Page last updated: 2024-11-12

1-amino-3-phenylpropylphosphonic acid

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Description

1-amino-3-phenylpropylphosphonic acid: inhibits L-phenylalanine ammonia-lyase activity of higher plants [Medical Subject Headings (MeSH), National Library of Medicine, extracted Dec-2023]

Cross-References

ID SourceID
PubMed CID11127644
CHEMBL ID1090914
SCHEMBL ID6518228
MeSH IDM0238669

Synonyms (10)

Synonym
CHEMBL1090914 ,
1-amino-3-phenylpropylphosphonic acid
bdbm50316049
phosphonic acid, (1-amino-3-phenylpropyl)-
89537-16-6
SCHEMBL6518228
(1-amino-3-phenylpropyl)phosphonic acid
DTXSID20456207
1(rs)-amino-3-phenylpropanephosphonic acid
PD127695
[information is derived through text-mining from research data collected from National Library of Medicine (NLM), extracted Dec-2023]

Protein Targets (5)

Inhibition Measurements

ProteinTaxonomyMeasurementAverageMin (ref.)Avg (ref.)Max (ref.)Bioassay(s)
Aminopeptidase NHomo sapiens (human)Ki0.00080.00081.956910.0000AID1162777
Aminopeptidase NSus scrofa (pig)IC50 (µMol)46.00000.00053.53548.9000AID472434
Aminopeptidase NSus scrofa (pig)Ki7.95200.00052.29697.8000AID1162778; AID573056
Cytosol aminopeptidaseSus scrofa (pig)Ki0.00460.00020.00220.0046AID1162779
Endoplasmic reticulum aminopeptidase 1Homo sapiens (human)Ki26.90005.08005.08005.0800AID1314018
[prepared from compound, protein, and bioassay information from National Library of Medicine (NLM), extracted Dec-2023]

Biological Processes (14)

Processvia Protein(s)Taxonomy
angiogenesisAminopeptidase NHomo sapiens (human)
cell differentiationAminopeptidase NHomo sapiens (human)
symbiont entry into host cellAminopeptidase NHomo sapiens (human)
proteolysisAminopeptidase NHomo sapiens (human)
peptide catabolic processAminopeptidase NHomo sapiens (human)
adaptive immune responseEndoplasmic reticulum aminopeptidase 2Homo sapiens (human)
antigen processing and presentation of peptide antigen via MHC class IEndoplasmic reticulum aminopeptidase 2Homo sapiens (human)
regulation of blood pressureEndoplasmic reticulum aminopeptidase 2Homo sapiens (human)
antigen processing and presentation of endogenous peptide antigen via MHC class IEndoplasmic reticulum aminopeptidase 2Homo sapiens (human)
peptide catabolic processEndoplasmic reticulum aminopeptidase 2Homo sapiens (human)
proteolysisEndoplasmic reticulum aminopeptidase 2Homo sapiens (human)
angiogenesisEndoplasmic reticulum aminopeptidase 1Homo sapiens (human)
adaptive immune responseEndoplasmic reticulum aminopeptidase 1Homo sapiens (human)
antigen processing and presentation of peptide antigen via MHC class IEndoplasmic reticulum aminopeptidase 1Homo sapiens (human)
membrane protein ectodomain proteolysisEndoplasmic reticulum aminopeptidase 1Homo sapiens (human)
regulation of blood pressureEndoplasmic reticulum aminopeptidase 1Homo sapiens (human)
response to bacteriumEndoplasmic reticulum aminopeptidase 1Homo sapiens (human)
antigen processing and presentation of endogenous peptide antigen via MHC class IEndoplasmic reticulum aminopeptidase 1Homo sapiens (human)
regulation of innate immune responseEndoplasmic reticulum aminopeptidase 1Homo sapiens (human)
fat cell differentiationEndoplasmic reticulum aminopeptidase 1Homo sapiens (human)
positive regulation of angiogenesisEndoplasmic reticulum aminopeptidase 1Homo sapiens (human)
peptide catabolic processEndoplasmic reticulum aminopeptidase 1Homo sapiens (human)
proteolysisEndoplasmic reticulum aminopeptidase 1Homo sapiens (human)
[Information is prepared from geneontology information from the June-17-2024 release]

Molecular Functions (12)

Processvia Protein(s)Taxonomy
virus receptor activityAminopeptidase NHomo sapiens (human)
aminopeptidase activityAminopeptidase NHomo sapiens (human)
metallopeptidase activityAminopeptidase NHomo sapiens (human)
signaling receptor activityAminopeptidase NHomo sapiens (human)
metalloaminopeptidase activityAminopeptidase NHomo sapiens (human)
zinc ion bindingAminopeptidase NHomo sapiens (human)
peptide bindingAminopeptidase NHomo sapiens (human)
endopeptidase activityEndoplasmic reticulum aminopeptidase 2Homo sapiens (human)
aminopeptidase activityEndoplasmic reticulum aminopeptidase 2Homo sapiens (human)
protein bindingEndoplasmic reticulum aminopeptidase 2Homo sapiens (human)
metallopeptidase activityEndoplasmic reticulum aminopeptidase 2Homo sapiens (human)
zinc ion bindingEndoplasmic reticulum aminopeptidase 2Homo sapiens (human)
metalloaminopeptidase activityEndoplasmic reticulum aminopeptidase 2Homo sapiens (human)
peptide bindingEndoplasmic reticulum aminopeptidase 2Homo sapiens (human)
endopeptidase activityEndoplasmic reticulum aminopeptidase 1Homo sapiens (human)
aminopeptidase activityEndoplasmic reticulum aminopeptidase 1Homo sapiens (human)
interleukin-6 receptor bindingEndoplasmic reticulum aminopeptidase 1Homo sapiens (human)
interleukin-1, type II receptor bindingEndoplasmic reticulum aminopeptidase 1Homo sapiens (human)
protein bindingEndoplasmic reticulum aminopeptidase 1Homo sapiens (human)
metalloexopeptidase activityEndoplasmic reticulum aminopeptidase 1Homo sapiens (human)
zinc ion bindingEndoplasmic reticulum aminopeptidase 1Homo sapiens (human)
peptide bindingEndoplasmic reticulum aminopeptidase 1Homo sapiens (human)
metalloaminopeptidase activityEndoplasmic reticulum aminopeptidase 1Homo sapiens (human)
[Information is prepared from geneontology information from the June-17-2024 release]

Ceullar Components (14)

Processvia Protein(s)Taxonomy
extracellular spaceAminopeptidase NHomo sapiens (human)
lysosomal membraneAminopeptidase NHomo sapiens (human)
endoplasmic reticulum-Golgi intermediate compartmentAminopeptidase NHomo sapiens (human)
plasma membraneAminopeptidase NHomo sapiens (human)
external side of plasma membraneAminopeptidase NHomo sapiens (human)
secretory granule membraneAminopeptidase NHomo sapiens (human)
extracellular exosomeAminopeptidase NHomo sapiens (human)
cytoplasmAminopeptidase NHomo sapiens (human)
plasma membraneAminopeptidase NHomo sapiens (human)
extracellular spaceAminopeptidase NHomo sapiens (human)
endoplasmic reticulum lumenEndoplasmic reticulum aminopeptidase 2Homo sapiens (human)
endoplasmic reticulum membraneEndoplasmic reticulum aminopeptidase 2Homo sapiens (human)
extracellular spaceEndoplasmic reticulum aminopeptidase 2Homo sapiens (human)
membraneEndoplasmic reticulum aminopeptidase 2Homo sapiens (human)
cytoplasmEndoplasmic reticulum aminopeptidase 2Homo sapiens (human)
extracellular regionEndoplasmic reticulum aminopeptidase 1Homo sapiens (human)
extracellular spaceEndoplasmic reticulum aminopeptidase 1Homo sapiens (human)
endoplasmic reticulumEndoplasmic reticulum aminopeptidase 1Homo sapiens (human)
endoplasmic reticulum lumenEndoplasmic reticulum aminopeptidase 1Homo sapiens (human)
endoplasmic reticulum membraneEndoplasmic reticulum aminopeptidase 1Homo sapiens (human)
cytosolEndoplasmic reticulum aminopeptidase 1Homo sapiens (human)
membraneEndoplasmic reticulum aminopeptidase 1Homo sapiens (human)
extracellular exosomeEndoplasmic reticulum aminopeptidase 1Homo sapiens (human)
extracellular spaceEndoplasmic reticulum aminopeptidase 1Homo sapiens (human)
cytoplasmEndoplasmic reticulum aminopeptidase 1Homo sapiens (human)
membraneEndoplasmic reticulum aminopeptidase 1Homo sapiens (human)
[Information is prepared from geneontology information from the June-17-2024 release]

Bioassays (17)

Assay IDTitleYearJournalArticle
AID1162777Inhibition of human recombinant alanyl aminopeptidase after 30 to 60 mins by morrison's equation2014Journal of medicinal chemistry, Oct-09, Volume: 57, Issue:19
Structure-guided, single-point modifications in the phosphinic dipeptide structure yield highly potent and selective inhibitors of neutral aminopeptidases.
AID1314018Inhibition of human ERAP1 preincubated for 30 to 60 mins followed by addition of Leu-AMC as substrate measured for 15 mins by spectrofluorimetric method2016Bioorganic & medicinal chemistry letters, 08-15, Volume: 26, Issue:16
Discovery of potent and selective inhibitors of human aminopeptidases ERAP1 and ERAP2 by screening libraries of phosphorus-containing amino acid and dipeptide analogues.
AID573045Antimalarial activity against Plasmodium falciparum 3D7 infected in O-positive human erythrocytes after 72 hrs2008Antimicrobial agents and chemotherapy, Sep, Volume: 52, Issue:9
Chemical target validation studies of aminopeptidase in malaria parasites using alpha-aminoalkylphosphonate and phosphonopeptide inhibitors.
AID1162776Inhibition of Neisseria meningitidis recombinant alanyl aminopeptidase after 30 to 60 mins by morrison's equation2014Journal of medicinal chemistry, Oct-09, Volume: 57, Issue:19
Structure-guided, single-point modifications in the phosphinic dipeptide structure yield highly potent and selective inhibitors of neutral aminopeptidases.
AID573051Inhibition of leucyl aminopeptidase activity in Plasmodium falciparum 3D7 at 10 uM using Leu-AMC as a substrate by spectrophotometer in presence of 1 nM CoCl22008Antimicrobial agents and chemotherapy, Sep, Volume: 52, Issue:9
Chemical target validation studies of aminopeptidase in malaria parasites using alpha-aminoalkylphosphonate and phosphonopeptide inhibitors.
AID573047Inhibition of leucyl aminopeptidase activity in Plasmodium falciparum 3D7 at 10 uM using Leu-AMC as a substrate by spectrophotometer2008Antimicrobial agents and chemotherapy, Sep, Volume: 52, Issue:9
Chemical target validation studies of aminopeptidase in malaria parasites using alpha-aminoalkylphosphonate and phosphonopeptide inhibitors.
AID472434Inhibition of pig kidney aminopeptidase N using Leu-AMC as substrate2010Bioorganic & medicinal chemistry, Apr-15, Volume: 18, Issue:8
New aromatic monoesters of alpha-aminoaralkylphosphonic acids as inhibitors of aminopeptidase N/CD13.
AID1162778Inhibition of pig recombinant alanyl aminopeptidase after 30 to 60 mins by morrison's equation2014Journal of medicinal chemistry, Oct-09, Volume: 57, Issue:19
Structure-guided, single-point modifications in the phosphinic dipeptide structure yield highly potent and selective inhibitors of neutral aminopeptidases.
AID573054Inhibition of leucyl aminopeptidase activity in Plasmodium falciparum 3D7 harboring tPfAP-M17 gene at 0.1 uM using Leu-AMC as a substrate by spectrophotometer in presence of 1 nM CoCl22008Antimicrobial agents and chemotherapy, Sep, Volume: 52, Issue:9
Chemical target validation studies of aminopeptidase in malaria parasites using alpha-aminoalkylphosphonate and phosphonopeptide inhibitors.
AID573055Inhibition of porcine kidney leucyl aminopeptidase2008Antimicrobial agents and chemotherapy, Sep, Volume: 52, Issue:9
Chemical target validation studies of aminopeptidase in malaria parasites using alpha-aminoalkylphosphonate and phosphonopeptide inhibitors.
AID573056Inhibition of pig kidney microsomal aminopeptidase N2008Antimicrobial agents and chemotherapy, Sep, Volume: 52, Issue:9
Chemical target validation studies of aminopeptidase in malaria parasites using alpha-aminoalkylphosphonate and phosphonopeptide inhibitors.
AID573049Inhibition of alanyl aminopeptidase activity in Plasmodium falciparum 3D7 at 10 uM using Ala-AMC as a substrate by spectrophotometer2008Antimicrobial agents and chemotherapy, Sep, Volume: 52, Issue:9
Chemical target validation studies of aminopeptidase in malaria parasites using alpha-aminoalkylphosphonate and phosphonopeptide inhibitors.
AID573048Inhibition of leucyl aminopeptidase activity in Plasmodium falciparum 3D7 at 0.1 uM using Leu-AMC as a substrate by spectrophotometer2008Antimicrobial agents and chemotherapy, Sep, Volume: 52, Issue:9
Chemical target validation studies of aminopeptidase in malaria parasites using alpha-aminoalkylphosphonate and phosphonopeptide inhibitors.
AID1314019Inhibition of human ERAP2 preincubated for 30 to 60 mins followed by addition of Arg-AMC as substrate measured for 15 mins by spectrofluorimetric method2016Bioorganic & medicinal chemistry letters, 08-15, Volume: 26, Issue:16
Discovery of potent and selective inhibitors of human aminopeptidases ERAP1 and ERAP2 by screening libraries of phosphorus-containing amino acid and dipeptide analogues.
AID573052Inhibition of leucyl aminopeptidase activity in Plasmodium falciparum 3D7 at 0.1 uM using Leu-AMC as a substrate by spectrophotometer in presence of 1 nM CoCl22008Antimicrobial agents and chemotherapy, Sep, Volume: 52, Issue:9
Chemical target validation studies of aminopeptidase in malaria parasites using alpha-aminoalkylphosphonate and phosphonopeptide inhibitors.
AID1162779Inhibition of pig recombinant leucine aminopeptidase after 30 to 60 mins by morrison's equation2014Journal of medicinal chemistry, Oct-09, Volume: 57, Issue:19
Structure-guided, single-point modifications in the phosphinic dipeptide structure yield highly potent and selective inhibitors of neutral aminopeptidases.
AID573050Inhibition of alanyl aminopeptidase activity in Plasmodium falciparum 3D7 at 0.1 uM using Ala-AMC as a substrate by spectrophotometer2008Antimicrobial agents and chemotherapy, Sep, Volume: 52, Issue:9
Chemical target validation studies of aminopeptidase in malaria parasites using alpha-aminoalkylphosphonate and phosphonopeptide inhibitors.
[information is prepared from bioassay data collected from National Library of Medicine (NLM), extracted Dec-2023]

Research

Studies (5)

TimeframeStudies, This Drug (%)All Drugs %
pre-19900 (0.00)18.7374
1990's1 (20.00)18.2507
2000's1 (20.00)29.6817
2010's3 (60.00)24.3611
2020's0 (0.00)2.80
[information is prepared from research data collected from National Library of Medicine (NLM), extracted Dec-2023]

Market Indicators

Research Demand Index: 12.87

According to the monthly volume, diversity, and competition of internet searches for this compound, as well the volume and growth of publications, there is estimated to be weak demand-to-supply ratio for research on this compound.

MetricThis Compound (vs All)
Research Demand Index12.87 (24.57)
Research Supply Index1.79 (2.92)
Research Growth Index4.66 (4.65)
Search Engine Demand Index0.00 (26.88)
Search Engine Supply Index0.00 (0.95)

This Compound (12.87)

All Compounds (24.57)

Study Types

Publication TypeThis drug (%)All Drugs (%)
Trials0 (0.00%)5.53%
Reviews0 (0.00%)6.00%
Case Studies0 (0.00%)4.05%
Observational0 (0.00%)0.25%
Other5 (100.00%)84.16%
[information is prepared from research data collected from National Library of Medicine (NLM), extracted Dec-2023]