Substrate recognition by gelatinase A: The C-terminal domain facilitates surface diffusion

Ivan E. Collier, Saveez Saffarian, Barry L. Marmer, Elliot L. Elson, Greg Goldberg

Research output: Contribution to journalArticlepeer-review

27 Scopus citations

Abstract

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.

Original languageEnglish
Pages (from-to)2370-2377
Number of pages8
JournalBiophysical Journal
Volume81
Issue number4
DOIs
StatePublished - 2001

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