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3.4.24.24: gelatinase A

This is an abbreviated version!
For detailed information about gelatinase A, go to the full flat file.

Word Map on EC 3.4.24.24

Reaction

Cleavage of gelatin type I and collagen types IV, V, VII, X. Cleaves the collagen-like sequence Pro-Gln-Gly-/-Ile-Ala-Gly-Gln =

Synonyms

72 kDa Gelatinase, 72 kDa Gelatinase type A, 72 kDa type IV collagenase, 72-kDa Gelatinase, Collagenase IV, Collagenase type IV, GelA, gelatinase, gelatinase A, human gelatinase A, human matrix metalloproteinase 2, human matrix metalloproteinase-2, LvMMP-2, matrix metallopeptidase 2, matrix metalloprotease 2, Matrix metalloproteinase 2, matrix metalloproteinase-2, matrix metalloprotenase-2, metalloproteinase-2, metrix metalloproteinase-2, MMP 2, MMP-2, MMP2, progelatinase, Type IV collagen metalloproteinase, Type IV collagenase, Type IV collagenase/gelatinase

ECTree

     3 Hydrolases
         3.4 Acting on peptide bonds (peptidases)
             3.4.24 Metalloendopeptidases
                3.4.24.24 gelatinase A

Inhibitors

Inhibitors on EC 3.4.24.24 - gelatinase A

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INHIBITOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
(2E)-3-(N-hydroxycarbamoyl)-2-(3-phenylpropylidene)propionyl-L-tryptophan-N-methylamide
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(2E)-3-(N-hydroxycarbamoyl)-2-heptylidenepropionyl-L-tryptophan-N-methylamide
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(2E)-3-(N-hydroxycarbamoyl)-2-isopropionyl-L-tryptophan-N-methylamide
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(2E)-3-(N-hydroxycarbamoyl)-2-[(2E)-3-phenylprop-2-en-1-ylidene]propionyl-L-tryptophan-N-methylamide
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(2E)-3-(N-hydroxycarbamoyl)-2-[(2E)-but-2-en-1-ylidene]propionyl-L-tryptophan-N-methylamide
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(2R)-2-[(4-biphenylylcarbonyl)amino]-N-hydroxy-3-(1H-indol-3-yl)propionamide
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(2R)-2-[(4-biphenylylsulfonyl)amino]-3-phenylpropionic acid
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(2R)-2-[(4-biphenylylsulfonyl)amino]-3-phenylpropionic acid benzyl ester
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(2R)-2-[[4-[benzenesulfonylhydrazonomethyl]benzenesulfonyl]-amino]-3-(1H-indol-3-yl)propionic acid methyl ester
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(2R)-2-[[4-[benzenesulfonylhydrazonomethyl]benzenesulfonyl]-amino]-3-methylbutanoic acid tert-butyl ester
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(2R)-2-[[5-(4-methoxyphenyl)thiophene-2-sulfonyl]-amino]-3-methylbutanoic acid
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(2R)-2-[[5-(4-methoxyphenyl)thiophene-2-sulfonyl]-amino]-3-methylbutanoic acid methyl ester
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(2R)-3-(1H-indol-3yl)-2-[[4-(phenylazo)benzenesulfonyl]amino]propionic acid
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(2R)-3-(1H-indol-3yl)-2-[[4-[phenylaminocarbonyl]-benzenesulfonyl]amino]propionic acid benzyl ester
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(2R)-3-methyl-2-[4-[phenoxybenzenesulfonyl]amino]butanoic acid
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(2R)-3-methyl-2-[[4-[(4-nitrobenzoyl)-amino]benzenesulfonyl]amino]butanoic acid
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(2R)-3-methyl-2-[[4-[(4-nitrobenzoyl)amino]benzenesulfonyl]amino]butanoic acid tert-butyl ester
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(2R)-3-methyl-2-[[4-[2-[4-methylmercaptophenyl]-2H-tetrazol-5-yl]benzenesulfonyl]-amino]butanoic acid
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(2R)-3-methyl-2-[[4-[2-[methylmercaptophenyl]-2H-tetrazol-5-yl]benzenesulfonyl]-amino]butanoic acid tert-butyl ester
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(2R)-3-methyl-2-[[5-[(4-methylphenyl)ethynyl]thiophene-2-sulfonyl]-amino]butanoic acid methyl ester
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(2R)-N-(benzyloxy)-2-[(4-biphenylsulfonyl)amino]-3-phenylpropionamide
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(2R)-N-hydroxy-3-methyl-2-[(4-phenoxybenzenesulfonyl)amino]butanamide
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(2R)-[(4-biphenylsulfonyl)amino]-N-hydroxy-3-phenylpropionamide
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(4-phenoxyphenylsulfonyl)methylthiirane
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selective inhibitor of MMP2
1,10-phenanthroline
1,4-dithiothreitol
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2-(4-(4-[(2-thiiranylpropyl)sulfonyl]phenoxy)phenyl)acetic acid
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selective inhibitor
2-([4-[3'-(2-aminoethoxy)-2-methylbiphenyl-4-yl]piperidin-1-yl]sulfonyl)-N-hydroxy-2-methylpropanamide
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2-[(4-biphenyl-4-yl-3,6-dihydropyridin-1(2H)-yl)sulfonyl]-N-hydroxyacetamide
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2-[(4-[3'-[2-(dimethylamino)ethoxy]-2-methylbiphenyl-4-yl]piperidin-1-yl)sulfonyl]-N-hydroxy-2-methylpropanamide
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2-[(biphenyl-4-ylsulfonyl)(isobutyl)amino]-N-hydroxyacetamide
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50% inhibition at 13 nM, comparison with inhibitory effect on matrix metalloproteinases MMP-3, MMp-7, MMP-9
2-[(biphenyl-4-ylsulfonyl)(isopropoxy)amino]-N-hydroxyacetamide
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50% inhibition at 12 nM, comparison with inhibitory effect on matrix metalloproteinases MMP-3, MMp-7, MMP-9
2-[[4-(2,3'-dimethylbiphenyl-4-yl)-3,6-dihydropyridin-1(2H)-yl]sulfonyl]-N-hydroxyacetamide
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2-[[4-(2-chlorobiphenyl-4-yl)-3,6-dihydropyridin-1(2H)-yl]sulfonyl]-N-hydroxyacetamide
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2-[[4-(2-ethylbiphenyl-4-yl)-3,6-dihydropyridin-1(2H)-yl]sulfonyl]-N-hydroxyacetamide
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2-[[4-(2-fluorobiphenyl-4-yl)-3,6-dihydropyridin-1(2H)-yl]sulfonyl]-N-hydroxyacetamide
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2-[[4-(3'-ethoxy-2-methylbiphenyl-4-yl)-3,6-dihydropyridin-1(2H)-yl]sulfonyl]-N-hydroxyacetamide
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2-[[4-(3'-ethoxy-2-methylbiphenyl-4-yl)piperidin-1-yl]sulfonyl]-N-hydroxy-2-methylpropanamide
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2-[[4-(3'-ethyl-2-methylbiphenyl-4-yl)-3,6-dihydropyridin-1(2H)-yl]sulfonyl]-N-hydroxyacetamide
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4-(2-phenyl-2H-tetrazol-5-yl)benzenesulfonyl chloride
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4-(3-phenylureido) benzenesulfonyl chloride
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4-(4-phenoxphenylsulfonyl)butane-1,2-dithiol
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4-Aminobenzoyl-Gly-Pro-D-Leu-D-Ala-NHOH
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5-(4-phenoxphenylsulfonyl)pentane-1,2-dithiol
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advanced glycation products
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inhibit the enzyme mediated through upregulation of the advanced glycation product receptor, overview
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Ag-3340
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i.e. N-hydroxy-2,2-dimethyl-4-[(4-phenoxyphenyl)sulfonyl]thiomorpholine-3-carboxamide, 50% inhibition at 0.083 nM, comparison with inhibitory effect on matrix metalloproteinases MMP-3, MMp-7, MMP-9
alpha-linolenic acid
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alpha2 macroglobulin
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alpha2-Macroglobulin
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APP-IP-TIMP-2
inhibition evaluation and kinetics, mechanism in concanavalin A-stimulated HT1080 fibrosarcoma cells, expression of APP-IP-TIMP-2 in HT1080 cells, overview. The ten amino acid residue sequence of APP-derived MMP-2 selective inhibitory peptide (APP-IP) is added to the N-terminus of tissue inhibitors of metalloproteinase 2, TIMP-2. The APP-IP and TIMP-2 regions of the fusion protein are designed to interact with the active site and the hemopexin-like domain of MMP-2, respectively.The reactive site of the TIMP-2 region, which has broad specificity against MMPs, is blocked by the APP-IP adduct. The recombinant APP-IP-TIMP-2 shows strong inhibitory activity toward MMP-2 whereas its inhibitory activity toward MMP-1, MMP-3, MMP-7, MMP-8, MMP-9, or MT1--MMP is six orders of magnitude or more weaker. Compared with the decapeptide APP-IP, APP-IP-TIMP-2 shows a much longer half-life in cultured tumor cells
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ascorbic acid
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batimastat
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i.e. BB-94, a peptidomimetic inhibitor
benzyloxycarbonyl-L-Trp-OH
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beta-amyloid precursor protein
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APP
CGS27023A
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50% inhibition at 20 nM, comparison with inhibitory effect on matrix metalloproteinases MMP-3, MMp-7, MMP-9
chitooligosaccharides
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inhibit MMP-2 enzyme expression, decrease of the gene expression and transcriptional activity of MMP-2, and catalytic activity in primary dermal fibroblasts, chitooligosaccharides of 3-5 kDa are most effective
curcumin
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treatment of whole cell, significant inhibition of enzyme activity after 15 days with concomitant decrease in expression of membrane type-1 matrix metalloproteinase and focal adhesion kinase to almost background level
D-tryptophan benzyl ester trifluoroacetate
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D-tryptophan methyl ester tosylate
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dibenzofuran-2-sulfonyl chloride
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dimethyl sulfoxide
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presence of 2% dimethyl sulfoxide disrupts interactions of enzyme with substrate and thereby reduces activity by 70%
docosahexaenoic acid
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endostatin
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extracellular domain of beta-amyloid peptide
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the extracellular domain of beta-amyloid precursor protein contains an inhibitor against MMP-2, the inhibitor is localized within the ISYGNDALMP sequence of APP, overview
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galardin
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gamma-linolenic acid
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glycine
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GNDAMPL
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APP-IP delta N3
ilomastat
isovitexin
interacts with enzyme residues Glu121, Leu83, Ala84, Pro140, Ile141, His120, Ala136, Leu116, Ala139, and Leu137, binding structure analysis, and modelling, overview
ISYGADALMP
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APP-IP delta N/A
ISYGNAALMP
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APP-IP delta D/A
ISYGNDAAMP
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APP-IP delta L/A
ISYGNDAL
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APP-IP delta C2
ISYGNDALM
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APP-IP delta C1
ISYGNDALMP
ISYGNDALMPSL
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APP586-597
ISYGNDALMPSLTETK
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APP586-601
L-ascorbic acid
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L-cysteine
L-histidine
L-homocysteine
L-methionine
linoleic acid
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methyl 2-(4-(4-[(2-thiiranylpropyl)-sulfonyl]phenoxy)phenyl)acetate
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mechanism-based inhibitor, selective for enzyme
N-(R)-(2-(hydroxyaminocarbonyl)methyl)-4-methylpentanoyl-L-naphthylalanyl-L-alanine-2-aminoethyl amide
TAPI-1
N-acetylcysteine
N-hydroxy-2-(isobutyl[(4-methoxyphenyl)sulfonyl]amino)acetamide
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50% inhibition at 6.9 nM, comparison with inhibitory effect on matrix metalloproteinases MMP-3, MMp-7, MMP-9
N-hydroxy-2-([4-[2-(trifluoromethyl)biphenyl-4-yl]-3,6-dihydropyridin-1(2H)-yl]sulfonyl)acetamide
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N-hydroxy-2-([4-[2-methyl-3'-(trifluoromethoxy)biphenyl-4-yl]-3,6-dihydropyridin-1(2H)-yl]sulfonyl)acetamide
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N-hydroxy-2-([4-[3'-(2-hydroxyethoxy)-2-methylbiphenyl-4-yl]piperidin-1-yl]sulfonyl)-2-methylpropanamide
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N-hydroxy-2-([4-[3'-(2-methoxyethoxy)-2-methylbiphenyl-4-yl]piperidin-1-yl]sulfonyl)-2-methylpropanamide
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N-hydroxy-2-([4-[3'-(methoxymethyl)-2-methylbiphenyl-4-yl]-3,6-dihydropyridin-1(2H)-yl]sulfonyl)acetamide
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N-hydroxy-2-methyl-2-[(4-[2-methyl-3'-[2-(methylamino)ethoxy]biphenyl-4-yl]piperidin-1-yl)sulfonyl]propanamide
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N-hydroxy-2-[(4-[4-[6-(2-hydroxyethoxy)pyridin-2-yl]-3-methylphenyl]piperidin-1-yl)sulfonyl]-2-methylpropanamide
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N-hydroxy-2-[[4-(2-methylbiphenyl-4-yl)-3,6-dihydropyridin-1(2H)-yl]sulfonyl]acetamide
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N-hydroxy-2-[[4-(3'-methoxy-2-methylbiphenyl-4-yl)-3,6-dihydropyridin-1(2H)-yl]sulfonyl]acetamide
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N-isobutyl-N-(4-methoxyphenylsulfonyl)glycyl hydroxamic acid
NNGH
NaCl
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binding to heparin and fibronectin can be disrupted by 0.3 M NaCl
oleic acid
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peptide P713
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inhibits the binding of the CBD as well as MMP-2E404A to gelatin, no inhibition of MMP-2 lacking thr CBD domain, competitively, P713 inhibits MMP-2 activities by blocking substrate access to the CBD exodomain, mechanism, overview
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procollagen C-terminal proteinase enhancer
PCPE
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procyanidin oligomers
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from Japanese quince, Chaenomeles japonica, fruit inhibit activity of MMP-2
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RECK
reversion-inducing cysteine-rich protein with Kazal motifs
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SB-3CT
mechanism-based synthetic inhibitor
SC-74020
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hydroxamic acid inhibitor
Stromelysin catalytic domain inhibitors
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gelatinase A synthetic 19000 MW catalytic domain
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SYGNDAMPL
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APP-IP delta N1
ter-butyloxycarbonyl-L-Trp-OH
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TIMP
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TIMP-1
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TIMP-2
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TIMP-3
binding also involves interaction between TIMP and the MMP-2 Hpx-like domain
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TIMP-4
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tissue factor pathway inhibitor
TFPI-2
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Tissue inhibitor of metalloproteinase-1
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Tissue inhibitor of metalloproteinase-2
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Tissue inhibitor of metalloproteinases
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tissue inhibitor of metalloproteinases-2
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tissue inhibitors of metalloproteinase 2
TIMP2
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UK-370106
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vitexin
interacts with enzyme residues Leu83, Ala84, His130, Pro140, Ala139, Met138, Ala, 136, Leu137, Thr143, Tyr142, Val117, His120, and Ile141, binding structure analysis, and modelling, overview
YGNDAMPL
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APP-IP delta N2
Zn2+
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required, synthetic 19000 MW catalytic domain, inhibition at high concentration
additional information
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