Cardiff University | Prifysgol Caerdydd ORCA
Online Research @ Cardiff 
WelshClear Cookie - decide language by browser settings

Plasmepsins

Berry, Colin ORCID: https://orcid.org/0000-0002-9943-548X and Goldberg, Daniel E. 2004. Plasmepsins. Barrett, Alan J., Woessner, J. Fred and Rawlings, Neil D., eds. Handbook of Proteolytic Enzymes (Second Edition) Volume 1: Aspartic and Metallo Peptidases, Elsevier, pp. 70-73. (10.1016/B978-0-12-079611-3.50022-7)

Full text not available from this repository.

Abstract

This chapter elaborates the structural chemistry and the biological aspects of plasmepsins. Plasmepsin I is capable of cleaving native human hemoglobin and acid-denatured globin, with a pH optimum around 5. Plasmepsin I, II, IV and HAP are made as 51 kDa precursors that are cleaved to 37 kDa mature forms. There are two disulfide bonds predicted. The second domain contains an active-site Asp-Ser-Gly instead of the usual aspartic protease Asp-Thr-Gly. HAP is an exception to this. A molecular model of plasmepsin I has been constructed, based on the crystal structure of the highly homologous plasmepsin II. The modeled structure bears general features of mammalian and fungal aspartic proteases, and among mammalian orthologs shares greatest structural similarity with cathepsin D. Pepstatin is bound in the active site with enough conformational difference from mammalian homologs to give hope for development of a selective inhibitor. Native plasmepsin I, II and HAP can be prepared in nanogram to low microgram amounts from cultured intraerythrocytic organisms. Plasmepsin I, II, IV and HAP are 55–75% identical at the amino acid level.

Item Type: Book Section
Date Type: Publication
Status: Published
Schools: Biosciences
Subjects: Q Science > QR Microbiology
Publisher: Elsevier
ISBN: 9780120796113
Related URLs:
Last Modified: 27 Oct 2022 09:13
URI: https://orca.cardiff.ac.uk/id/eprint/64839

Citation Data

Actions (repository staff only)

Edit Item Edit Item