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Literature summary extracted from

  • Huffman, G.W.; Gesellchen, P.D.; Turner, J.R.; Rothenberger, R.B.; Osborne, H.E.; Miller, F.D.; Chapman, J.L.; Queener, S.W.
    Substrate specificity of isopenicillin N synthase (1992), J. Med. Chem., 35, 1897-1914.
    View publication on PubMed

Activating Compound

EC Number Activating Compound Comment Organism Structure
1.21.3.1 O2 required Penicillium chrysogenum
1.21.3.1 O2 required Acremonium chrysogenum

Cloned(Commentary)

EC Number Cloned (Comment) Organism
1.21.3.1 expression in Escherichia coli Acremonium chrysogenum

Inhibitors

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

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 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
-
 ?

Organism

EC Number Organism UniProt Comment Textmining
1.21.3.1 Acremonium chrysogenum
-
 i.e. Acremonium chrysogenum
-
1.21.3.1 Penicillium chrysogenum
-
-
-

Purification (Commentary)

EC Number Purification (Comment) Organism
1.21.3.1
-
 Penicillium chrysogenum
1.21.3.1 recombinant from Escherichia coli Acremonium chrysogenum

Substrates and Products (Substrate)

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
-
 ?

Synonyms

EC Number Synonyms Comment Organism
1.21.3.1 IPNS
-
 Penicillium chrysogenum
1.21.3.1 IPNS
-
 Acremonium chrysogenum