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Literature summary extracted from

  • Rowe, C.J.; Shorrock, C.P.; Claridge, T.D.W.; Sutherland, J.D.
    Analysis of the conversion of d-(L-alpha-aminoadipoyl)-L-cysteinyl-D-a-aminobutyrate by active-site mutants of Aspergillus nidulans isopenicillin N synthase (1998), Chem. Biol., 5, 229-239.
    View publication on PubMed

Activating Compound

EC Number Activating Compound Comment Organism Structure
1.21.3.1 ascorbic acid
-
Aspergillus nidulans
1.21.3.1 dithiothreitol
-
Aspergillus nidulans
1.21.3.1 O2 required Aspergillus nidulans

Cloned(Commentary)

EC Number Cloned (Comment) Organism
1.21.3.1 expression of wild-type and mutants as maltose-binding fusion proteins in Escherichia coli Aspergillus nidulans

Protein Variants

EC Number Protein Variants Comment Organism
1.21.3.1 L223A reduced activity with N-[(5S)-5-amino-5-carboxypentanoyl]-L-cysteinyl-D-valine, delta-(L-alpha-aminoadipoyl)-L-cysteinyl-D-alpha-aminobutyrate is a poor substrate Aspergillus nidulans
1.21.3.1 L223I reduced activity with N-[(5S)-5-amino-5-carboxypentanoyl]-L-cysteinyl-D-valine, product spectrum differs from that of the wild-type with delta-(L-alpha-aminoadipoyl)-L-cysteinyl-D-alpha-aminobutyrate as substrate Aspergillus nidulans
1.21.3.1 L223V reduced activity with N-[(5S)-5-amino-5-carboxypentanoyl]-L-cysteinyl-D-valine, product spectrum differs from that of the wild-type with delta-(L-alpha-aminoadipoyl)-L-cysteinyl-D-alpha-aminobutyrate as substrate Aspergillus nidulans

Metals/Ions

EC Number Metals/Ions Comment Organism Structure
1.21.3.1 Fe2+
-
Aspergillus nidulans

Natural Substrates/ Products (Substrates)

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 Aspergillus nidulans catalytic reaction is under steric regulation isopenicillin N + 2 H2O product has antibiotic activity ?
1.21.3.1 N-[(5S)-5-amino-5-carboxypentanoyl]-L-cysteinyl-D-valine + O2 Aspergillus nidulans common step in the biosynthesis of penicillins, cephalosporins and cephamycins isopenicillin N + 2 H2O product has antibiotic activity ?

Organism

EC Number Organism UniProt Comment Textmining
1.21.3.1 Aspergillus nidulans
-
-
-

Purification (Commentary)

EC Number Purification (Comment) Organism
1.21.3.1 recombinant wild-type and mutants from Escherichia coli Aspergillus nidulans

Reaction

EC Number Reaction Comment Organism Reaction ID
1.21.3.1 N-[(5S)-5-amino-5-carboxypentanoyl]-L-cysteinyl-D-valine + O2 = isopenicillin N + 2 H2O structure and mechanism Aspergillus nidulans
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 Aspergillus nidulans

Substrates and Products (Substrate)

EC Number Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
1.21.3.1 delta-(L-alpha-aminoadipyl)-L-cysteinyl-D-alpha-aminobutyrate + O2 wild-type and mutants, reaction mechanism Aspergillus nidulans ?
-
ir
1.21.3.1 additional information delta-(L-alpha-aminoadipoyl)-L-cysteinyl-D-alpha-aminobutyrate as substrate is converted to 3 different products: an alpha- and a beta-methyl-penam, and a cepham Aspergillus nidulans ?
-
?
1.21.3.1 N-[(5S)-5-amino-5-carboxypentanoyl]-L-cysteinyl-D-valine + O2 catalytic reaction is under steric regulation Aspergillus nidulans isopenicillin N + 2 H2O
-
?
1.21.3.1 N-[(5S)-5-amino-5-carboxypentanoyl]-L-cysteinyl-D-valine + O2 catalytic reaction is under steric regulation Aspergillus nidulans isopenicillin N + 2 H2O product has antibiotic activity ?
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 Aspergillus nidulans isopenicillin N + 2 H2O product has antibiotic activity ?

Synonyms

EC Number Synonyms Comment Organism
1.21.3.1 IPNS
-
Aspergillus nidulans

Temperature Optimum [°C]

EC Number Temperature Optimum [°C] Temperature Optimum Maximum [°C] Comment Organism
1.21.3.1 27
-
assay at Aspergillus nidulans