2. Academic Validation
  3. δ-(L-α-aminoadipyl)-L-cysteinyl-D-valine synthetase (ACVS): discovery and perspectives

δ-(L-α-aminoadipyl)-L-cysteinyl-D-valine synthetase (ACVS): discovery and perspectives

  • J Ind Microbiol Biotechnol. 2017 May;44(4-5):517-524. doi: 10.1007/s10295-016-1850-7.
Kapil Tahlan 1,  Marcus A Moore 2,  Susan E Jensen 3
Affiliations

Affiliations

  • 1 Department of Biology, Memorial University of Newfoundland, St. John's, NL, A1B 3X9, Canada. [email protected].
  • 2 Department of Biology, Memorial University of Newfoundland, St. John's, NL, A1B 3X9, Canada.
  • 3 Department of Biological Sciences, University of Alberta, Edmonton, AB, T6G 2E9, Canada.
PMID: 27766439 DOI: 10.1007/s10295-016-1850-7
Abstract

The δ-(L-α-aminoadipyl)-L-cysteinyl-D-valine (ACV) tripeptide is the first dedicated intermediate in the biosynthetic pathway leading to the penicillin and cephalosporin classes of β-lactam natural products in bacteria and fungi. It is synthesized nonribosomally by the ACV synthetase (ACVS) enzyme, which has been purified and partially characterized from many sources. Due to its large size and instability, many details regarding the reaction mechanism of ACVS are still not fully understood. In this review we discuss the chronology and associated methodology that led to the discovery of ACVS, some of the main findings regarding its activities, and some recent/current studies being conducted on the enzyme. In addition, we conclude with perspectives on what can be done to increase our understating of this very important protein in the future.

Keywords

ACVS; Cephalosporin; Penicillin; Protein purification; Streptomyces; β-lactams.

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