[HTML][HTML] Structural and kinetic analysis of the substrate specificity of human fibroblast activation protein α
K Aertgeerts, I Levin, L Shi, GP Snell, A Jennings… - Journal of Biological …, 2005 - ASBMB
Fibroblast activation protein α (FAPα) is highly expressed in epithelial cancers and has been
implicated in extracellular matrix remodeling, tumor growth, and metastasis. We present the
first high resolution structure for the apoenzyme as well as kinetic data toward small
dipeptide substrates. FAPα exhibits a dipeptidyl peptidase IV (DPPIV)-like fold, featuring an
α/β-hydrolase domain and an eight-bladed β-propeller domain. Known DPPIV dipeptides
are cleaved by FAPα with an∼ 100-fold decrease in catalytic efficiency compared with …
implicated in extracellular matrix remodeling, tumor growth, and metastasis. We present the
first high resolution structure for the apoenzyme as well as kinetic data toward small
dipeptide substrates. FAPα exhibits a dipeptidyl peptidase IV (DPPIV)-like fold, featuring an
α/β-hydrolase domain and an eight-bladed β-propeller domain. Known DPPIV dipeptides
are cleaved by FAPα with an∼ 100-fold decrease in catalytic efficiency compared with …