δ‐l‐(α‐Aminoadipoyl)‐l‐cysteinyl‐d‐valine synthetase: isolation of l‐cysteinyl‐d‐valine, a ‘shunt’ product, and implications for the order of peptide bond formation

FEBS Letters

Shiau, Chia-Yang¹  Byford, Michael F.¹  Schofield, Christopher J.¹  Baldwin, Jack E.¹ 

[1] The Dyson Perrins Laboratory and Oxford Centre for Molecular Sciences, South Parks Road, Oxford OX1 3QY, UK

关键词: Antibiotic;    Biosynthesis;    β-Lactam;    Peptide synthetase;    Cephalosporium acremonium;   

DOI  :  10.1016/0014-5793(95)01045-G

学科分类：生物化学/生物物理

来源: John Wiley & Sons Ltd.

【 摘 要 】

l-Cysteinyl-d-valine was isolated from incubations of l-glutamate, l-cysteine and l-valine with δ-l-(α-aminoadipoyl)-l-cysteinyl-d-valine synthetase and identified by ¹H NMR and electrospray ionization MS. This is entirely consistent with our prior proposal (Shiau, C.-Y., Baldwin, J.E., Byford, M.F., Sobey, W.J. and Schofield, C.J. (1995) FEBS Lett. 358, 97–100) that the α-peptide bond between cysteine and valine is formed before the δ-peptide bond between α-aminoadipate and cysteine. The inclusion of l-glutamate, an analogue of l-α-aminoadipate, did not result in a detectable amount of tripeptide product, but did increase apparent yields of l-cysteinyl-d-valine. Conceivably, formation of the l-glutamyladenylate stimulates synthesis of the cysteinyl-valine dipeptide indirectly via a conformational change in the enzyme.

【 授权许可】

Unknown