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Literature summary for 3.4.24.B12 extracted from

  • Lim, N.H.; Kashiwagi, M.; Visse, R.; Jones, J.; Enghild, J.J.; Brew, K.; Nagase, H.
    Reactive-site mutants of N-TIMP-3 that selectively inhibit ADAMTS-4 and ADAMTS-5: biological and structural implications (2010), Biochem. J., 431, 113-122.
    View publication on PubMedView publication on EuropePMC

Inhibitors

Inhibitors Comment Organism Structure
N-terminal inhibitory domain of tissue inhibitor of metalloproteinases 3 N-terminal mutants of N-TIMP-3 (tissue inhibitor of metalloproteinases 3) that have lost their matrix metalloproteinaseP-inhibitory activities (N-TIMP-3(T2G) and [-1A]N-TIMP-3), retain their ability to inhibit ADAMTS-4 and ADAMTS-5. The [-2A]N-TIMP-3 mutant also retains strong affinity with ADAMTS-5, but has a lower affinity for ADAMTS-4 and ADAM17 Homo sapiens

Organism

Organism UniProt Comment Textmining
Homo sapiens Q9UNA0
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-

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
additional information recombinant protein substrate based on the IGD (interglobular domain) of aggrecan, gst-IGD-flag Homo sapiens ?
-
?

Synonyms

Synonyms Comment Organism
ADAMTS-5-2 ADAMTS-5 which lacks the C-terminal cysteine-rich spacer and thrombospondin domains Homo sapiens

Temperature Optimum [°C]

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

Ki Value [mM]

Ki Value [mM] Ki Value maximum [mM] Inhibitor Comment Organism Structure
additional information
-
additional information Ki(app) of N-terminal alanine-extension mutants and of position [-1] mutants of N-terminal inhibitory domain of tissue inhibitor of metalloproteinases 3 Homo sapiens