA double-strand breaks in treated cells, and activates a DNA damage response that results in focal phosphorylation of histones. This leads to inhibition of DNA replication and/or DNA elongation. Some studies indicate that mimosine prevents the initiation of DNA replication, whereas other studies indicate that mimosine disrupts elongation of the replication fork by impairing deoxyribonucleotide synthesis by inhibiting the activity of the iron-dependent enzyme ribonucleotide reductase and the transcription of the cytoplasmic serine hydroxymethyltransferase gene (SHMT). Inhibition of serine hydroxymethyltransferase is moderated by a zinc responsive unit located in front of the SHMT gene.
Structure
Thumb
Synonyms
ValueSource
(S)-2-amino-3-(3-Hydroxy-4-oxo-4H-pyridin-1-yl)propanoateChEBI
(S)-2-amino-3-(3-Hydroxy-4-oxo-4H-pyridin-1-yl)propanoic acidGenerator
L-MimosineHMDB
LeucaenineHMDB
LeucaenolHMDB
LeucenineHMDB
LeucenolHMDB
MimosinHMDB
Chemical FormulaC8H10N2O4
Average Molecular Weight198.176
Monoisotopic Molecular Weight198.064056818
IUPAC Name(2S)-2-amino-3-(3-hydroxy-4-oxo-1,4-dihydropyridin-1-yl)propanoic acid
Traditional Namemimosine
CAS Registry Number500-44-7
SMILES
N[C@@H](CN1C=CC(=O)C(O)=C1)C(O)=O
InChI Identifier
InChI=1S/C8H10N2O4/c9-5(8(13)14)3-10-2-1-6(11)7(12)4-10/h1-2,4-5,12H,3,9H2,(H,13,14)/t5-/m0/s1
InChI KeyInChIKey=WZNJWVWKTVETCG-YFKPBYRVSA-N
Chemical Taxonomy
DescriptionThis compound belongs to the class of organic compounds known as l-alpha-amino acids. These are alpha amino acids which have the L-configuration of the alpha-carbon atom.
KingdomOrganic compounds
Super ClassOrganic acids and derivatives
ClassCarboxylic acids and derivatives
Sub ClassAmino acids, peptides, and analogues
Direct ParentL-alpha-amino acids
Alternative Parents
Substituents
  • L-alpha-amino acid
  • Hydroxypyridine
  • Dihydropyridine
  • Pyridine
  • Hydropyridine
  • Heteroaromatic compound
  • Vinylogous amide
  • Cyclic ketone
  • Azacycle
  • Organoheterocyclic compound
  • Monocarboxylic acid or derivatives
  • Carboxylic acid
  • Hydrocarbon derivative
  • Primary amine
  • Organooxygen compound
  • Organonitrogen compound
  • Primary aliphatic amine
  • Carbonyl group
  • Amine
  • Aromatic heteromonocyclic compound
Molecular FrameworkAromatic heteromonocyclic compounds
External Descriptors
Ontology
StatusExpected but not Quantified
Origin
  • Drug
Biofunction
  • Antineoplastic Agents
Application
  • Pharmaceutical
Cellular locations
  • Cytoplasm
  • Extracellular
  • Membrane
Physical Properties
StateSolid
Experimental Properties
PropertyValueReference
Melting Point228 °CNot Available
Boiling PointNot AvailableNot Available
Water Solubility1.31e+01 g/LNot Available
LogP-2.5Not Available
Predicted Properties
PropertyValueSource
Water Solubility13.1 mg/mLALOGPS
logP-2.4ALOGPS
logP-3ChemAxon
logS-1.2ALOGPS
pKa (Strongest Acidic)1.94ChemAxon
pKa (Strongest Basic)8.88ChemAxon
Physiological Charge0ChemAxon
Hydrogen Acceptor Count6ChemAxon
Hydrogen Donor Count3ChemAxon
Polar Surface Area103.86 Å2ChemAxon
Rotatable Bond Count3ChemAxon
Refractivity48.66 m3·mol-1ChemAxon
Polarizability18.2 Å3ChemAxon
Number of Rings1ChemAxon
Bioavailability1ChemAxon
Rule of FiveYesChemAxon
Ghose FilterYesChemAxon
Veber's RuleYesChemAxon
MDDR-like RuleYesChemAxon
Spectra
SpectraNot Available
Biological Properties
Cellular Locations
  • Cytoplasm
  • Extracellular
  • Membrane
Biofluid Locations
  • Blood
  • Urine
Tissue LocationNot Available
PathwaysNot Available
Normal Concentrations
BiofluidStatusValueAgeSexConditionReferenceDetails
BloodExpected but not QuantifiedNot ApplicableNot AvailableNot AvailableTaking drug identified by DrugBank entry DB01055
  • Not Applicable
details
UrineExpected but not QuantifiedNot ApplicableNot AvailableNot AvailableTaking drug identified by DrugBank entry DB01055
  • Not Applicable
details
Abnormal Concentrations
Not Available
Associated Disorders and Diseases
Disease ReferencesNone
Associated OMIM IDsNone
DrugBank IDDB01055
DrugBank Metabolite IDNot Available
Phenol Explorer Compound IDNot Available
Phenol Explorer Metabolite IDNot Available
FoodDB IDNot Available
KNApSAcK IDNot Available
Chemspider ID389405
KEGG Compound IDC04771
BioCyc IDNot Available
BiGG IDNot Available
Wikipedia LinkMimosine
NuGOwiki LinkHMDB15188
Metagene LinkHMDB15188
METLIN IDNot Available
PubChem Compound440473
PDB IDNot Available
ChEBI ID29063
References
Synthesis ReferenceNot Available
Material Safety Data Sheet (MSDS)Not Available
General ReferencesNot Available

Enzymes

General function:
Involved in oxidoreductase activity
Specific function:
This is a copper-containing oxidase that functions in the formation of pigments such as melanins and other polyphenolic compounds. Catalyzes the rate-limiting conversions of tyrosine to DOPA, DOPA to DOPA-quinone and possibly 5,6-dihydroxyindole to indole-5,6 quinone.
Gene Name:
TYR
Uniprot ID:
P14679
Molecular weight:
60392.69
References
  1. Ahmad VU, Ullah F, Hussain J, Farooq U, Zubair M, Khan MT, Choudhary MI: Tyrosinase inhibitors from Rhododendron collettianum and their structure-activity relationship (SAR) studies. Chem Pharm Bull (Tokyo). 2004 Dec;52(12):1458-61. [15577244 ]
  2. Khan KM, Mughal UR, Khan MT, Zia-Ullah, Perveen S, Choudhary MI: Oxazolones: new tyrosinase inhibitors; synthesis and their structure-activity relationships. Bioorg Med Chem. 2006 Sep 1;14(17):6027-33. Epub 2006 Jun 5. [16750372 ]
  3. Sugumaran M: Tyrosinase catalyzes an unusual oxidative decarboxylation of 3,4-dihydroxymandelate. Biochemistry. 1986 Aug 12;25(16):4489-92. [3094574 ]
  4. Woolery GL, Powers L, Winkler M, Solomon EI, Lerch K, Spiro TG: Extended X-ray absorption fine structure study of the coupled binuclear copper active site of tyrosinase from Neurospora crassa. Biochim Biophys Acta. 1984 Jul 31;788(2):155-61. [6234942 ]
General function:
Involved in catalytic activity
Specific function:
Interconversion of serine and glycine.
Gene Name:
SHMT1
Uniprot ID:
P34896
Molecular weight:
53082.18
References
  1. Oppenheim EW, Nasrallah IM, Mastri MG, Stover PJ: Mimosine is a cell-specific antagonist of folate metabolism. J Biol Chem. 2000 Jun 23;275(25):19268-74. [10766749 ]
  2. Conti P, Frydas S, Reale M, Barbacane RC, Di Gioacchino M, Felaco M, Trakatellis A: Inhibition of MCP-1 and MIP-2 transcription and translation by mimosine in muscle tissue infected with the parasite Trichinella spiralis. Mol Cell Biochem. 2002 Jan;229(1-2):129-37. [11936838 ]
  3. Perry C, Sastry R, Nasrallah IM, Stover PJ: Mimosine attenuates serine hydroxymethyltransferase transcription by chelating zinc. Implications for inhibition of DNA replication. J Biol Chem. 2005 Jan 7;280(1):396-400. Epub 2004 Nov 4. [15531579 ]
  4. Lin HB, Falchetto R, Mosca PJ, Shabanowitz J, Hunt DF, Hamlin JL: Mimosine targets serine hydroxymethyltransferase. J Biol Chem. 1996 Feb 2;271(5):2548-56. [8576220 ]
General function:
Involved in chemokine activity
Specific function:
Chemotactic factor that attracts monocytes and basophils but not neutrophils or eosinophils. Augments monocyte anti-tumor activity. Has been implicated in the pathogenesis of diseases characterized by monocytic infiltrates, like psoriasis, rheumatoid arthritis or atherosclerosis. May be involved in the recruitment of monocytes into the arterial wall during the disease process of atherosclerosis
Gene Name:
CCL2
Uniprot ID:
P13500
Molecular weight:
11024.9
References
  1. Conti P, Frydas S, Reale M, Barbacane RC, Di Gioacchino M, Felaco M, Trakatellis A: Inhibition of MCP-1 and MIP-2 transcription and translation by mimosine in muscle tissue infected with the parasite Trichinella spiralis. Mol Cell Biochem. 2002 Jan;229(1-2):129-37. [11936838 ]
  2. Frydas S, Papaioannou N, Papazahariadou M, Hatzistilianou M, Karagouni E, Trakatelli M, Brellou G, Petrarca C, Castellani ML, Conti P, Riccioni G, Patruno A, Grilli A: Inhibition of MCP-1 and MIP-2 chemokines in murine trichinellosis: effect of the anti-inflammatory compound L-mimosine. Int J Immunopathol Pharmacol. 2005 Jan-Mar;18(1):85-94. [15698514 ]