The C-terminal domains of ADAMTS1 contain exosites involved in its proteoglycanase activity.

ABSTRACT: A disintegrin-like and metalloproteinase with thrombospondin type 1 motifs (ADAMTS1) is a protease involved in fertilization, cancer, cardiovascular development, and thoracic aneurysms. Proteoglycans such as versican and aggrecan have been identified as ADAMTS1 substrates, and Adamts1 ablation in mice typically results in versican accumulation; however, previous qualitative studies have suggested that ADAMTS1 proteoglycanase activity is weaker than that of other family members such as ADAMTS4 and ADAMTS5. Here, we investigated the functional determinants of ADAMTS1 proteoglycanase activity. We found that ADAMTS1 versicanase activity is approximately 1000-fold lower than ADAMTS5 and 50-fold lower than ADAMTS4 with a kinetic constant (k_cat/K_m) of 3.6 × 10³ M<

SUBMITTER: Minns AF 

PROVIDER: S-EPMC10033314 | biostudies-literature | 2023 Apr

REPOSITORIES: biostudies-literature