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
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angiotensin-converting
- angiotensin
- astacins
- metalloproteases
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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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Natural Substrates Products
Natural Substrates Products on EC 3.4.24.18 - meprin A
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REACTION DIAGRAM
fibrillar procollagen type I + H2O
fibrillar collagen type I + fibrillar collagen type I propeptide
fibrillar procollagen type III + H2O
fibrillar collagen type III + fibrillar collagen type I propeptide
procollagen I + H2O
collagen I + propeptide of collagen III
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meprin alpha removes both the C- and N-propeptides of type I procollagen, subsequently releasing fibril-forming mature collagen molecules. The C-terminal cleavage sites in the proalpha1(I) chain generated by the enzyme is identified as Ala1218/Asp1219, identical to the BMP-1 cleavage site, and also Arg1227/Asp1228, nine residues C-terminal to the BMP-1 cleavage site
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protein kinase A + H2O
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the enzyme cleaves at defined sites, isoform-specific interactions between the catalytic subunit of PKA (PKA C) and meprins, overview
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Reelin + H2O
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Reelin is a secreted glycoprotein whose function is regulated by proteolysis
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tissue growth factor-alpha + H2O
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meprin alpha can process tissue growth factor-alpha
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fibrillar collagen type I + fibrillar collagen type I propeptide
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the enzyme is capable of cleaving off the globular C- and N-terminal prodomains of fibrillar collagen type I and type III. Cleavage sites are at positions YYRA1218-/-1219DDAN and VRDR1227/-1228DLEV for the alpha1(I) chain, and additionally GGGY1108-/-1109DFGY for alpha2(I). For the N-terminal propeptide SYGY166-/-167DEKS (alpha1(I)) and AAQY81-/-82DGKG (alpha2(I)) are identified as meprin cleavage sites
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fibrillar procollagen type I + H2O
fibrillar collagen type I + fibrillar collagen type I propeptide
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the enzyme is capable of cleaving off the globular C- and N-terminal prodomains of fibrillar collagen type I and type III. Cleavage sites are at positions YYRA1218-/-1219DDAN and VRDR1227/-1228DLEV for the alpha1(I) chain, and additionally GGGY1108-/-1109DFGY for alpha2(I). For the N-terminal propeptide SYGY166-/-167DEKS (alpha1(I)) and AAQY81-/-82DGKG (alpha2(I)) are identified as meprin cleavage sites
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fibrillar collagen type III + fibrillar collagen type I propeptide
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the enzyme is capable of cleaving off the globular C- and N-terminal prodomains of fibrillar collagen type I and type III
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fibrillar procollagen type III + H2O
fibrillar collagen type III + fibrillar collagen type I propeptide
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the enzyme is capable of cleaving off the globular C- and N-terminal prodomains of fibrillar collagen type I and type III
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Parathyroid hormone + H2O
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involved in PTH-degradation in human kidney
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no activity with claudin-4 in MDCK cells
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additional information
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no activity with claudin-4 in MDCK cells
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additional information
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meprin interacts with epithelial Na+ channel (ENaC)
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additional information
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the enzyme is capable of hydrolyzing and processing a large number of substrates, including extracellular matrix proteins, cytokines, adherens junction proteins, hormones, bioactive peptides, and cell surface proteins
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additional information
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meprin beta preferentially cleaves substrates with acidic amino acids in P1'-position
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additional information
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cleaves growth factors, extracellular matrix proteins, and biological active peptides
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additional information
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the enzyme is capable of hydrolyzing and processing a large number of substrates, including extracellular matrix proteins, cytokines, adherens junction proteins, hormones, bioactive peptides, and cell surface proteins
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additional information
?
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no activity with claudin-4 in MDCK cells
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?
additional information
?
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the enzyme is capable of hydrolyzing and processing a large number of substrates, including extracellular matrix proteins, cytokines, adherens junction proteins, hormones, bioactive peptides, and cell surface proteins
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?
additional information
?
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the enzyme is capable of hydrolyzing and processing a large number of substrates, including extracellular matrix proteins, cytokines, adherens junction proteins, hormones, bioactive peptides, and cell surface proteins
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?