Substrate recognition by gelatinase A: the C-terminal domain facilitates surface diffusion.
An investigation of gelatinase A binding to gelatin produced results that are inconsistent with a traditional bimolecular Michaelis-Menten formalism but are effectively accounted for by a power law characteristic of fractal kinetics. The main reason for this inconsistency is that the bulk of the gelatinase A binding depends on its ability to diffuse laterally on the gelatin surface. Most interestingly, we show that the anomalous lateral diffusion and, consequently, the binding to gelatin is greatly facilitated by the C-terminal hemopexin-like domain of the enzyme whereas the specificity of binding resides with the fibronectin-like gelatin-binding domain.
Collier
I E
IE
Division of Dermatology, Washington University School of Medicine, St. Louis, Missouri 63110, USA.
Saffarian
S
S
Marmer
B L
BL
Elson
E L
EL
Goldberg
G
G
D020816:Amino Acid Motifs / Q000502:physiology; D000818:Animals; D001665:Binding Sites / Q000502:physiology; D002478:Cells, Cultured / Q000201:enzymology; D004058:Diffusion; D017709:Fractals; D005780:Gelatin / Q000378:metabolism*; D007553:Isotope Labeling / Q000379:methods; D007700:Kinetics; D020778:Matrix Metalloproteinase 2 / Q000378:metabolism*; D008954:Models, Biological; D017434:Protein Structure, Tertiary / Q000502:physiology; D013379:Substrate Specificity / Q000502:physiology; D013462:Sulfur Radioisotopes / Q000378:metabolism; D013499:Surface Properties
D013462:Sulfur Radioisotopes; D005780:Gelatin; D020778:Matrix Metalloproteinase 2