Page last updated: 2024-08-07 15:49:15

Matrilysin

A matrilysin that is encoded in the genome of human. [PRO:DNx, UniProtKB:P09237]

Synonyms

EC 3.4.24.23;
Matrin;
Matrix metalloproteinase-7;
MMP-7;
Pump-1 protease;
Uterine metalloproteinase

Research

Bioassay Publications (33)

TimeframeStudies on this Protein(%)All Drugs %
pre-19900 (0.00)18.7374
1990's3 (9.09)18.2507
2000's18 (54.55)29.6817
2010's8 (24.24)24.3611
2020's4 (12.12)2.80

Compounds (35)

Drugs with Inhibition Measurements

DrugTaxonomyMeasurementAverage (mM)Bioassay(s)Publication(s)
2,3-dihydroxybenzoic acidHomo sapiens (human)IC50200.000011
protocatechuic acidHomo sapiens (human)IC50137.000011
gallic acidHomo sapiens (human)IC5065.008617
beta-resorcylic acidHomo sapiens (human)IC50200.000011
2,5-dihydroxybenzoic acidHomo sapiens (human)IC50115.000011
veratric acidHomo sapiens (human)IC50200.000011
methyl gallateHomo sapiens (human)IC5026.500012
3,4,5-trimethoxybenzoic acidHomo sapiens (human)IC50200.000011
syringic acidHomo sapiens (human)IC50200.000011
epigallocatechin gallateHomo sapiens (human)IC509.314327
marimastatHomo sapiens (human)IC502.009055
n-(2-isobutyl-3-(n'-hydroxycarbonylamido)propanoyl)-o-methyltyrosinemethylamideHomo sapiens (human)IC500.030011
ilomastatHomo sapiens (human)IC500.019022
bb3497Homo sapiens (human)IC50100.000011
3-((benzyl)(methylaminocarbonyl)methylaminocarbonyl)n-hydroxy-5-methylhexanamideHomo sapiens (human)IC500.008311
prinomastatHomo sapiens (human)IC500.072333
prinomastatHomo sapiens (human)Ki0.054011
isoliquiritigeninHomo sapiens (human)IC500.008011
rs-130830Homo sapiens (human)IC500.932544
rs-130830Homo sapiens (human)Ki1.200011
tmi-1Homo sapiens (human)IC500.013016
batimastatHomo sapiens (human)IC503.501222
ik 682Homo sapiens (human)Ki0.259033
epigallocatechin-3-o-(3''-o-methyl)-gallateHomo sapiens (human)IC5020.000011
ro 32-3555Homo sapiens (human)IC500.018511
abt-770Homo sapiens (human)IC5010.000033
sb 3ct compoundHomo sapiens (human)Ki88.750044
pd 166793Homo sapiens (human)IC507.200011
sc 78080Homo sapiens (human)IC507.000011
sc 78080Homo sapiens (human)Ki7.000011
arp-100Homo sapiens (human)IC5050.000033
s 3304Homo sapiens (human)IC501.000011
N(2)-([biphenyl]-4-ylsulfonyl)-N-hydroxy-N(2)-isopropoxy-D-valinamideHomo sapiens (human)IC506.055512
bms-566394Homo sapiens (human)IC504.000712
bms-566394Homo sapiens (human)Ki10.000022
incb3619Homo sapiens (human)IC505.000011
grassystatin aHomo sapiens (human)IC505.000011
minocyclineHomo sapiens (human)IC50125.000011
guanosine diphosphateHomo sapiens (human)IC50125.260015

Enables

This protein enables 6 target(s):

TargetCategoryDefinition
endopeptidase activitymolecular functionCatalysis of the hydrolysis of internal, alpha-peptide bonds in a polypeptide chain. [http://merops.sanger.ac.uk/about/glossary.htm#ENDOPEPTIDASE]
metalloendopeptidase activitymolecular functionCatalysis of the hydrolysis of internal, alpha-peptide bonds in a polypeptide chain by a mechanism in which water acts as a nucleophile, one or two metal ions hold the water molecule in place, and charged amino acid side chains are ligands for the metal ions. [GOC:mah, https://www.ebi.ac.uk/merops/about/glossary.shtml#CATTYPE, https://www.ebi.ac.uk/merops/about/glossary.shtml#ENDOPEPTIDASE]
serine-type endopeptidase activitymolecular functionCatalysis of the hydrolysis of internal, alpha-peptide bonds in a polypeptide chain by a catalytic mechanism that involves a catalytic triad consisting of a serine nucleophile that is activated by a proton relay involving an acidic residue (e.g. aspartate or glutamate) and a basic residue (usually histidine). [GOC:mah, https://www.ebi.ac.uk/merops/about/glossary.shtml#CATTYPE]
protein bindingmolecular functionBinding to a protein. [GOC:go_curators]
metallopeptidase activitymolecular functionCatalysis of the hydrolysis of peptide bonds by a mechanism in which water acts as a nucleophile, one or two metal ions hold the water molecule in place, and charged amino acid side chains are ligands for the metal ions. [GOC:mah, https://www.ebi.ac.uk/merops/about/glossary.shtml#CATTYPE]
zinc ion bindingmolecular functionBinding to a zinc ion (Zn). [GOC:ai]

Located In

This protein is located in 3 target(s):

TargetCategoryDefinition
extracellular regioncellular componentThe space external to the outermost structure of a cell. For cells without external protective or external encapsulating structures this refers to space outside of the plasma membrane. This term covers the host cell environment outside an intracellular parasite. [GOC:go_curators]
extracellular matrixcellular componentA structure lying external to one or more cells, which provides structural support, biochemical or biomechanical cues for cells or tissues. [GOC:BHF, GOC:mah, GOC:rph, NIF_Subcellular:nlx_subcell_20090513, PMID:21123617, PMID:28089324]
extracellular exosomecellular componentA vesicle that is released into the extracellular region by fusion of the limiting endosomal membrane of a multivesicular body with the plasma membrane. Extracellular exosomes, also simply called exosomes, have a diameter of about 40-100 nm. [GOC:BHF, GOC:mah, GOC:vesicles, PMID:15908444, PMID:17641064, PMID:19442504, PMID:19498381, PMID:22418571, PMID:24009894]

Active In

This protein is active in 1 target(s):

TargetCategoryDefinition
extracellular spacecellular componentThat part of a multicellular organism outside the cells proper, usually taken to be outside the plasma membranes, and occupied by fluid. [ISBN:0198547684]

Involved In

This protein is involved in 11 target(s):

TargetCategoryDefinition
antibacterial peptide secretionbiological processThe regulated release of an antibacterial peptide from a cell or a tissue. [GOC:add, ISBN:0781735149, PMID:11807545, PMID:15638771]
antibacterial peptide biosynthetic processbiological processThe chemical reactions and pathways resulting in the formation of an antibacterial peptide. [GOC:add, ISBN:0781735149, PMID:11807545, PMID:15638771]
proteolysisbiological processThe hydrolysis of proteins into smaller polypeptides and/or amino acids by cleavage of their peptide bonds. [GOC:bf, GOC:mah]
response to xenobiotic stimulusbiological processAny process that results in a change in state or activity of a cell or an organism (in terms of movement, secretion, enzyme production, gene expression, etc.) as a result of a stimulus from a xenobiotic, a compound foreign to the organim exposed to it. It may be synthesized by another organism (like ampicilin) or it can be a synthetic chemical. [GOC:jl, GOC:krc]
extracellular matrix disassemblybiological processA process that results in the breakdown of the extracellular matrix. [GOC:jid]
positive regulation of cell migrationbiological processAny process that activates or increases the frequency, rate or extent of cell migration. [GOC:go_curators]
collagen catabolic processbiological processThe proteolytic chemical reactions and pathways resulting in the breakdown of collagen in the extracellular matrix, usually carried out by proteases secreted by nearby cells. [GOC:mah, ISBN:0815316194]
regulation of cell population proliferationbiological processAny process that modulates the frequency, rate or extent of cell proliferation. [GOC:jl]
defense response to Gram-negative bacteriumbiological processReactions triggered in response to the presence of a Gram-negative bacterium that act to protect the cell or organism. [GOC:ai]
defense response to Gram-positive bacteriumbiological processReactions triggered in response to the presence of a Gram-positive bacterium that act to protect the cell or organism. [GOC:ai]
extracellular matrix organizationbiological processA process that is carried out at the cellular level which results in the assembly, arrangement of constituent parts, or disassembly of an extracellular matrix. [GOC:mah]