Prolyl tripeptidyl peptidase from Porphyromonas gingivalis -: A novel enzyme with possible pathological implications for the development of periodontitis
Prolyl tripeptidyl peptidase from Porphyromonas gingivalis -: A novel enzyme with possible pathological implications for the development of periodontitis
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DOI：
10.1074/jbc.274.14.9246
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发表时间：
1999-04-02
影响因子：
4.8
通讯作者：
Potempa, J
中科院分区：
文献类型：
--
作者：
Banbula, A;Mak, P;Potempa, J
牙龈卟啉单胞菌具有复杂的蛋白水解酶系统，对其生长和逃避寄主防御机制是必不可少的。本文从蛋白质和基因组水平鉴定了该系统中一种新的具有脯氨酰三肽基肽酶活性的多肽酶。对该酶进行了纯化，并对其酶活性和生化性质进行了研究，氨基末端的氨基酸序列和内部的多肽片段使我们能够鉴定该酶的编码基因，我们称之为Pro基三肽基肽酶A的PTPA。该基因编码一个82 kDa的蛋白质，其中包含一个GWSYGG基序，这是S9 Pro基寡肽酶家族丝氨酸蛋白酶家族成员特有的。然而，它与其他属于枯草杆菌蛋白家族的三肽基肽酶在结构上没有任何相似之处。脯氨酰三肽基肽酶的产生可能通过该酶与宿主和细菌胶原酶的相互作用，以及二肽基肽酶在感染过程中对胶原的降解而参与牙周组织破坏的发病机制。
Porphyromonas gingivalis possesses a complex proteolytic system, which is essential for both its growth and evasion of host defense mechanisms, In this report we characterized, both at a protein and genomic level, a novel peptidase of this system with prolyl tripeptidyl peptidase activity. The enzyme was purified to homogeneity, and its enzymatic activity and biochemical properties were investigated The amino acid sequence at the amino terminus and of internal peptide fragments enabled identification of the gene encoding this enzyme, which we refer to as PtpA for prolyl tripeptidyl peptidase A. The gene encodes an 82-kDa protein, which contains a GWSYGG motif, characteristic for members of the S9 prolyl oligopeptidase family of serine proteases. However, it does not share any structural similarity to Other tripeptidyl peptidases, which, belong to the subtilisin family. The production of prolyl tripeptidyl peptidase may contribute to the pathogenesis of periodontal tissue destruction through the mutual interaction of this enzyme, host and bacterial collagenases, and, dipeptidyl peptidases in the degradation of collagen during the course of infection.