Exchange of the valine 2-H in the biosynthesis of L-δ-(α-aminoadipoyl)-L-Cysteinyl-D-valine
✍ Scribed by Jack E. Baldwin; Michael F. Byford; Robert A. Field; Chia-Yang Shiau; Wendy J. Sobey; Christopher J. Schofield
- Publisher
- Elsevier Science
- Year
- 1993
- Tongue
- French
- Weight
- 423 KB
- Volume
- 49
- Category
- Article
- ISSN
- 0040-4020
No coin nor oath required. For personal study only.
✦ Synopsis
Incubanon of [2-2H]-valme with punfled ACV synthetase from both Cephalosporlum acremontum and Streptomyces clavulrgerus produced L-&(a-ammoadqoyl)-L-cystemyl-D-vahne (ACV), determmed by the essentzilly complete (>95%) loss of deutenum from the a posmon of the Incorporated vahne Incubations with deutermm oxide/water as solvent produced ACV Hnth slgmficant mcorporatton of deutermm mto the valmyl residue These observations confirm the prior proposal that a single mulafuncttonal enzyme IS responsible for both the formatton of the peptlde bonds of ACV and the eplmensanon of the valmyl residue
📜 SIMILAR VOLUMES
cysteinyl-D-valine (ACV) is a key intermediate in the biosynthesis pathway of penicillins and cephalosporins. Therefore, the accurate quantification of ACV is relevant, e.g. for kinetic studies on the production of these b-lactam antibiotics. However, accurate quantification of ACV is a challenge, b
## Abstract A new tripeptide, L‐α‐aminoadipyl‐L‐seryl‐D‐valine has been synthesized by coupling the protected L‐seryl‐D‐valine dipeptide with an appropriately protected L‐α‐aminoadipic acid ester. The free tripeptide was obtained after treatment with liquid HF and purification by HPLC.