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首页> 外文期刊>Biochemistry >A high-affinity inhibitor of yeast carboxypeptidase Y is encoded by TFSI and shows homology to a family of lipid binding proteins
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A high-affinity inhibitor of yeast carboxypeptidase Y is encoded by TFSI and shows homology to a family of lipid binding proteins

机译：酵母羧肽酶Y的高亲和力抑制剂由TFSI编码，与脂质结合蛋白家族具有同源性

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摘要

A 25-kDa inhibitor of the vacuolar enzyme carboxypeptidase Y from Saccharomyces cerevisiae has been characterized. The inhibitor, I-c, binds tightly with an apparent K-i of 0.1 nM. Consistent with a cytoplasmic localization, I-c is soluble and contains no sequences which could serve as potential signals for transport into the endoplasmic reticulum. Surprisingly, I-c is encoded by TFS1, which has previously been isolated as a high-copy suppressor of cdc25-1. CDC25 encodes the putative GTP exchange factor for Ras1p/Ras2p in yeast. In an attempt to rationalize this finding, we looked for a physiological relationship by deleting or overexpressing the gene for carboxypeptidase Y in a cdc25-1 strain. However, this did not change the phenotype of this mutant strain. I-c is the first member of a new family of protease inhibitors. The inhibitor is not hydrolyzed on binding to CPY, It has fairly high degree of specificity, showing a 200-fold higher K-i toward a carboxypeptidase from Candida albicans which is highly homologous to carboxypeptidase Y. The TFS1 gene product shows extensive similarity to a class of proteins termed "21-23-kDa lipid binding proteins", members of which are found in several higher eukaryotes, including man. These proteins are highly abundant in some tissues (e.g., brain) and have in general been found to bind lipids. Considering their homology to I-c, it is tempting to speculate that they may also be inhibitors of serine carboxypeptidases. [References: 27]
机译：已经鉴定了来自酿酒酵母的液泡酶羧肽酶Y的25-kDa抑制剂。抑制剂I-c以0.1 nM的表观K-i紧密结合。与细胞质定位一致，I-c是可溶的，不包含任何序列，这些序列可以用作转运到内质网的潜在信号。出乎意料的是，I-c由TFS1编码，TFS1先前已被分离为cdc25-1的高复制抑制因子。 CDC25编码酵母中Ras1p / Ras2p的假定GTP交换因子。为了合理化此发现，我们通过删除或过表达cdc25-1菌株中羧肽酶Y的基因来寻找生理关系。但是，这并没有改变该突变株的表型。 I-c是蛋白酶抑制剂新家族的第一个成员。该抑制剂与CPY结合时不会水解，它具有相当高的特异性，对来自白色念珠菌的羧肽酶显示200倍的Ki，与羧肽酶Y高度同源。TFS1基因产物与一类称为“ 21-23-kDa脂质结合蛋白”的蛋白质，其成员存在于包括人在内的几种高级真核生物中。这些蛋白质在某些组织（例如脑）中高度丰富，并且通常被发现与脂质结合。考虑到它们与I-c的同源性，很容易推测它们也可能是丝氨酸羧肽酶的抑制剂。 [参考：27]

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