来自淡紫青霉IBT 3991的羧肽酶S3的一级结构。

The primary structure of carboxypeptidase S3 from Penicillium janthinellum IBT 3991.

作者信息

Svendsen I, Day E S

机构信息

Carlsberg Laboratory, Department of Chemistry, Copenhagen, Denmark.

出版信息

FEBS Lett. 1995 Aug 28;371(1):1-3. doi: 10.1016/0014-5793(95)00840-6.

DOI:10.1016/0014-5793(95)00840-6

PMID:7664873

Abstract

The complete amino acid sequence of penicillopeptidase S3, a serine carboxypeptidase isolated from Penicillium janthinellum IBT 3991, has been determined. The enzyme consists of 481 amino acids arranged in a single polypeptide chain. Six glycosylation sites were established in positions 41, 218, 256, 326, 384 and 392. The molecule contains six cysteinyl residues among which disulfide bridges was established between Cys-71-Cys-333 and Cys-233-Cys-289. Carboxypeptidase S3 is homologous to carboxypeptidase PEPF (or carboxypeptidase I) from Aspergillus niger (67% identical positions). It is proposed that these enzymes form a separate sub-family among the serine carboxypeptidases.

摘要

已确定从产黄青霉IBT 3991中分离出的丝氨酸羧肽酶——青霉素肽酶S3的完整氨基酸序列。该酶由481个氨基酸组成，排列在一条单一的多肽链中。在第41、218、256、326、384和392位确定了六个糖基化位点。该分子含有六个半胱氨酸残基，其中在Cys-71-Cys-333和Cys-233-Cys-289之间形成了二硫键。羧肽酶S3与黑曲霉的羧肽酶PEPF（或羧肽酶I）同源（相同位置为67%）。有人提出，这些酶在丝氨酸羧肽酶中形成一个单独的亚家族。