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Isolation and structure elucidation of an α‐amylase inhibitor, AI‐3688, from Streptomyces aureofaciens
Author(s) -
Vértesy L.,
Tripier D.
Publication year - 1985
Publication title -
febs letters
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.593
H-Index - 257
eISSN - 1873-3468
pISSN - 0014-5793
DOI - 10.1016/0014-5793(85)80767-5
Subject(s) - edman degradation , streptomyces aureofaciens , streptomyces , biochemistry , peptide sequence , amylase , peptide , protein primary structure , stereochemistry , biology , active site , chemistry , enzyme , genetics , bacteria , gene
A novel polypeptide inhibitor, AI‐3688, which acts upon human pancreatic α‐amylase, was isolated from fermentation broth of Streptomyces aureofaciens . The purified peptide contains no unusual amino acids. Its M r is 3936. The primary structure of AI‐3688 was elucidated by automatic Edman degradation of the native or modified inhibitor. Two intramolecular cysteines form a disulphide bridge, thus creating a ring structure consisting of 17 amino acids. Strong sequence homology also exists to another microbial α‐amylase inhibitor, tendamistat (HOE 467). This paper discusses the role of a common partial sequence, ‐Gln‐Ser‐Trp‐Arg‐Tyr‐, present in the loop of both inhibitors as the active site of microbial peptide α‐amylase inhibitors.