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Literature summary for 1.21.3.1 extracted from

  • Clifton, I.J.; Ge, W.; Adlington, R.M.; Baldwin, J.E.; Rutledge, P.J.
    The crystal structure of an isopenicillin N synthase complex with an ethereal substrate analogue reveals water in the oxygen binding site (2013), FEBS Lett., 587, 2705-2709.
    View publication on PubMed
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Cloned(Commentary)

Cloned (Comment) Organism
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 Aspergillus nidulans

Crystallization (Commentary)

Crystallization (Comment) Organism
in complex with substrat analogue delta-(L-alpha-aminoadipoyl)-L-cysteinyl-O-methyl-D-threonine and Fe(II). Structure reveals an additional water molecule bound to the active site metal, held by hydrogen-bonding to the ether oxygen atom of the substrate analogue Aspergillus nidulans

Inhibitors

Inhibitors Comment Organism Structure
delta-(L-alpha-aminoadipoyl)-L-cysteinyl-O-methyl-D-threonine substrate analogue, not turned over by IPNS Aspergillus nidulans

Organism

Organism UniProt Comment Textmining
Aspergillus nidulans P05326
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Aspergillus nidulans ATCC 38163 P05326
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Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
delta-(L-alpha-aminoadipoyl)-L-cysteinyl-O-methyl-D-allo-threonine + O2
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 Aspergillus nidulans (2S,3S,5R,6R)-6-[[(5S)-5-amino-5-carboxypentanoyl]amino]-3-methoxy-3-methyl-7-oxo-4-thia-1-azabicyclo[3.2.0]heptane-2-carboxylic acid + 2 H2O product is a bioactive penam. Epimeric delta-(L-alpha-aminoadipoyl)-L-cysteinyl-O-methyl-D-threonine is not turned over by the enzyme ?
delta-(L-alpha-aminoadipoyl)-L-cysteinyl-O-methyl-D-allo-threonine + O2
-
 Aspergillus nidulans ATCC 38163 (2S,3S,5R,6R)-6-[[(5S)-5-amino-5-carboxypentanoyl]amino]-3-methoxy-3-methyl-7-oxo-4-thia-1-azabicyclo[3.2.0]heptane-2-carboxylic acid + 2 H2O product is a bioactive penam. Epimeric delta-(L-alpha-aminoadipoyl)-L-cysteinyl-O-methyl-D-threonine is not turned over by the enzyme ?