Isopenicillin N synthase (IPNS)

Isopenicillin N synthase (IPNS) is a non-heme iron-dependent enzyme that catalyzes the oxidative cyclization of the tripeptide δ-(L-α-aminoadipoyl)-L-cysteinyl-D-valine (ACV) to isopenicillin N. This reaction constitutes the central step in the formation of the β-lactam ring, a core structure widely found in penicillin and cephalosporin antibiotics. The enzyme acts as an oxidoreductase, coupling oxygen reduction with the cyclization of ACV, and is a member of the non-heme iron(II)-dependent oxidase superfamily, sharing mechanistic features with other 2-histidine-1-carboxylate facial triad oxygenases. IPNS is not itself a drug target or human protein, but regulation and optimization of its activity are crucial in industrial production of β-lactam antibiotics. The enzyme is sometimes referred to as isopenicillin N synthetase in older literature[1][2][3][4][5][7][8][9][10].

Other names

isopenicillin N synthetaseisopenicillin N synthase enzymeIPNSipnA