1qdm

</td></tr><tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[https://en.wikipedia.org/wiki/Phytepsin Phytepsin], with EC number [https://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.4.23.40 3.4.23.40] </span></td></tr>

[[https://www.uniprot.org/uniprot/ASPR_HORVU ASPR_HORVU]] Involved in the breakdown of propeptides of storage proteins in protein-storage vacuoles (By similarity).

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== Publication Abstract from PubMed ==

We determined at 2.3 A resolution the crystal structure of prophytepsin, a zymogen of a barley vacuolar aspartic proteinase. In addition to the classical pepsin-like bilobal main body of phytepsin, we also traced most of the propeptide, as well as an independent plant-specific domain, never before described in structural terms. The structure revealed that, in addition to the propeptide, 13 N-terminal residues of the mature phytepsin are essential for inactivation of the enzyme. Comparison of the plant-specific domain with NK-lysin indicates that these two saposin-like structures are closely related, suggesting that all saposins and saposin-like domains share a common topology. Structural analysis of prophytepsin led to the identification of a putative membrane receptor-binding site involved in Golgi-mediated transport to vacuoles.

Crystal structure of plant aspartic proteinase prophytepsin: inactivation and vacuolar targeting.,Kervinen J, Tobin GJ, Costa J, Waugh DS, Wlodawer A, Zdanov A EMBO J. 1999 Jul 15;18(14):3947-55. PMID:10406799<ref>PMID:10406799</ref>

From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>

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== References ==

<references/>

[[Category: Costa, J]]

[[Category: Kervinen, J]]

[[Category: Tobin, G J]]

[[Category: Waugh, D S]]

[[Category: Wlodawer, A]]

[[Category: Zdanov, A]]

[[Category: Zymogen structure]]