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. 2020 Dec 8;10(12):1648. doi: 10.3390/biom10121648

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© 2020 by the authors.

Licensee MDPI, Basel, Switzerland. This article is an open access article distributed under the terms and conditions of the Creative Commons Attribution (CC BY) license (http://creativecommons.org/licenses/by/4.0/).

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Potential enzymatic functions and structural visualization of TNAP. (A) Depiction of potential TNAP substrates. (B) Schematic depiction of a predicted homology model of TNAP’s dimerized 3D structure (https://swissmodel.expasy.org/; SWISS-MODEL: P05186 (PPBT_HUMAN); homology model according to the template: 3mk1.1.B “Refinement of placental alkaline phosphatase complexed with nitrophenyl”) and magnified view of the active site [26,27,28]. Figure 1B was modified according to SWISS-MODEL database terms of use and is licensed under a Creative Commons Attribution 4.0 (https://creativecommons.org/licenses/by-sa/4.0/). ATP/ADP/AMP: adenosine tri-/di-/monophosphate, GPI-anchor: glycosyl-phosphatidylinositol anchor, Pi: phosphate, PLP: pyridoxal-5′-phosphate, p-OPN: phosphorylated osteopontin, PPi: inorganic pyrophosphate, TNAP: tissue-nonspecific alkaline phosphatase.