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Literature summary for 3.4.24.80 extracted from

  • Minond, D.; Lauer-Fields, J.L.; Nagase, H.; Fields, G.B.
    Matrix metalloproteinase triple-helical peptidase activities are differentially regulated by substrate stability (2004), Biochemistry, 43, 11474-11481.
    View publication on PubMed
Search for more literature for 3.4.24.80

Protein Variants

Protein Variants Comment Organism
additional information MMP-14delta279-523, linker and C-terminal hemopexin-like domain deleted, does not undergo rapid autoproteolysis, relatively small differences to wild type Homo sapiens

KM Value [mM]

KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
additional information
-
 additional information increase in substrate triple-helical thermal stability is not detrimental to enzyme binding of substrate Homo sapiens

Organism

Organism UniProt Comment Textmining
Homo sapiens
-
-
-

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
additional information hydrolysis of triple helical substrates that, via addition of N-terminal alkyl chains, differ in their thermal stabilities, substitution of Cys(4-methoxybenzyl) for Leu in the P1' subsite is greatly favored by MMP-14, increase in substrate triple-helical thermal stability leads to the decreased ability of the enzyme to cleave such substrates Homo sapiens ?
-
 ?

Synonyms

Synonyms Comment Organism
MMP-14
-
 Homo sapiens
MT1-MMP
-
 Homo sapiens

Turnover Number [1/s]

Turnover Number Minimum [1/s] Turnover Number Maximum [1/s] Substrate Comment Organism Structure
additional information
-
 additional information increase in substrate triple-helical thermal stability is detrimental to enzyme turnover of substrate Homo sapiens