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首页> 外文期刊>Proceedings of the National Academy of Sciences of the United States of America >AMINOPEPTIDASE B FROM THE RAT TESTIS IS A BIFUNCTIONAL ENZYME STRUCTURALLY RELATED TO LEUKOTRIENE-A(4) HYDROLASE
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AMINOPEPTIDASE B FROM THE RAT TESTIS IS A BIFUNCTIONAL ENZYME STRUCTURALLY RELATED TO LEUKOTRIENE-A(4) HYDROLASE

机译：来自大鼠睾丸的肽酶B是一种结构上与白三烯-A（4）水解酶有关的功能性酶

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摘要

An aminopeptidase B (Ap-B) was previously purified to homogeneity from rat testis extracts and characterized, In the present work, by using oligonucleotides selected on the basis of partial amino acid microsequences of pure Ap-B and PCR techniques, the nucleotide sequence of a 2.2-kb cDNA was obtained, The deduced amino acid sequence corresponds to a 648-residue protein (72.3 kDa) containing the canonical ''HEXXHX(18)E'' signature, which allowed its classification as a member of the MI family of metallopeptidases, It exhibits 33% identity and 48% similarity with leukotriene-A(4) hydrolase, a relation further supported by the capacity of Ap-B to hydrolyze leukotriene A(4). Both enzymes also were closely related to a partially sequenced protein from Dictyostelium discoideum, which might constitute the putative common ancestor of either aminopeptidase or epo tide hydrolase, or both, Ap-B and its mRNA were detected in the germ line and in the Sertoli and peritubular cells of the seminiferous tubules, Because the enzyme was found in the medium conditioned by spermatocytes and spermatids and in the acrosome during spermatozoa formation, together these observations suggested an involvement of this exometallopeptidase in the secretory pathway, It is concluded that this ubiquitous enzyme may be Involved in multiple processing mechanisms. [References: 45]
机译：预先从大鼠睾丸提取物中纯化出氨肽酶B（Ap-B），使其具有同质性，并进行表征。在本工作中，通过使用基于纯Ap-B的部分氨基酸微序列和PCR技术选择的寡核苷酸，获得了一个2.2kb的cDNA，推导的氨基酸序列对应于648个残基蛋白质（72.3 kDa），含有规范的``HEXXHX（18）E''签名，从而使其可以分类为MI家族的成员。金属肽酶，与白三烯-A（4）水解酶具有33％的同一性和48％的相似性，Ap-B水解白三烯A（4）的能力进一步支持了这种关系。两种酶还与盘基网柄菌的部分测序蛋白密切相关，该蛋白可能构成了氨肽酶或肽水解酶的推定共同祖先，或者在种系和Sertoli和Sertoli中检测到了Ap-B及其mRNA。由于精子形成过程中在精子细胞和精子调节的培养基中以及顶体中发现了该酶，因此这些发现共同表明这种外金属肽酶参与了分泌途径，因此得出结论，这种遍在酶可能是存在的。参与多种处理机制。 [参考：45]

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