EC Number | Activating Compound | Comment | Organism | Structure |
---|---|---|---|---|
1.21.3.1 | O2 | required | Penicillium chrysogenum | |
1.21.3.1 | O2 | required | Acremonium chrysogenum |
EC Number | Cloned (Comment) | Organism |
---|---|---|
1.21.3.1 | expression in Escherichia coli | Acremonium chrysogenum |
EC Number | Inhibitors | Comment | Organism | Structure |
---|---|---|---|---|
1.21.3.1 | alpha-aminoadipic(-Cys-Gly) | - |
Acremonium chrysogenum | |
1.21.3.1 | alpha-aminoadipic(-Cys-Gly) | - |
Penicillium chrysogenum | |
1.21.3.1 | bis[alpha-aminoadipic(-Cys-D-chloroalanine)] | - |
Acremonium chrysogenum | |
1.21.3.1 | bis[alpha-aminoadipic(-Cys-D-chloroalanine)] | - |
Penicillium chrysogenum | |
1.21.3.1 | bis[alpha-aminoadipic(-Cys-D-hexafluorovaline)] | - |
Acremonium chrysogenum | |
1.21.3.1 | bis[alpha-aminoadipic(-Cys-D-hexafluorovaline)] | - |
Penicillium chrysogenum | |
1.21.3.1 | bis[alpha-aminoadipic(-Cys-D-Phe)] | - |
Acremonium chrysogenum | |
1.21.3.1 | bis[alpha-aminoadipic(-Cys-D-Phe)] | - |
Penicillium chrysogenum | |
1.21.3.1 | bis[alpha-aminoadipic(-Cys-D-Trp)] | - |
Acremonium chrysogenum | |
1.21.3.1 | bis[alpha-aminoadipic(-Cys-D-Trp)] | - |
Penicillium chrysogenum | |
1.21.3.1 | bis[alpha-aminoadipic(-Cys-D-Tyr)] | - |
Acremonium chrysogenum | |
1.21.3.1 | bis[alpha-aminoadipic(-Cys-D-Tyr)] | - |
Penicillium chrysogenum | |
1.21.3.1 | bis[alpha-aminoadipic(-Cys-DL-hexafluorovaline)] | - |
Acremonium chrysogenum | |
1.21.3.1 | bis[alpha-aminoadipic(-Cys-DL-hexafluorovaline)] | - |
Penicillium chrysogenum | |
1.21.3.1 | bis[alpha-aminoadipic(-Cys-hexafluorovaline)] | - |
Acremonium chrysogenum | |
1.21.3.1 | bis[alpha-aminoadipic(-Cys-hexafluorovaline)] | - |
Penicillium chrysogenum | |
1.21.3.1 | bis[H-Cys-D-Val] | - |
Acremonium chrysogenum | |
1.21.3.1 | bis[H-Cys-D-Val] | - |
Penicillium chrysogenum | |
1.21.3.1 | additional information | conversion of the D-valine residue in third position of the enzyme to an aromatic amino acid or to a highly electronegative residue such as trifluorovaline results in elimination of substrate activity and creation of an inhibitor | Acremonium chrysogenum | |
1.21.3.1 | additional information | conversion of the D-valine residue in third position of the enzyme to an aromatic amino acid or to a highly electronegative residue such as trifluorovaline results in elimination of substrate activity and creation of an inhibitor | Penicillium chrysogenum |
EC Number | Natural Substrates | Organism | Comment (Nat. Sub.) | Natural Products | Comment (Nat. Pro.) | Rev. | Reac. |
---|---|---|---|---|---|---|---|
1.21.3.1 | N-[(5S)-5-amino-5-carboxypentanoyl]-L-cysteinyl-D-valine + O2 | Penicillium chrysogenum | common step in the biosynthesis of penicillins, cephalosporins and cephamycins | isopenicillin N + 2 H2O | - |
? | |
1.21.3.1 | N-[(5S)-5-amino-5-carboxypentanoyl]-L-cysteinyl-D-valine + O2 | Acremonium chrysogenum | common step in the biosynthesis of penicillins, cephalosporins and cephamycins | isopenicillin N + 2 H2O | - |
? | |
1.21.3.1 | N-[(5S)-5-amino-5-carboxypentanoyl]-L-cysteinyl-D-valine + O2 | Penicillium chrysogenum | modifications of the L-cysteine residue in the second position of the enzyme result in tripeptides that are unable to serve as substrates | isopenicillin N + 2 H2O | - |
? | |
1.21.3.1 | N-[(5S)-5-amino-5-carboxypentanoyl]-L-cysteinyl-D-valine + O2 | Acremonium chrysogenum | modifications of the L-cysteine residue in the second position of the enzyme result in tripeptides that are unable to serve as substrates | isopenicillin N + 2 H2O | - |
? |
EC Number | Organism | UniProt | Comment | Textmining |
---|---|---|---|---|
1.21.3.1 | Acremonium chrysogenum | - |
i.e. Acremonium chrysogenum | - |
1.21.3.1 | Penicillium chrysogenum | - |
- |
- |
EC Number | Purification (Comment) | Organism |
---|---|---|
1.21.3.1 | - |
Penicillium chrysogenum |
1.21.3.1 | recombinant from Escherichia coli | Acremonium chrysogenum |
EC Number | Substrates | Comment Substrates | Organism | Products | Comment (Products) | Rev. | Reac. |
---|---|---|---|---|---|---|---|
1.21.3.1 | N-[(5S)-5-amino-5-carboxypentanoyl]-L-cysteinyl-D-valine + O2 | - |
Penicillium chrysogenum | isopenicillin N + 2 H2O | - |
? | |
1.21.3.1 | N-[(5S)-5-amino-5-carboxypentanoyl]-L-cysteinyl-D-valine + O2 | - |
Acremonium chrysogenum | isopenicillin N + 2 H2O | - |
? | |
1.21.3.1 | N-[(5S)-5-amino-5-carboxypentanoyl]-L-cysteinyl-D-valine + O2 | common step in the biosynthesis of penicillins, cephalosporins and cephamycins | Penicillium chrysogenum | isopenicillin N + 2 H2O | - |
? | |
1.21.3.1 | N-[(5S)-5-amino-5-carboxypentanoyl]-L-cysteinyl-D-valine + O2 | common step in the biosynthesis of penicillins, cephalosporins and cephamycins | Acremonium chrysogenum | isopenicillin N + 2 H2O | - |
? | |
1.21.3.1 | N-[(5S)-5-amino-5-carboxypentanoyl]-L-cysteinyl-D-valine + O2 | modifications of the L-cysteine residue in the second position of the enzyme result in tripeptides that are unable to serve as substrates | Penicillium chrysogenum | isopenicillin N + 2 H2O | - |
? | |
1.21.3.1 | N-[(5S)-5-amino-5-carboxypentanoyl]-L-cysteinyl-D-valine + O2 | modifications of the L-cysteine residue in the second position of the enzyme result in tripeptides that are unable to serve as substrates | Acremonium chrysogenum | isopenicillin N + 2 H2O | - |
? |
EC Number | Synonyms | Comment | Organism |
---|---|---|---|
1.21.3.1 | IPNS | - |
Penicillium chrysogenum |
1.21.3.1 | IPNS | - |
Acremonium chrysogenum |