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Literature summary for 3.4.24.63 extracted from

  • Schneppenheim, J.; Scharfenberg, F.; Lucius, R.; Becker-Pauly, C.; Arnold, P.
    Meprin beta and BMP-1 are differentially regulated by CaCl2 (2017), Cell Calcium, 65, 8-13 .
    View publication on PubMed

Inhibitors

Inhibitors Comment Organism Structure
Ca2+ inhibits, a negative regulator of meprin beta Homo sapiens

Localization

Localization Comment Organism GeneOntology No. Textmining
cell surface
-
Homo sapiens 9986
-
membrane meprin beta is a membrane-bound protein with a transmembrane helix and a small C-terminal cytosolic domain Homo sapiens 16020
-
additional information meprin beta is primarily membrane-bound and forms asymmetric disulfide linked homodimer at the cell surface Homo sapiens
-
-

Metals/Ions

Metals/Ions Comment Organism Structure
Zn2+ a zinc-dependent metalloprotease Homo sapiens

Natural Substrates/ Products (Substrates)

Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
pro-collagen I + H2O Homo sapiens maturation collagen I + collagen I propeptide
-
?

Organism

Organism UniProt Comment Textmining
Homo sapiens Q16820
-
-

Posttranslational Modification

Posttranslational Modification Comment Organism
proteolytic modification the crystal structure of the zymogen form of meprin beta revealsthat the active side is shielded by the pro-peptide. Gln62 is directed away from the salt bridge that is formed by Glu163 and Lys248. The new N-terminus is formed by Asp62 after removal of the pro-peptide by tryptic serine protease cleavage between Arg61 and Gln62. In active meprin beta N62 forms a salt bridge with E163 and thus removes the new N-terminus from the active site, overview Homo sapiens

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
pro-collagen I + H2O maturation Homo sapiens collagen I + collagen I propeptide
-
?
pro-collagen I + H2O cleavage of the C-terminal pro-domain Homo sapiens collagen I + collagen I propeptide
-
?

Subunits

Subunits Comment Organism
homodimer the enzyme consists of the protease domain with a 39 amino acid long inhibitory pro-peptide, a MAM domain, a TRAF domain, an EGF-like domain, a transmembrane helix, and a small C-terminal cytosolic domain Homo sapiens

Synonyms

Synonyms Comment Organism
meprin beta
-
Homo sapiens

Temperature Optimum [°C]

Temperature Optimum [°C] Temperature Optimum Maximum [°C] Comment Organism
37
-
assay at Homo sapiens

pH Optimum

pH Optimum Minimum pH Optimum Maximum Comment Organism
7.5
-
assay at Homo sapiens

General Information

General Information Comment Organism
malfunction ablation of one of the two zinc metalloproteinases, meprin beta and BMP-1, leads to different collagen I associated phenotypes in vivo Homo sapiens
metabolism the zinc metalloproteinases meprin beta and BMP-1 are differentially regulated by CaCl2, overview Homo sapiens
additional information structural differences between meprin beta and BMP-1 (EC 3.4.24.21). Molecular dynamics simulation Homo sapiens
physiological function a reduction in activity is reported under increasing calcium concentrations for meprin beta Homo sapiens