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Record Information
Version3.6
Creation Date2012-09-06 15:16:50 UTC
Update Date2016-02-11 01:30:37 UTC
HMDB IDHMDB14924
Secondary Accession NumbersNone
Metabolite Identification
Common NameMarimastat
DescriptionMarimastat is only found in individuals that have used or taken this drug. It is used in the treatment of cancer, Marmiastat is an angiogenesis and metastasis inhibitor. As an angiogenesis inhibitor it limits the growth and production of blood vessels. As an antimetatstatic agent it prevents malignant cells from breaching the basement membranes.Marimastat is a broad spectrum matrix metalloprotease inhibitor. It mimics the peptide structure of natural MMP substrates and binds to matrix metalloproteases, thereby preventing the degradation of the basement membrane by these proteases. This antiprotease action prevents the migration of endothelial cells needed to form new blood vessels. Inhibition of MMPs also prevents the entry and exit of tumor cells into existing blood cells, thereby preventing metastasis.
Structure
Thumb
SynonymsNot Available
Chemical FormulaC15H29N3O5
Average Molecular Weight331.4079
Monoisotopic Molecular Weight331.210721053
IUPAC Name(2S,3R)-N'-[(1S)-2,2-dimethyl-1-(methylcarbamoyl)propyl]-N,2-dihydroxy-3-(2-methylpropyl)butanediamide
Traditional Name(2S,3R)-N'-[(1S)-2,2-dimethyl-1-(methylcarbamoyl)propyl]-N,2-dihydroxy-3-(2-methylpropyl)succinamide
CAS Registry Number154039-60-8
SMILES
CNC(=O)[C@@H](NC(=O)[C@H](CC(C)C)[C@H](O)C(=O)NO)C(C)(C)C
InChI Identifier
InChI=1S/C15H29N3O5/c1-8(2)7-9(10(19)13(21)18-23)12(20)17-11(14(22)16-6)15(3,4)5/h8-11,19,23H,7H2,1-6H3,(H,16,22)(H,17,20)(H,18,21)/t9-,10+,11-/m1/s1
InChI KeyInChIKey=OCSMOTCMPXTDND-OUAUKWLOSA-N
Chemical Taxonomy
DescriptionThis compound belongs to the class of organic compounds known as n-acyl-alpha amino acids and derivatives. These are compounds containing an alpha amino acid (or a derivative thereof) which bears an acyl group at its terminal nitrogen atom.
KingdomOrganic compounds
Super ClassOrganic acids and derivatives
ClassCarboxylic acids and derivatives
Sub ClassAmino acids, peptides, and analogues
Direct ParentN-acyl-alpha amino acids and derivatives
Alternative Parents
Substituents
  • N-acyl-alpha amino acid or derivatives
  • Alpha-amino acid amide
  • Fatty acyl
  • N-acyl-amine
  • Monosaccharide
  • Fatty amide
  • Secondary carboxylic acid amide
  • Secondary alcohol
  • Hydroxamic acid
  • Carboxamide group
  • Carboxylic acid amide
  • Hydrocarbon derivative
  • Organooxygen compound
  • Organonitrogen compound
  • Carbonyl group
  • Alcohol
  • Aliphatic acyclic compound
Molecular FrameworkAliphatic acyclic compounds
External Descriptors
Ontology
StatusExpected but not Quantified
Origin
  • Drug
Biofunction
  • Antineoplastic Agents
  • Enzyme Inhibitors
Application
  • Pharmaceutical
Cellular locations
  • Cytoplasm
  • Extracellular
  • Membrane
Physical Properties
StateSolid
Experimental Properties
PropertyValueReference
Melting PointNot AvailableNot Available
Boiling PointNot AvailableNot Available
Water Solubility3.38e+00 g/LNot Available
LogP0.4Not Available
Predicted Properties
PropertyValueSource
Water Solubility3.38 mg/mLALOGPS
logP0.41ALOGPS
logP-0.059ChemAxon
logS-2ALOGPS
pKa (Strongest Acidic)8.61ChemAxon
pKa (Strongest Basic)-1ChemAxon
Physiological Charge0ChemAxon
Hydrogen Acceptor Count5ChemAxon
Hydrogen Donor Count5ChemAxon
Polar Surface Area127.76 Å2ChemAxon
Rotatable Bond Count8ChemAxon
Refractivity84.2 m3·mol-1ChemAxon
Polarizability34.99 Å3ChemAxon
Number of Rings0ChemAxon
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 DB00786
  • Not Applicable
details
UrineExpected but not QuantifiedNot ApplicableNot AvailableNot AvailableTaking drug identified by DrugBank entry DB00786
  • Not Applicable
details
Abnormal Concentrations
Not Available
Associated Disorders and Diseases
Disease ReferencesNone
Associated OMIM IDsNone
DrugBank IDDB00786
DrugBank Metabolite IDNot Available
Phenol Explorer Compound IDNot Available
Phenol Explorer Metabolite IDNot Available
FoodDB IDNot Available
KNApSAcK IDNot Available
Chemspider ID106358
KEGG Compound IDNot Available
BioCyc IDNot Available
BiGG IDNot Available
Wikipedia LinkMarimastat
NuGOwiki LinkHMDB14924
Metagene LinkHMDB14924
METLIN IDNot Available
PubChem Compound119031
PDB ID097
ChEBI ID50662
References
Synthesis ReferenceNot Available
Material Safety Data Sheet (MSDS)Not Available
General ReferencesNot Available

Enzymes

General function:
Involved in metalloendopeptidase activity
Specific function:
May play an essential role in local proteolysis of the extracellular matrix and in leukocyte migration. Could play a role in bone osteoclastic resorption. Cleaves KiSS1 at a Gly-|-Leu bond. Cleaves type IV and type V collagen into large C-terminal three quarter fragments and shorter N-terminal one quarter fragments. Degrades fibronectin but not laminin or Pz-peptide
Gene Name:
MMP9
Uniprot ID:
P14780
Molecular weight:
78457.5
References
  1. Underwood CK, Min D, Lyons JG, Hambley TW: The interaction of metal ions and Marimastat with matrix metalloproteinase 9. J Inorg Biochem. 2003 Jun 1;95(2-3):165-70. [12763661 ]
  2. Nenan S, Lagente V, Planquois JM, Hitier S, Berna P, Bertrand CP, Boichot E: Metalloelastase (MMP-12) induced inflammatory response in mice airways: effects of dexamethasone, rolipram and marimastat. Eur J Pharmacol. 2007 Mar 15;559(1):75-81. Epub 2006 Dec 12. [17234180 ]
  3. Chen X, Ji ZL, Chen YZ: TTD: Therapeutic Target Database. Nucleic Acids Res. 2002 Jan 1;30(1):412-5. [11752352 ]
General function:
Involved in calcium ion binding
Specific function:
Degrades collagen type I. Does not act on gelatin or casein. Could have a role in tumoral process
Gene Name:
MMP13
Uniprot ID:
P45452
Molecular weight:
53819.3
References
  1. Heath EI, Grochow LB: Clinical potential of matrix metalloprotease inhibitors in cancer therapy. Drugs. 2000 May;59(5):1043-55. [10852638 ]
  2. Belotti D, Paganoni P, Giavazzi R: MMP inhibitors: experimental and clinical studies. Int J Biol Markers. 1999 Oct-Dec;14(4):232-8. [10669951 ]
General function:
Involved in metalloendopeptidase activity
Specific function:
Cleaves collagens of types I, II, and III at one site in the helical domain. Also cleaves collagens of types VII and X. In case of HIV infection, interacts and cleaves the secreted viral Tat protein, leading to a decrease in neuronal Tat's mediated neurotoxicity
Gene Name:
MMP1
Uniprot ID:
P03956
Molecular weight:
54006.6
References
  1. Heath EI, Grochow LB: Clinical potential of matrix metalloprotease inhibitors in cancer therapy. Drugs. 2000 May;59(5):1043-55. [10852638 ]
  2. Belotti D, Paganoni P, Giavazzi R: MMP inhibitors: experimental and clinical studies. Int J Biol Markers. 1999 Oct-Dec;14(4):232-8. [10669951 ]
  3. Chen X, Ji ZL, Chen YZ: TTD: Therapeutic Target Database. Nucleic Acids Res. 2002 Jan 1;30(1):412-5. [11752352 ]
General function:
Involved in metalloendopeptidase activity
Specific function:
Can degrade fibronectin, laminin, gelatins of type I, III, IV, and V; collagens III, IV, X, and IX, and cartilage proteoglycans. Activates procollagenase
Gene Name:
MMP3
Uniprot ID:
P08254
Molecular weight:
53976.8
References
  1. Chen X, Ji ZL, Chen YZ: TTD: Therapeutic Target Database. Nucleic Acids Res. 2002 Jan 1;30(1):412-5. [11752352 ]
General function:
Involved in metalloendopeptidase activity
Specific function:
Degrades amelogenin, the major protein component of the enamel matrix and two of the macromolecules characterizing the cartilage extracellular matrix:aggrecan and the cartilage oligomeric matrix protein (COMP). May play a central role in tooth enamel formation
Gene Name:
MMP20
Uniprot ID:
O60882
Molecular weight:
54359.4
References
  1. Heath EI, Grochow LB: Clinical potential of matrix metalloprotease inhibitors in cancer therapy. Drugs. 2000 May;59(5):1043-55. [10852638 ]
  2. Belotti D, Paganoni P, Giavazzi R: MMP inhibitors: experimental and clinical studies. Int J Biol Markers. 1999 Oct-Dec;14(4):232-8. [10669951 ]
General function:
Involved in metalloendopeptidase activity
Specific function:
PEX, the C-terminal non-catalytic fragment of MMP2, posseses anti-angiogenic and anti-tumor properties and inhibits cell migration and cell adhesion to FGF2 and vitronectin. Ligand for integrinv/beta3 on the surface of blood vessels
Gene Name:
MMP2
Uniprot ID:
P08253
Molecular weight:
73881.7
References
  1. Chen X, Ji ZL, Chen YZ: TTD: Therapeutic Target Database. Nucleic Acids Res. 2002 Jan 1;30(1):412-5. [11752352 ]
  2. Treharne GD, Boyle JR, Goodall S, Loftus IM, Bell PR, Thompson MM: Marimastat inhibits elastin degradation and matrix metalloproteinase 2 activity in a model of aneurysm disease. Br J Surg. 1999 Aug;86(8):1053-8. [10460642 ]
  3. Fanchon S, Bourd K, Septier D, Everts V, Beertsen W, Menashi S, Goldberg M: Involvement of matrix metalloproteinases in the onset of dentin mineralization. Eur J Oral Sci. 2004 Apr;112(2):171-6. [15056115 ]
  4. Bernardo MM, Brown S, Li ZH, Fridman R, Mobashery S: Design, synthesis, and characterization of potent, slow-binding inhibitors that are selective for gelatinases. J Biol Chem. 2002 Mar 29;277(13):11201-7. Epub 2002 Jan 14. [11790786 ]
  5. Shinoda K, Shibuya M, Hibino S, Ono Y, Matsuda K, Takemura A, Zou D, Kokubo Y, Takechi A, Kudoh S: A novel matrix metalloproteinase inhibitor, FYK-1388 suppresses tumor growth, metastasis and angiogenesis by human fibrosarcoma cell line. Int J Oncol. 2003 Feb;22(2):281-8. [12527923 ]
  6. Bourd-Boittin K, Fridman R, Fanchon S, Septier D, Goldberg M, Menashi S: Matrix metalloproteinase inhibition impairs the processing, formation and mineralization of dental tissues during mouse molar development. Exp Cell Res. 2005 Apr 1;304(2):493-505. Epub 2005 Jan 11. [15748894 ]
General function:
Involved in metalloendopeptidase activity
Specific function:
Seems to specifically activate progelatinase A. May thus trigger invasion by tumor cells by activating progelatinase A on the tumor cell surface
Gene Name:
MMP14
Uniprot ID:
P50281
Molecular weight:
65883.4
References
  1. Heath EI, Grochow LB: Clinical potential of matrix metalloprotease inhibitors in cancer therapy. Drugs. 2000 May;59(5):1043-55. [10852638 ]
  2. Belotti D, Paganoni P, Giavazzi R: MMP inhibitors: experimental and clinical studies. Int J Biol Markers. 1999 Oct-Dec;14(4):232-8. [10669951 ]
General function:
Involved in metalloendopeptidase activity
Specific function:
Degrades casein, gelatins of types I, III, IV, and V, and fibronectin. Activates procollagenase
Gene Name:
MMP7
Uniprot ID:
P09237
Molecular weight:
29676.6
References
  1. Heath EI, Grochow LB: Clinical potential of matrix metalloprotease inhibitors in cancer therapy. Drugs. 2000 May;59(5):1043-55. [10852638 ]
  2. Belotti D, Paganoni P, Giavazzi R: MMP inhibitors: experimental and clinical studies. Int J Biol Markers. 1999 Oct-Dec;14(4):232-8. [10669951 ]
General function:
Involved in metalloendopeptidase activity
Specific function:
Can degrade fibronectin, gelatins of type I, III, IV, and V; weakly collagens III, IV, and V. Activates procollagenase
Gene Name:
MMP10
Uniprot ID:
P09238
Molecular weight:
54150.7
References
  1. Heath EI, Grochow LB: Clinical potential of matrix metalloprotease inhibitors in cancer therapy. Drugs. 2000 May;59(5):1043-55. [10852638 ]
  2. Belotti D, Paganoni P, Giavazzi R: MMP inhibitors: experimental and clinical studies. Int J Biol Markers. 1999 Oct-Dec;14(4):232-8. [10669951 ]
General function:
Involved in metalloendopeptidase activity
Specific function:
May play an important role in the progression of epithelial malignancies
Gene Name:
MMP11
Uniprot ID:
P24347
Molecular weight:
54617.5
References
  1. Heath EI, Grochow LB: Clinical potential of matrix metalloprotease inhibitors in cancer therapy. Drugs. 2000 May;59(5):1043-55. [10852638 ]
  2. Belotti D, Paganoni P, Giavazzi R: MMP inhibitors: experimental and clinical studies. Int J Biol Markers. 1999 Oct-Dec;14(4):232-8. [10669951 ]
General function:
Involved in metalloendopeptidase activity
Specific function:
May be involved in tissue injury and remodeling. Has significant elastolytic activity. Can accept large and small amino acids at the P1' site, but has a preference for leucine. Aromatic or hydrophobic residues are preferred at the P1 site, with small hydrophobic residues (preferably alanine) occupying P3
Gene Name:
MMP12
Uniprot ID:
P39900
Molecular weight:
54001.2
References
  1. Heath EI, Grochow LB: Clinical potential of matrix metalloprotease inhibitors in cancer therapy. Drugs. 2000 May;59(5):1043-55. [10852638 ]
  2. Belotti D, Paganoni P, Giavazzi R: MMP inhibitors: experimental and clinical studies. Int J Biol Markers. 1999 Oct-Dec;14(4):232-8. [10669951 ]
General function:
Involved in metalloendopeptidase activity
Specific function:
Endopeptidase that degrades various components of the extracellular matrix. May activate progelatinase A
Gene Name:
MMP15
Uniprot ID:
P51511
Molecular weight:
75806.4
References
  1. Heath EI, Grochow LB: Clinical potential of matrix metalloprotease inhibitors in cancer therapy. Drugs. 2000 May;59(5):1043-55. [10852638 ]
  2. Belotti D, Paganoni P, Giavazzi R: MMP inhibitors: experimental and clinical studies. Int J Biol Markers. 1999 Oct-Dec;14(4):232-8. [10669951 ]
General function:
Involved in metalloendopeptidase activity
Specific function:
Endopeptidase that degrades various components of the extracellular matrix, such as collagen type III and fibronectin. Activates progelatinase A. Involved in the matrix remodeling of blood vessels. Isoform short cleaves fibronectin and also collagen type III, but at lower rate. It has no effect on type I, II, IV and V collagen. However, upon interaction with CSPG4, it may be involved in degradation and invasion of type I collagen by melanoma cells
Gene Name:
MMP16
Uniprot ID:
P51512
Molecular weight:
69521.0
References
  1. Heath EI, Grochow LB: Clinical potential of matrix metalloprotease inhibitors in cancer therapy. Drugs. 2000 May;59(5):1043-55. [10852638 ]
  2. Belotti D, Paganoni P, Giavazzi R: MMP inhibitors: experimental and clinical studies. Int J Biol Markers. 1999 Oct-Dec;14(4):232-8. [10669951 ]
General function:
Involved in metalloendopeptidase activity
Specific function:
Endopeptidase that degrades various components of the extracellular matrix, such as fibrin. May be involved in the activation of membrane-bound precursors of growth factors or inflammatory mediators, such as tumor necrosis factor-alpha. May also be involved in tumoral process. Not obvious if able to proteolytically activate progelatinase A. Does not hydrolyze collagen types I, II, III, IV and V, gelatin, fibronectin, laminin, decorin nor alpha1-antitrypsin
Gene Name:
MMP17
Uniprot ID:
Q9ULZ9
Molecular weight:
66652.2
References
  1. Heath EI, Grochow LB: Clinical potential of matrix metalloprotease inhibitors in cancer therapy. Drugs. 2000 May;59(5):1043-55. [10852638 ]
  2. Belotti D, Paganoni P, Giavazzi R: MMP inhibitors: experimental and clinical studies. Int J Biol Markers. 1999 Oct-Dec;14(4):232-8. [10669951 ]
General function:
Involved in metalloendopeptidase activity
Specific function:
Endopeptidase that degrades various components of the extracellular matrix, such as aggrecan and cartilage oligomeric matrix protein (comp), during development, haemostasis and pathological conditions (arthritic disease). May also play a role in neovascularization or angiogenesis. Hydrolyzes collagen type IV, laminin, nidogen, nascin-C isoform, fibronectin, and type I gelatin
Gene Name:
MMP19
Uniprot ID:
Q99542
Molecular weight:
57356.6
References
  1. Heath EI, Grochow LB: Clinical potential of matrix metalloprotease inhibitors in cancer therapy. Drugs. 2000 May;59(5):1043-55. [10852638 ]
  2. Belotti D, Paganoni P, Giavazzi R: MMP inhibitors: experimental and clinical studies. Int J Biol Markers. 1999 Oct-Dec;14(4):232-8. [10669951 ]
General function:
Involved in metalloendopeptidase activity
Specific function:
May have an important and specific function in tumor progression and embryogenesis. Cleaves alpha-1-antitrypsin
Gene Name:
MMP21
Uniprot ID:
Q8N119
Molecular weight:
65014.8
References
  1. Heath EI, Grochow LB: Clinical potential of matrix metalloprotease inhibitors in cancer therapy. Drugs. 2000 May;59(5):1043-55. [10852638 ]
  2. Belotti D, Paganoni P, Giavazzi R: MMP inhibitors: experimental and clinical studies. Int J Biol Markers. 1999 Oct-Dec;14(4):232-8. [10669951 ]
General function:
Involved in metalloendopeptidase activity
Specific function:
Activates progelatinase A. May also be a proteoglycanase involved in degradation of proteoglycans, such as dermatan sulfate and chondroitin sulfate proteoglycans. Cleaves partially fibronectin, but not collagen type I, nor laminin
Gene Name:
MMP24
Uniprot ID:
Q9Y5R2
Molecular weight:
73230.9
References
  1. Heath EI, Grochow LB: Clinical potential of matrix metalloprotease inhibitors in cancer therapy. Drugs. 2000 May;59(5):1043-55. [10852638 ]
  2. Belotti D, Paganoni P, Giavazzi R: MMP inhibitors: experimental and clinical studies. Int J Biol Markers. 1999 Oct-Dec;14(4):232-8. [10669951 ]
General function:
Involved in metalloendopeptidase activity
Specific function:
May activate progelatinase A
Gene Name:
MMP25
Uniprot ID:
Q9NPA2
Molecular weight:
62553.4
References
  1. Heath EI, Grochow LB: Clinical potential of matrix metalloprotease inhibitors in cancer therapy. Drugs. 2000 May;59(5):1043-55. [10852638 ]
  2. Belotti D, Paganoni P, Giavazzi R: MMP inhibitors: experimental and clinical studies. Int J Biol Markers. 1999 Oct-Dec;14(4):232-8. [10669951 ]
General function:
Involved in metalloendopeptidase activity
Specific function:
May hydrolyze collagen type IV, fibronectin, fibrinogen, beta-casein, type I gelatin and alpha-1 proteinase inhibitor. Is also able to activates progelatinase B
Gene Name:
MMP26
Uniprot ID:
Q9NRE1
Molecular weight:
29708.3
References
  1. Heath EI, Grochow LB: Clinical potential of matrix metalloprotease inhibitors in cancer therapy. Drugs. 2000 May;59(5):1043-55. [10852638 ]
  2. Belotti D, Paganoni P, Giavazzi R: MMP inhibitors: experimental and clinical studies. Int J Biol Markers. 1999 Oct-Dec;14(4):232-8. [10669951 ]
General function:
Involved in metalloendopeptidase activity
Specific function:
Matrix metalloproteinases degrade protein components of the extracellular matrix such as fibronectin, laminin, gelatins and/or collagens
Gene Name:
MMP27
Uniprot ID:
Q9H306
Molecular weight:
59025.4
References
  1. Heath EI, Grochow LB: Clinical potential of matrix metalloprotease inhibitors in cancer therapy. Drugs. 2000 May;59(5):1043-55. [10852638 ]
  2. Belotti D, Paganoni P, Giavazzi R: MMP inhibitors: experimental and clinical studies. Int J Biol Markers. 1999 Oct-Dec;14(4):232-8. [10669951 ]
General function:
Involved in metalloendopeptidase activity
Specific function:
Can degrade casein. Could play a role in tissues homeostasis and repair
Gene Name:
MMP28
Uniprot ID:
Q9H239
Molecular weight:
58938.5
References
  1. Heath EI, Grochow LB: Clinical potential of matrix metalloprotease inhibitors in cancer therapy. Drugs. 2000 May;59(5):1043-55. [10852638 ]
  2. Belotti D, Paganoni P, Giavazzi R: MMP inhibitors: experimental and clinical studies. Int J Biol Markers. 1999 Oct-Dec;14(4):232-8. [10669951 ]
General function:
Involved in metalloendopeptidase activity
Specific function:
Can degrade fibrillar type I, II, and III collagens
Gene Name:
MMP8
Uniprot ID:
P22894
Molecular weight:
53411.7
References
  1. Heath EI, Grochow LB: Clinical potential of matrix metalloprotease inhibitors in cancer therapy. Drugs. 2000 May;59(5):1043-55. [10852638 ]
  2. Belotti D, Paganoni P, Giavazzi R: MMP inhibitors: experimental and clinical studies. Int J Biol Markers. 1999 Oct-Dec;14(4):232-8. [10669951 ]