Jan 1, 2001 · The Michaelis constant (Km) and first-order rate constant of substrate peptide turnover (kcat) were measured by incubating a range of each peptide with MMP-9. Peptide hydrolysis was measured by incorporation of fluorescamine onto newly formed amino termini as previously described (31, 33, 34).

This active form of MMP-9 degraded SP with a kcat/Km of 170 mM-1 min-1, which is 30-fold greater than the previously reported value for a representative collagen-derived peptide. The major digestion products were identified as SP and SP, which were derived from cleavage of the Gln6-Phe7 bond.

Sep 24, 2018 · Matrix metalloproteinases-2 and -9 (MMP-2/-9) are key tissue remodeling enzymes that have multiple overlapping activities critical for wound healing and tumor progression in vivo.

Importantly, however, even this mutant peptide had a measurable kcat/Km ratio (2000 M21 s21), indicating that efficient hydrolysis can be enacted by MMP-9 if the rest of the substrate sequence is optimal.

It has been previously shown that TGFβ1 induces endothelial cell expression of MMP-2, MMP-9, and MMP-13 [45 – 47], which, in this study, resulted in degradation of each matrix consistent with their degradation kinetics as per their Michaelis-Menten kcat/Km parameters (Table 1).

The initial degradation rates of substance P at a substrate concentration of 25 microM were 5 min-1 for MMP 9 and 150 min-1 for MMP 8. The kinetic constants KM and kcat were determined by concentration-dependent measurements.

Excellent fluorogenic substrate for MMP-7 (k cat /K m = 1.9 x 10 5 M -1 s -1). Excitation maximum: ~280 nm; emission maximum: ~360 nm. The cleavage occurs at the Ala-Leu bond.

I have a protein sequence that can be cleaved by MMP-9 enzymes. The sequence: KGPRQIT. From Kridel, S.J. et al., J.Biol.Chem. 2001, 276:20572-20578 I have found the Kcat, Km value and...

Fluorogenic substrate for several matrix metalloproteinases (MMPs). It is cleaved by MMP-1 (kcat/Km=3.3x10M-1s-1), MMP-2 (kcat/Km=5.8x10), MMP-3 (kcat/Km=2.2x10), MMP-7 (kcat/Km=1.2x10), MMP-8, MMP-9 (kcat/Km=6.9x10), and MMP-26 (kcat/Km=4.9x10) Ex/Em=280nm/346nm, although 283/350,360 are also appropriate.

Feb 22, 2021 · First two tabs, corresponding to MMP-2 and 9, respectively, contain information about a) the sequence of hexamer substrate, b) the corresponding amino acid tetramer sequences for P3-P1՛ positions, c) rank of tetramer based on RP value, d) relative probability (RP), e) measured k cat /K M (M -1 s -1 ), f-g) standard deviation and standard error ...