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Literature summary for 1.21.3.1 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
Search for more literature for 1.21.3.1

Activating Compound

Activating Compound Comment Organism Structure
O2 required Penicillium chrysogenum
O2 required Acremonium chrysogenum

Cloned(Commentary)

Cloned (Comment) Organism
expression in Escherichia coli Acremonium chrysogenum

Inhibitors

Inhibitors Comment Organism Structure
alpha-aminoadipic(-Cys-Gly)
-
 Acremonium chrysogenum
alpha-aminoadipic(-Cys-Gly)
-
 Penicillium chrysogenum
bis[alpha-aminoadipic(-Cys-D-chloroalanine)]
-
 Acremonium chrysogenum
bis[alpha-aminoadipic(-Cys-D-chloroalanine)]
-
 Penicillium chrysogenum
bis[alpha-aminoadipic(-Cys-D-hexafluorovaline)]
-
 Acremonium chrysogenum
bis[alpha-aminoadipic(-Cys-D-hexafluorovaline)]
-
 Penicillium chrysogenum
bis[alpha-aminoadipic(-Cys-D-Phe)]
-
 Acremonium chrysogenum
bis[alpha-aminoadipic(-Cys-D-Phe)]
-
 Penicillium chrysogenum
bis[alpha-aminoadipic(-Cys-D-Trp)]
-
 Acremonium chrysogenum
bis[alpha-aminoadipic(-Cys-D-Trp)]
-
 Penicillium chrysogenum
bis[alpha-aminoadipic(-Cys-D-Tyr)]
-
 Acremonium chrysogenum
bis[alpha-aminoadipic(-Cys-D-Tyr)]
-
 Penicillium chrysogenum
bis[alpha-aminoadipic(-Cys-DL-hexafluorovaline)]
-
 Acremonium chrysogenum
bis[alpha-aminoadipic(-Cys-DL-hexafluorovaline)]
-
 Penicillium chrysogenum
bis[alpha-aminoadipic(-Cys-hexafluorovaline)]
-
 Acremonium chrysogenum
bis[alpha-aminoadipic(-Cys-hexafluorovaline)]
-
 Penicillium chrysogenum
bis[H-Cys-D-Val]
-
 Acremonium chrysogenum
bis[H-Cys-D-Val]
-
 Penicillium chrysogenum
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
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)

Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
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
-
 ?
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
-
 ?
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
-
 ?
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

Organism UniProt Comment Textmining
Acremonium chrysogenum
-
 i.e. Acremonium chrysogenum
-
Penicillium chrysogenum
-
-
-

Purification (Commentary)

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

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
N-[(5S)-5-amino-5-carboxypentanoyl]-L-cysteinyl-D-valine + O2
-
 Penicillium chrysogenum isopenicillin N + 2 H2O
-
 ?
N-[(5S)-5-amino-5-carboxypentanoyl]-L-cysteinyl-D-valine + O2
-
 Acremonium chrysogenum isopenicillin N + 2 H2O
-
 ?
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
-
 ?
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
-
 ?
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
-
 ?
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

Synonyms Comment Organism
IPNS
-
 Penicillium chrysogenum
IPNS
-
 Acremonium chrysogenum