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

被引：29

作者：

Smalley, John W. ^{[1
]}

Birss, Andrew J. ^{[1
]}

Szmigielski, Borys ^{[3
]}

Potempa, Jan ^{[2
,3
]}

机构：

[1] Univ Liverpool, Sch Dent Sci, Unit Plaque Related Dis, Liverpool L69 3GN, Merseyside, England

[2] Univ Georgia, Dept Biochem & Mol Biol, Athens, GA 30602 USA

[3] Jagiellonian Univ, Fac Biochem Biophys & Biotechnol, Dept Microbiol, PL-30387 Krakow, Poland

来源：

BIOLOGICAL CHEMISTRY | 2008年 / 389卷 / 09期

基金：

美国国家卫生研究院;

关键词：

gingipains; haem; haemoglobin; periodontal disease; Porphyromonas; protease;

D O I：

10.1515/BC.2008.140

中图分类号：

Q5 [生物化学]; Q7 [分子生物学];

学科分类号：

071010 ; 081704 ;

摘要：

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 N-3(-), 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.

引用

页码：1235 / 1238

页数：4

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