A disintegrin and metalloproteinase with thrombospondin motifs 14

Definition:

Has aminoprocollagen type I processing activity in the absence of ADAMTS2. Seems to be synthesized as a latent enzyme that requires activation to display aminoprocollagen peptidase activity. Cleaves lysyl oxidase LOX at a site downstream of its propeptide cleavage site to produce a short LOX form.

References:

[1]. Alain Colige, et al. Cloning and characterization of ADAMTS-14, a novel ADAMTS displaying high homology with ADAMTS-2 and ADAMTS-3. J Biol Chem. 2002 Feb 22;277(8):5756-66. [Content Brief]

[2]. Tamara Rosell-García, et al. Differential cleavage of lysyl oxidase by the metalloproteinases BMP1 and ADAMTS2/14 regulates collagen binding through a tyrosine sulfate domain. J Biol Chem. 2019 Jul 19;294(29):11087-11100. [Content Brief]

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