Collagenase Module

Enzymatic activity (but only partial peptide processing) is contained within the peptidase domain (Asp398-Gly790), confirmed by an enzymatic assay of a deletion construct containing only (lys396-lys1118) having 100% activity (Figure 1.) 


The Glycine rich hinge region is also shown in figure 1. to be essential in collagenolytic activity due to the deletion construct delta(Gly3890-Val397) causing a significant drop in collagen processivity.

Figure.1 This deletion construct assay tells us that the entire molecule is essential for collagen processivity, rather than just short peptide specificity. This is due to varying interactions between the peptidase domain and activator domain. The glycine rich hinge region deletion construct also showed it's significance in collagen processivity

Processing of the entire collagen molecule rather than just partial peptide processing requires the activator domain in conjunction with the peptidase domain, as the peptidase domain deletion construct was only able to have activity against small peptide substrate. The collagenase module therefore consists of the activator + peptidase domain (Tyr119-Gly790)