N‐terminal amino acid sequence and some properties of isopenicillin‐N synthetase from Cephalosporium acremonium

FEBS Letters

Gagnon, Jean¹  Baldwin, Jack E.²  Ting, Hong-hoi² 

[1] MRC Immunology Unit, University of Oxford South Parks Road. Oxford OX1 3QU, England;Dyson Perrins Laboratory, University of Oxford, South Parks Road, Oxford OX1 3QY, England

关键词: Cephalosporium;    Isopenicillin-N synthetase;    Amino acid sequence;    IPNS isopenicillin-N synthetase;    FPLC;    fast protein liquid chromatography;    SDS-PAGE;    SDS-polyacrylamide gel electrophoresis;   

DOI  :  10.1016/0014-5793(85)80382-3

学科分类：生物化学/生物物理

来源: John Wiley & Sons Ltd.

【 摘 要 】

Isopenicillin-N synthetase (IPNS) was purified to homogeneity from Cephalosporium acremonium C0728. The enzyme existed in two states during purification; an oxidised state with a disulphide linkage and its reduced state. These two forms can be interconverted in the presence or absence of thiol agents, and separated by fast protein liquid chromatography (FPLC) with the strong anion exchange Mono-Q column. The enzyme is a monomer with a molecular mass of 38 kDa and pI 5.05. The first 50 amino acid N-terminal sequence of the enzyme was determined. The purified enzyme has an absolute requirement of Fe²⁺ and a 2-electron donor for activity.

【 授权许可】

Unknown