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
-
3.4.24.18
-
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
-
dipeptidylaminopeptidase
-
metzincins
-
pharmacology
-
neurokinins
-
astacin-like
-
met5enkephalin
-
depressor
-
medicine
-
tachykinins
-
neurotensin
-
leu-enkephalin
- 3.4.24.18
-
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
-
dipeptidylaminopeptidase
-
metzincins
- pharmacology
- neurokinins
-
astacin-like
-
met5enkephalin
-
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 (Posttranslational Modification
Posttranslational Modification on EC 3.4.24.18 - meprin A
Please wait a moment until all data is loaded. This message will disappear when all data is loaded.
top
POSTTRANSLATIONAL MODIFICATION 
ORGANISM
UNIPROT
COMMENTARY 
LITERATURE
glycoprotein
proteolytic modification
glycoprotein
-
nine out of ten potential glycoslytation sites are glycosylated. Removal of two glycans at N234 and N270, as well as removal of glycan at N452, decrease the chemical and thermal stability of the homooligomer without affecting quarternary structure
proteolytic modification
-
activation of the inactive zymogen by proteases. In colon carcinoma Caco-2 cells, meprin alpha is activated by plasmin
proteolytic modification
ADAM10 is the major sheddase responsible for the release of membrane-associated meprin A
proteolytic modification
ADAM10 is the major sheddase responsible for the release of membrane-associated meprin A. ADAM10 is the protease responsible for the shedding of meprin beta from the meprin beta and meprin alphabeta transfectants, determination by inhibiotr experiments. Both constitutive as well as PMA- and ionomycin-induced shedding of meprin A in the primary renal tubular epithelial cells is markedly prevented by the hydroxamate inhibitor TAPI-1 and the ADAM10-specific inhibitor GI254023X
proteolytic modification
-
meprins are secreted as zymogens and are activated by trypsin-like serine proteases (e.g., human kallikrein related peptidases, KLK)
proteolytic modification
meprin alpha contains an additional inserted domain (I-domain), which is proteolytically cleaved by furin within the Golgi. Activation of meprin alpha by proteolytic cleavage through furin. Meprin alpha also contains a conserved sequence motif, which gives rise to enzymatic activation by tryptic serine proteases. Pancreatic trypsin performs this activation in the gut. Outside the intestinal tract, meprin alpha can be efficiently activated by plasmin. In the skin, maturation of meprin alpha is done by KLK5 only, not by other KLK proteases
proteolytic modification
the recombinant His6-tagged enzyme is activated by cleavage through trypsin
proteolytic modification
-
meprins are secreted as zymogens and are activated by trypsin-like serine proteases
proteolytic modification
-
activation of recombinant zymogen enzyme by trypsin
-
