Open AccessConversion of phenylacetyl‐cysteinyl‐valine in vitro into penicillin G by isopenicillin N synthase of Streptomyces lactamdurans
Author(s) -
Castro JoséM.,
Liras Paloma,
Cortés Jesús,
Martín Juan F.
Publication year - 1986
Publication title -
fems microbiology letters
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 0.899
H-Index - 151
eISSN - 1574-6968
pISSN - 0378-1097
DOI - 10.1111/j.1574-6968.1986.tb01435.x
Subject(s) - valine , penicillin , streptomyces , dithiothreitol , biochemistry , stereochemistry , enzyme , chemistry , biosynthesis , amino acid , biology , antibiotics , bacteria , genetics
Purified isopenicillin N synthase of Streptomyces lactamdurans JC1843 converted phenylacetyl‐cysteinyl‐valine, a structural analogue of the natural substrate (α‐amino‐adipyl‐cysteinyl‐valine), into a penicillinase‐sensitive β‐lactam antibiotic. The antibiotic was identified as penicillin G by HPLC. Cyclization of phenylacetyl cysteinylvaline into penicillin G required dithiothreitol (DTT), ascorbic acid and Fe 2+ . The affinity of the enzyme for phenylacetyl cysteinylvaline was about 20 times lower than the affinity for α‐aminoadipyl‐cysteinyl‐valine.