Amino acid sequence of guinea pig prostate kallikrein.
Amino acid sequence of guinea pig prostate kallikrein.
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豚鼠前列腺激肽释放酶的氨基酸序列。
DOI：
10.1021/bi00386a034
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发表时间：
1987
期刊：
影响因子：
2.9
通讯作者：
Bradshaw,RA
中科院分区：
文献类型：
--
作者：
Dunbar,JC;Bradshaw,RA
琼c Dunbar** 和Ryna. Bradshaw* 生物化学系，加州医学院，加州大学欧文分校，加州92717接收日期：1986年11月7日;修订后的手册，1987年1月7日摘要：来自豚鼠前列腺的主要精氨酸酯肽酶的一级结构已经从梭菌蛋白酶、溴化氰、内切蛋白酶Lys-C、和金黄色葡萄球菌V8蛋白酶消化的蛋白质。酯肽酶是由239个氨基酸组成的单一多肽链，并含有2个表观碳水化合物连接位点，Asn-78和Asn-169。两者都出现在N-连接糖基化位点的共有序列中。酯肽酶与胰蛋白酶具有约35%的同源性，包括催化残基的保守性和赋予对碱性氨基酸特异性的天冬氨酸。然而，与丝氨酸蛋白酶的激肽释放酶家族的序列同一性延伸至大于60%。除了整体同源性之外，豚鼠酶还显示出许多激肽释放酶的特征，包括10个保守的半胱氨酸残基、C-末端脯氨酸和“激肽释放酶环”。基于这种结构相关性，该酶被命名为豚鼠前列腺激肽释放酶。与其他物种和组织的许多激肽释放酶相反，这种酶在激肽释放酶环内不含对导致多肽链内部断裂的蛋白酶敏感的任何位点。腺激肽释放酶是酯肽酶的丝氨酸蛋白酶家族的一个独特子集（Schachter，1980）。它们优先水解由酯组成的合成底物。这项工作得到了USPHS研究赠款NS 19964和DK 32465（以前的AM 32465）的支持。信件应寄给作者。*现住址：分子生物学和遗传学系，韦恩州立大学医学院，底特律，MI 48207。以及精氨酸的酰胺和较小程度的赖氨酸（Fielder，1979）。与胰蛋白酶相反，激肽释放酶具有非常小的一般蛋白酶活性，而是显示出高度的底物选择性（Schachter，1969）。这些酶最初被定义为具有在体外从激肽原释放激肽的能力的激肽原酶。然而，激肽原酶活性在激肽释放酶家族的成员之间变化很大，并且许多酯肽酶现在已经被鉴定为kal-1。
Joan C. Dunbar** and RalphA. Bradshaw* Department of Biological Chemistry, California College of Medicine, University of California, Irvine, California 92717 Received November 7, 1986; Revised Manuscript Received January 7, 1987 abstract: The primary structure of the major arginine esteropeptidase from guinea pig prostate has been deduced from automated Edman degradation of peptides generated by clostripain, cyanogen bromide, endoproteinase Lys-C, and Staphylococcus aureus V8 protease digestion of the protein. The esteropeptidase is a single polypeptide chain comprised of 239 amino acids and contains 2 apparent sites of carbohydrate attachment, Asn-78 and Asn-169. Both occur in consensus sequences for N-linked glycosylation sites. The esteropeptidase exhibits approximately 35% homology with trypsin including conservation of the catalytic residues and the aspartic acid which confers specificity toward basic aminoacids. The sequence identity, however, extends to greater than 60% with the kallikrein family of serine proteases. In addition to the overall homology, the guinea pig enzyme displays a number of features characteristic of kallikreins including 10 conserved half-cystine residues, a C-terminal proline, and the “kallikrein loop”. On the basis of this structural relatedness, the enzyme has been designated as guinea pig prostate kallikrein. In contrast to many of the kallikreins of other species and tissues, this enzyme does not contain any sites within the kallikrein loop sensitive to proteases that result in internal breaks in the polypeptide chain.(jTlandular kallikreins are a distinct subset of the serine protease family of esteropeptidases (Schachter, 1980). They preferentially hydrolyze syntheticsubstrates composed of esters fThis work was supported by USPHS Research Grants NS 19964 and DK32465 (formerly AM32465).* Correspondence should be addressed to this author.* Present address: Department of Molecular Biology and Genetics, Wayne State University School of Medicine, Detroit, MI 48207. and amides of arginine and, to a lesser extent, lysine (Fielder, 1979). In contrastto trypsin, kallikreins have very little general protease activity but rather display a high degree of substrate selectivity (Schachter, 1969). These enzymes were originally defined as kininogenases with the capacity, in vitro, to release kinin fromkininogen. However, the kininogenase activity varies considerably among members of the kallikrein family, and many esteropeptidases have now been identified as kal-
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激肽释放酶（激肽原酶）——一组具有生物调节作用的丝氨酸蛋白酶。
影响因子：
21.1
作者：
M. Schachter
通讯作者：
M. Schachter
大鼠颌下肌张力的氨基酸序列揭示了与丝氨酸蛋白酶的相似性
影响因子：
64.8
作者：
C. Lazure;R. Leduc;N. Seidah;G. Thibault;J. Genest;M. Chrétien
通讯作者：
M. Chrétien
β-神经生长因子前体（β-神经生长因子的生物合成前体）的证据
DOI：
--
发表时间：
1977
期刊：
影响因子：
--
作者：
E. Berger;E. Shooter
通讯作者：
E. Shooter
影响因子：
4.8
作者：
R. Richards;D. Catanzaro;A. Mason;B. Morris;J. Baxter;J. Shine
通讯作者：
J. Shine
激肽释放酶多基因家族：生物活性肽的特异性加工。
DOI：
--
发表时间：
1983
期刊：
Cold Spring Harbor Symposia on Quantitative Biology
影响因子：
--
作者：
J. Shine;A. Mason;B. A. Evans;R. Richards
通讯作者：
R. Richards