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
-
phosphoramidon-sensitive
- sheddase
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dipeptidylaminopeptidase
-
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
3.4.24.18 meprin AAdvanced search results
results (
results (Subunits
Subunits on EC 3.4.24.18 - meprin A
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SUBUNIT 
ORGANISM
UNIPROT
COMMENTARY 
LITERATURE
dimer
heterodimer
homodimer
-
homodimer linked by a disulfide bridge, domain structure of human meprins, overview
oligomer
tetramer
additional information
oligomer
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x * 69000 + x * 79000, mouse, deglycosylated alpha and beta-subunit, SDS-PAGE in the presence of 2-mercaptoethanol
oligomer
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x * 86000, mouse, performic acid oxidized enzyme, sedimentation equilibrium centrifugation with 4 M guanidine-HCl
oligomer
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x * 69000 + x * 79000, mouse, deglycosylated alpha and beta-subunit, SDS-PAGE in the presence of 2-mercaptoethanol
oligomer
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x * 86000, mouse, performic acid oxidized enzyme, sedimentation equilibrium centrifugation with 4 M guanidine-HCl
tetramer
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disulfide-bridged dimers (alpha2 or alphabeta) aggregate non-covalently to form higher MW complexes, predominantly tetramers
tetramer
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disulfide-bridged dimers (alpha2 or alphabeta) aggregate non-covalently to form higher MW complexes, predominantly tetramers
additional information
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meprin alpha is a multidomain metalloprotease, enzyme domain structure, overview. It tends to oligomerize to huge complexes ring and chain like structures up to the mega Dalton range, which makes it the largest extracellular protease. The enzyme consists of a propeptide (PRO), a catalytic domain (CAT), a MAM (meprin A5 protein tyrosine phosphatase mu) domain, a TRAF (tumor-necrosis-factor-receptor-associated factor) domain, an EGF (epidermal growth factor) like domain, a transmembrane region and a C-terminal part. Additionally, there is a so called inserted domain found in meprin alpha between the TRAF and the EGF like domain. This inserted domain is cleaved by furin resulting in secretion into extracellular space
additional information
meprin alpha is the largest secreted protease known, forming complex homooligomers of molecular weights up to 6MDa
additional information
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the mouse enzyme is composed of disulfide linked dimers associating non-covalently to form tetramers and sometimes higher order oligomers
additional information
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enzyme forms oligomers of ten or more subunits with intersubunit disulfide bonds and further association of subunits. No single glycan is essential for oligomer formation
additional information
-
meprin alpha is a multidomain metalloprotease, enzyme domain structure, overview. It tends to oligomerize to huge complexes ring and chain like structures up to the mega Dalton range, which makes it the largest extracellular protease. The enzyme consists of a propeptide (PRO), a catalytic domain (CAT), a MAM (meprin A5 protein tyrosine phosphatase mu) domain, a TRAF (tumor-necrosis-factor-receptor-associated factor) domain, an EGF (epidermal growth factor) like domain, a transmembrane region and a C-terminal part. Additionally, there is a so called inserted domain found in meprin alpha between the TRAF and the EGF like domain. This inserted domain is cleaved by furin resulting in secretion into extracellular space
additional information
-
the mouse enzyme is composed of disulfide linked dimers associating non-covalently to form tetramers and sometimes higher order oligomers
