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Literature summary for 3.4.24.B12 extracted from

  • Wang, Z.; Luo, J.; Iwamoto, S.; Chen, Q.
    Matrilin-2 is proteolytically cleaved by ADAMTS-4 and ADAMTS-5 (2014), Molecules, 19, 8472-8487.
    View publication on PubMedView publication on EuropePMC

Organism

Organism UniProt Comment Textmining
Homo sapiens Q9UNA0
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-

Source Tissue

Source Tissue Comment Organism Textmining
commercial preparation
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Homo sapiens
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Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
matrilin-2 + H2O
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Homo sapiens ? substrate contains two putative cleavage sites. The first site is located between residues D851 and L852 in the middle of the domain and the second at the boundary with the coiled-coil domain at the C-terminus. Deletion of the entire unique domain eliminates the proteolysis of matrilin-2. The first cleavage site is present in all matrilin-2 oligomers, the second cleavage site becomes apparent only in the matrilin-2 hetero-oligomers with matrilin-1 or matrilin-3 ?