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Literature summary for 3.4.24.7 extracted from

  • Lauer-Fields, J.L.; Broder, T.; Sritharan, T.; Chung, L.; Nagase, H.; Fields, G.B.
    Kinetic analysis of matrix metalloproteinase activity using fluorogenic triple-helical substrates (2001), Biochemistry, 40, 5795-5803.
    View publication on PubMed
Search for more literature for 3.4.24.7

Protein Variants

Protein Variants Comment Organism
DELTA243-340 about 10% increase in turnover number and 9% increase in Km-value compared to wild-type enzyme with fTHP-3 as substrate Homo sapiens

KM Value [mM]

KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
0.0612
-
 fTHP-3 30°C, MMP-1 Homo sapiens
0.0666
-
 fTHP-3 30°C, MMP-1(DELTA243-450) Homo sapiens

Organism

Organism UniProt Comment Textmining
Homo sapiens
-
-
-

Source Tissue

Source Tissue Comment Organism Textmining
culture supernatant of rheumatoid synovial cells stimulated with rabbit macrophage-conditioned medium Homo sapiens
-

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
fTHP-3 + H2O the fluorogenic triple-helical substrate mimics the behavior of the native collagen substrate and may be useful for the investigation of collagenase triple-helical activity Homo sapiens additional information the Gly-Leu bond is cleaved, the triple helix denatures and the two products generated are the single-stranded N-terminal peptide C6-(Gly-Pro-Hyp)5-Gly-Pro-Lys[(7-methoxycoumarin-4-yl)acetyl]-Gly-Pro-Gln-Gly and the single-stranded C-terminal peptide Leu-Arg-Gly-Gln-Lys-(2,4-dinitrophenyl)-Gly-Val-Arg-(Gly-Pro-Hyp)5-NH2 ?

Turnover Number [1/s]

Turnover Number Minimum [1/s] Turnover Number Maximum [1/s] Substrate Comment Organism Structure
0.08
-
 fTHP-3 30°C, MMP-1 Homo sapiens
0.087
-
 fTHP-3 30°C, MMP-1(DELTA243-450) Homo sapiens