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
-
natriuretic
- enkephalin
- thiorphan
-
angiotensin-converting
- angiotensin
- astacins
- metalloproteases
-
brush
- bradykinin
-
3.4.15.1
- captopril
- neprilysin
- metallopeptidases
- anp
- aminopeptidases
- acetorphan
-
math
- endopeptidases
-
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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Localization
Localization on EC 3.4.24.18 - meprin A
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additional information
meprin alpha contains an additional inserted domain (I-domain), which is proteolytically cleaved by furin within the Golgi
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brush-border membranes of proximal tubules and intestines
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brush-border membranes of proximal tubules and intestines
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brush-border membranes of proximal tubules and intestines
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brush-border membranes of proximal tubules and intestines
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meprin alpha is constitutively shed by furin during the secretory pathway and secreted into extracellular space. Meprin alpha tends to oligomerize to huge complexes ring and chain like structures up to the mega Dalton range, which makes it the largest extracellular protease
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meprin alpha is constitutively shed by furin during the secretory pathway and secreted into extracellular space. Meprin alpha tends to oligomerize to huge complexes ring and chain like structures up to the mega Dalton range, which makes it the largest extracellular protease
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ADAM10 is the major sheddase responsible for the release of membrane-associated meprin A
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meprin A, is a membrane-associated neutral metalloendoprotease. Importance of a sheddase involved in the release of membrane-associated meprin A under pathological conditions
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cell surface metalloproteinase, alphabeta-heterodimers firmly attached to brush border membrane, alpha2-homodimers only associated with membrane
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beta subunits are type I integral membrane proteins and alpha subunits are disulfide linked to or non-covalently associated with membrane-anchored meprin beta subunits
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meprin A, is a membrane-associated neutral metalloendoprotease. Importance of a sheddase involved in the release of membrane-associated meprin A under pathological conditions
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meprin A, is a membrane-associated neutral metalloendoprotease. Importance of a sheddase involved in the release of membrane-associated meprin A under pathological conditions
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cell surface metalloproteinase, alphabeta-heterodimers firmly attached to brush border membrane, alpha2-homodimers only associated with membrane
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beta subunits are type I integral membrane proteins and alpha subunits are disulfide linked to or non-covalently associated with membrane-anchored meprin beta subunits
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meprin A, is a membrane-associated neutral metalloendoprotease. Importance of a sheddase involved in the release of membrane-associated meprin A under pathological conditions