3.4.24.18: meprin A
This is an abbreviated version!
For detailed information about meprin A, go to the full flat file.
Word Map on EC 3.4.24.18
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3.4.24.18
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3.4.24.11
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enkephalinase
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metalloendopeptidase
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atrial
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phosphoramidon
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natriuretic
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enkephalin
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thiorphan
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angiotensin-converting
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angiotensin
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astacins
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metalloproteases
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brush
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bradykinin
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3.4.15.1
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captopril
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neprilysin
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metallopeptidases
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anp
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aminopeptidases
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acetorphan
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math
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endopeptidases
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brush-border
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microvillar
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actinonin
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calla
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bestatin
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amastatin
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azocasein
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phosphoramidon-sensitive
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sheddase
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dipeptidylaminopeptidase
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metzincins
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pharmacology
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neurokinins
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astacin-like
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met5enkephalin
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depressor
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medicine
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tachykinins
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neurotensin
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leu-enkephalin
- 3.4.24.18
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3.4.24.11
- enkephalinase
- metalloendopeptidase
- atrial
- phosphoramidon
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natriuretic
- enkephalin
- thiorphan
-
angiotensin-converting
- angiotensin
- astacins
- metalloproteases
-
brush
- bradykinin
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3.4.15.1
- captopril
- neprilysin
- metallopeptidases
- anp
- aminopeptidases
- acetorphan
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math
- endopeptidases
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brush-border
- microvillar
- actinonin
- calla
- bestatin
- amastatin
- azocasein
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phosphoramidon-sensitive
- sheddase
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dipeptidylaminopeptidase
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metzincins
- pharmacology
- neurokinins
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astacin-like
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met5enkephalin
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depressor
- medicine
- tachykinins
- neurotensin
- leu-enkephalin
Reaction
Hydrolysis of protein and peptide substrates preferentially on carboxyl side of hydrophobic residues =
Synonyms
E-24.18, EC 3.4.24.11, Endopeptidase-2, M12.002, MEP1A, Meprin, meprin A, meprin A metalloprotease, meprin A metalloproteinase, meprin A subunit alpha, meprin alpha, meprin alpha1, meprin alpha2, meprin beta, meprin metalloprotease, meprin metalloproteinase, Meprin-a, meprin-alpha, metalloprotease meprin A, metalloproteinase meprin alpha, Mmepa, More, mouse meprin alpha, N-Benzoyl-L-tyrosyl-p-aminobenzoic acid hydrolase, PABA peptide hydrolase, PABA-peptide hydrolase, PPH, PPH alpha, PPH beta, procollagen proteinase, Rmepa
ECTree
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Inhibitors
Inhibitors on EC 3.4.24.18 - meprin A
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2-(N-Hydroxycarboxamido)-4-methylpentanoyl-L-alanyl-glycylamide
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i.e. Zinkov inhibitor
3-[(E)-[4-formyl-5-hydroxy-6-methyl-3-[(phosphonooxy)methyl]pyridin-2-yl]diazenyl]-7-nitronaphthalene-1,5-disulfonic acid
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competitive inhibition
N-[1-[(1-amino-1-oxopropan-2-yl)amino]-3-(naphthalen-1-yl)-1-oxopropan-2-yl]-4-(hydroxyamino)-2-(2-methylpropyl)pent-4-enamide
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N-[4-(hydroxyamino)-2-(2-methylpropyl)pent-4-enoyl]-3-methylvalyl-N-(2-aminoethyl)-DL-alaninamide
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N4-hydroxy-N1-[3-(1H-indol-3-yl)-1-(methylamino)-1-oxopropan-2-yl]-2-(2-methylpropyl)butanediamide
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verapamil
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verapamil at 1 mg/kg, i.v. can efficiently prevent the ischemic acute kidney injury in female rats, as well as male rats
actinonin
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a hydroxamate derivate and naturally occurring compound produced in actinomycetes. Hydroxamate inhibitors chelate the zinc ion in the active site
actinonin
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i.e. 3-[[1-[[2-(hydroxymethyl)-1-pyrolidinyl]carbonyl]-2-methylpropyl]carbamoyl]octano hydroxamic acid, strong, kinetics
actinonin
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in a mouse model of sepsis induced by cecal ligation puncture that results in elevated levels of serum interleukin 1beta, meprin inhibitor actinonin significantly reduces levels of serum interleukin 1beta
actinonin
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a hydroxamate derivate and naturally occurring compound produced in actinomycetes. Hydroxamate inhibitors chelate the zinc ion in the active site
actinonin
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pre-ischemic treatment with actinonin at 10 or 30 mg/kg, i.v. dose-ependently attenuates the ischemia/reperfusion-induced renal injury in male rats, but fails to improve the renal injury in female rats
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restored by divalent metal ions, Zn2+ being more effective than Ca2+ or Mg2+
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binding structure in S subsites, overview. A decrease in solvent accessibility values at specific residues upon inhibitor binding occurs. The S subsite of the enzyme interacts with residues at P site of the inhibitor
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amastatin, bestatin, puromycin, N-tosyl-L-Phe chloromethyl ketone, monoclonal antibody HBB 3/716/36; iodoacetate; leupeptin; no inhibition by phosphoramidon; PMSF, pepstatin
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additional information
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inhibitors of elastase, aminopeptidase, serine, aspartic or cysteic proteases; no inhibition by phosphoramidon
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additional information
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3,4-dichloroisocoumarin; iodoacetate; no inhibition by phosphoramidon; PMSF, pepstatin; soybean trypsin inhibitor
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additional information
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inhibitor screening, overview. Poor inhibition by NF449, a suramin analogue
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additional information
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binding sites and binding structure of hydroxamic acid derivative inhibitors, molecular dynamics simulation study, overview
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additional information
analysis of binding sites of human meprins, screening of inhibitors by molecular dynamics simulation study, molecular docking, overview
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additional information
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analysis of binding sites of human meprins, screening of inhibitors by molecular dynamics simulation study, molecular docking, overview
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additional information
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diisopropyl phosphofluoridate, p-hydroxymercuribenzoate, phenylmercurisulfonate, antipain, cystine, oxidized glutathione; iodoacetate; leupeptin; no inhibition by phosphoramidon; PMSF, pepstatin
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additional information
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iodoacetate; L-trans-epoxysuccinyl-leucylamido-(4-guanidino)-butane (i.e. E-64); no inhibition by phosphoramidon; soybean trypsin inhibitor
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additional information
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3,4-dichloroisocoumarin; iodoacetate; no inhibition by phosphoramidon; PMSF, pepstatin; soybean trypsin inhibitor
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additional information
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hippuryl-His-Leu, His-Leu, benzamidine; soybean trypsin inhibitor
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additional information
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leupeptin; L-trans-epoxysuccinyl-leucylamido-(4-guanidino)-butane (i.e. E-64); NEM, tissue inhibitor of metalloproteinases; no inhibition by phosphoramidon; PMSF, pepstatin; soybean trypsin inhibitor
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additional information
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3,4-dichloroisocoumarin; iodoacetate; no inhibition by phosphoramidon; PMSF, pepstatin; soybean trypsin inhibitor
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