Characterization of PepB, a group B streptococcal oligopeptidase.
Characterization of PepB, a group B streptococcal oligopeptidase.
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PepB（一种 B 族链球菌寡肽酶）的表征。
DOI：
10.1128/iai.64.8.3401-3406.1996
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发表时间：
1996
影响因子：
3.1
通讯作者：
Pritchard,DG
中科院分区：
文献类型：
--
作者：
Lin,B;Averett,WF;Novak,J;Chatham,WW;Hollingshead,SK;Coligan,JE;Egan,ML;Pritchard,DG
最近报道B族链球菌具有细胞相关胶原酶。尽管该酶水解了合成的胶原样底物N-（3-[2-呋喃基]丙烯酰基）-Leu-Gly-Pro-Ala，但我们发现，无论是高度纯化的酶还是粗制的B族链球菌细胞裂解物都不能溶解重构的鼠尾胶原蛋白膜，这种活性被认为是真正的胶原酶所必需的。我们克隆并测序了酶（pepB）的基因。推导的氨基酸序列显示66.4%的同一性，从乳酸乳球菌，M3或thimet家族的锌金属肽酶的成员PepF寡肽酶。组B链球菌酶也表现出寡肽酶活性和降解各种小的生物活性肽，包括缓激肽，神经降压素，和P物质和促肾上腺皮质激素的肽片段。
Group B streptococci were recently reported to possess a cell-associated collagenase. Although the enzyme hydrolyzed the synthetic collagen-like substrate N-(3-[2-furyl]acryloyl)-Leu-Gly-Pro-Ala, we found that neither the highly purified enzyme nor crude group B streptococcal cell lysate solubilized a film of reconstituted rat tail collagen, an activity regarded as obligatory for a true collagenase. We cloned and sequenced the gene for the enzyme (pepB). The deduced amino acid sequence showed 66.4% identity to the PepF oligopeptidase from Lactococcus lactis, a member of the M3 or thimet family of zinc metallopeptidases. The group B streptococcal enzyme also showed oligopeptidase activity and degraded a variety of small bioactive peptides, including bradykinin, neurotensin, and peptide fragments of substance P and adrenocorticotropin.