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3.4.24.63: meprin B

This is an abbreviated version!
For detailed information about meprin B, go to the full flat file.

Word Map on EC 3.4.24.63

Reaction

Hydrolysis of proteins, including azocasein, and peptides. Hydrolysis of -His5-/-Leu-, -Leu6-/-Cys-, -Ala14-/-Leu- and -Cys19-/-Gly- bonds in insulin B chain =

Synonyms

beta-secretase, cell surface sheddase, h-meprin beta, MEP1B, mephrin beta, meprin A subunit beta, Meprin b, meprin B metalloprotease, meprin beta, meprin beta metalloproteinase, meprin metalloprotease, meprin metalloproteinase, meprin metalloproteinase beta, meprin-beta, meprinbeta, metalloprotease meprin, metalloprotease meprin B, metalloprotease meprin beta, metalloproteinase meprin beta, Mmepb, More, mouse meprin beta, procollagen proteinase, Rmepb

ECTree

     3 Hydrolases
         3.4 Acting on peptide bonds (peptidases)
             3.4.24 Metalloendopeptidases
                3.4.24.63 meprin B

Engineering

Engineering on EC 3.4.24.63 - meprin B

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PROTEIN VARIANTS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
D240A
site-directed mutagenesis, the D204A mutant shows almost no signal at the cell surface, but strongly colocalized with the endoplasmic reticulum marker, low cell surface activity of D204A enzyme
D245A
site-directed mutagenesis
D47A
the mutation is localized in the pro-peptide of the protease, the mutant is transported to the cell surface and exhibit expression comparable with wild-type meprin beta
E153A
site-directed mutagenesis, a proteolytic inactive mutant enzyme
E90A
soluble inactive mutant of meprin beta
G32R
naturally occuring mutant, the mutation is localized in the pro-peptide of the protease and identified in endometrium cancer, the mutant is transported to the cell surface and exhibit expression comparable with wild-type meprin beta, the mutant is more active against a peptide substrate (meprin beta-specific peptide substrate that is linked to a fluorogenic group (MCA) at the N-terminus and a quencher (DPN) at the C-terminus) and the interleukin-6 receptor than wild-type meprin beta. The change to an arginine residue at position 32 represents an additional activation site used by furin-like proteases in the Golgi, which consequently leads to reduced shedding by ADAM17. The meprin beta G32R variant assesses cell proliferation, invasion through a collagen IV matrix, and outgrowth from tumor spheroids. Increased meprin beta G32R activity at the cell surface reduces cell proliferation, but increases cell invasion. The G32R meprin beta variant shows increased activity. Phenotype, overview
G32R/R61S
site-directed mutagenesis, the double mutant has two altered sites that can no longer be proteolytically cleaved and cannot be activated or shedded
K185Y
-
site-directed mutagenesis
additional information