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Literature summary for 3.4.24.18 extracted from

  • Broder, C.; Arnold, P.; Vadon-Le Goff, S.; Konerding, M.A.; Bahr, K.; Mueller, S.; Overall, C.M.; Bond, J.S.; Koudelka, T.; Tholey, A.; Hulmes, D.J.; Moali, C.; Becker-Pauly, C.
    Metalloproteases meprin ? and meprin ? are C- and N-procollagen proteinases important for collagen assembly and tensile strength (2013), Proc. Natl. Acad. Sci. USA, 110, 14219-14224.
    View publication on PubMedView publication on EuropePMC
Search for more literature for 3.4.24.18

Protein Variants

Protein Variants Comment Organism
additional information generation of meprin A deficient Mep1a-/- mice, phenotype overview. Maturation of type I procollagen is reduced in skin and primary fibroblasts from Mep1a?/? mice, the skin shows reduced tensile strength Mus musculus

Natural Substrates/ Products (Substrates)

Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
procollagen I + H2O Mus musculus meprin alpha removes both the C- and N-propeptides of type I procollagen, subsequently releasing fibril-forming mature collagen molecules. The C-terminal cleavage sites in the proalpha1(I) chain generated by the enzyme is identified as Ala1218/Asp1219, identical to the BMP-1 cleavage site, and also Arg1227/Asp1228, nine residues C-terminal to the BMP-1 cleavage site collagen I + propeptide of collagen III
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 ?

Organism

Organism UniProt Comment Textmining
Mus musculus
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-
-

Source Tissue

Source Tissue Comment Organism Textmining
fibroblast
-
 Mus musculus
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skin
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 Mus musculus
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Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
miniprocollagen alpha1(I) homotrimers + H2O
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 Mus musculus ?
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 ?
procollagen I + H2O meprin alpha removes both the C- and N-propeptides of type I procollagen, subsequently releasing fibril-forming mature collagen molecules. The C-terminal cleavage sites in the proalpha1(I) chain generated by the enzyme is identified as Ala1218/Asp1219, identical to the BMP-1 cleavage site, and also Arg1227/Asp1228, nine residues C-terminal to the BMP-1 cleavage site Mus musculus collagen I + propeptide of collagen III
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 ?
procollagen I + H2O recombinant human substrate, generation of mature collagen molecules that spontaneously assemble into collagen fibrils Mus musculus collagen I + propeptide of collagen III
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 ?

Synonyms

Synonyms Comment Organism
meprin alpha
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 Mus musculus

General Information

General Information Comment Organism
malfunction enzyme-deficient mice show lower amounts of mature collagen I compared with wild-type mice and exhibit significantly reduced collagen deposition in skin, along with markedly decreased tissue tensile strength Mus musculus
physiological function physiological relevance of the unique ability of meprin alpha and meprin beta, EC 3.4.24.63, to remove the both the C- and N-propeptides of type I procollagen, subsequently releasing fibril-forming mature collagen molecules. The enzyme contributes to the integrity of connective tissue in skin Mus musculus