EC Number |
Reaction |
Reference |
---|
1.21.3.1 | N-[(5S)-5-amino-5-carboxypentanoyl]-L-cysteinyl-D-valine + O2 = isopenicillin N + 2 H2O |
active site with conserved jelly-roll motif, cysteine residues are not directly involved in the coordination of the metal ion |
440320 |
1.21.3.1 | N-[(5S)-5-amino-5-carboxypentanoyl]-L-cysteinyl-D-valine + O2 = isopenicillin N + 2 H2O |
catalytic reaction is under steric regulation |
440325 |
1.21.3.1 | N-[(5S)-5-amino-5-carboxypentanoyl]-L-cysteinyl-D-valine + O2 = isopenicillin N + 2 H2O |
Cys106 is involved in substrate binding, Cys255 is involved in maintaining the protein structure |
440317 |
1.21.3.1 | N-[(5S)-5-amino-5-carboxypentanoyl]-L-cysteinyl-D-valine + O2 = isopenicillin N + 2 H2O |
isopenicillin-N synthase is the main rate-limiting enzyme for penicillin-G biosynthesis |
714549 |
1.21.3.1 | N-[(5S)-5-amino-5-carboxypentanoyl]-L-cysteinyl-D-valine + O2 = isopenicillin N + 2 H2O |
ligation of substrate to the iron centre |
440322 |
1.21.3.1 | N-[(5S)-5-amino-5-carboxypentanoyl]-L-cysteinyl-D-valine + O2 = isopenicillin N + 2 H2O |
radical pathway, analogous to the first step of a radicalbased hydroxylation reaction |
672246 |
1.21.3.1 | N-[(5S)-5-amino-5-carboxypentanoyl]-L-cysteinyl-D-valine + O2 = isopenicillin N + 2 H2O |
removal of 4 hydrogen atoms to form the 4-membered beta-lactam and the 5-membered thiazolidine ring |
440314 |
1.21.3.1 | N-[(5S)-5-amino-5-carboxypentanoyl]-L-cysteinyl-D-valine + O2 = isopenicillin N + 2 H2O |
structure and mechanism |
440320, 440322, 440323, 440325 |
1.21.3.1 | N-[(5S)-5-amino-5-carboxypentanoyl]-L-cysteinyl-D-valine + O2 = isopenicillin N + 2 H2O |
the hydroperoxide-ferrous intermediate, formed by O2-activated H atom abstraction from the substrate, can exploit different reaction pathways and interactions with the substrate govern the final pathway |
714183 |