Mechanism of methaemoglobin breakdown by the lysine-specific gingipain of the periodontal pathogen Porphyromonas gingivalis.

Smalley, John W, Birss, Andrew J, Szmigielski, Borys and Potempa, Jan (2008) Mechanism of methaemoglobin breakdown by the lysine-specific gingipain of the periodontal pathogen Porphyromonas gingivalis. Biological chemistry, 389 (9). pp. 1235-1238.

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Abstract

Abstract The R- and K-gingipain proteases of Porphyromonas gingivalis are involved in proteolysis of haemoglobin from which the defensive dimeric haem pigment is formed. Whilst oxyhaemoglobin is refractory towards K-gingipain, methaemoglobin is rapidly degraded. Ligation of methaemoglobin with N3-, which effectively blocks haem dissociation from the protein, prevented haemoglobin breakdown. Haem-free globin was rapidly degraded by K-gingipain. These data emphasise the need for haemoglobin oxidation which encourages haem dissociation and makes the haem-free globin susceptible to proteolytic attack.

Item Type:	Article
Additional Information:	published online: 17/09/2008. Citation Information. Biological Chemistry. Volume 389, Issue 9, Pages 1235–1238, ISSN (Online) 1437-4315, ISSN (Print) 1431-6730, DOI: 10.1515/BC.2008.140, September 2008
Uncontrolled Keywords:	Animals, Horses, Porphyromonas gingivalis, Cysteine Endopeptidases, Adhesins, Bacterial, Methemoglobin, Ligands, Gingipain Cysteine Endopeptidases
Subjects:	?? RK ??
Divisions:	Faculty of Health and Life Sciences > Institute of Life Courses and Medical Sciences > School of Dentistry
Depositing User:	Symplectic Admin
Date Deposited:	05 Dec 2008 10:17
Last Modified:	15 Mar 2024 06:52
DOI:	10.1515/bc.2008.140
Publisher's Statement :	The Version of Record (VoR) is available at www.biochemj.org
Related URLs:	Author Publisher
URI:	https://livrepository.liverpool.ac.uk/id/eprint/946