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Literature summary for 3.4.24.65 extracted from

  • Liang, X.; Arunima, A.; Zhao, Y.; Bhaskaran, R.; Shende, A.; Byrne, T.S.; Fleeks, J.; Palmier, M.O.; Van Doren, S.R.
    Apparent tradeoff of higher activity in MMP-12 for enhanced stability and flexibility in MMP-3 (2010), Biophys. J., 99, 273-283.
    View publication on PubMedView publication on EuropePMC
Search for more literature for 3.4.24.65

Protein Variants

Protein Variants Comment Organism
E219A NMR studies used MMP-12 preserved by E219A substitution of the general base Homo sapiens

General Stability

General Stability Organism
catalytic domain of MMP-12 exhibits higher activity, more rigidity of its backbone, and lower folding stability than its counterpart of the MMP-3 catalytic domain that has more internal motions throughout Homo sapiens

Organism

Organism UniProt Comment Textmining
Homo sapiens
-
-
-

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
DQ-collagen I + H2O
-
 Homo sapiens ?
-
 ?
DQ-collagen IV + H2O
-
 Homo sapiens ?
-
 ?
elastin fELN-125 + H2O
-
 Homo sapiens ?
-
 ?
Mca-Pro-Leu-Gly-Leu-Dpa-Ala-Arg-NH2 + H2O
-
 Homo sapiens ?
-
 ?
triple helical peptide alpha1(V) + H2O collagen V fibrils Homo sapiens ?
-
 ?

Synonyms

Synonyms Comment Organism
MMP-12
-
 Homo sapiens

kcat/KM [mM/s]

kcat/KM Value [1/mMs-1] kcat/KM Value Maximum [1/mMs-1] Substrate Comment Organism Structure
9.8
-
 elastin fELN-125 pH 7.5, 25°C Homo sapiens
29.2
-
 DQ-collagen IV pH 7.5, 25°C Homo sapiens
34.6
-
 DQ-collagen I pH 7.5, 25°C Homo sapiens
55.4
-
 triple helical peptide alpha1(V) pH 7.5, 25°C Homo sapiens
133.8
-
 Mca-Pro-Leu-Gly-Leu-Dpa-Ala-Arg-NH2 pH 7.5, 25°C Homo sapiens