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. 2020 Jun 9;7:319. doi: 10.3389/fvets.2020.00319

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Copyright © 2020 Bhowmick and Han.

This is an open-access article distributed under the terms of the Creative Commons Attribution License (CC BY). The use, distribution or reproduction in other forums is permitted, provided the original author(s) and the copyright owner(s) are credited and that the original publication in this journal is cited, in accordance with accepted academic practice. No use, distribution or reproduction is permitted which does not comply with these terms.

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A proposed model for the hemoglobinolytic pathway in I. ricinus [modified from (75)]. The enzymes are color-coded according to clan membership- AA clan aspartic peptidases (red), CD clan cysteine peptidases (purple), CA clan (papain family) cysteine peptidases (green), and serine and metallopeptidases (black). The endopeptidases, cathepsin D (CatD) supported by cathepsin L (CatL) and legumain (AE), are responsible for the primary cleavage of hemoglobin. The production of secondary small fragments is dominated by the endopeptidase activity of cathepsin B (CatB). Exopeptidases act on the peptides released by the action of the endopeptidases through the carboxy-dipeptidase activity of CatB and the amino-dipeptidase activity of cathepsin C (CatC). Monopeptidases, including leucine aminopeptidase (LAP) and serine carboxypeptidase (SCP), might participate in the liberation of free amino acids.