Cloned (Comment) | Organism |
---|---|
- |
Aspergillus nidulans |
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 | Comment | Organism | Structure |
---|---|---|---|
delta-(L-alpha-aminoadipoyl)-L-cysteinyl-O-methyl-D-threonine | substrate analogue, not turned over by IPNS | Aspergillus nidulans |
Organism | UniProt | Comment | Textmining |
---|---|---|---|
Aspergillus nidulans | P05326 | - |
- |
Aspergillus nidulans ATCC 38163 | P05326 | - |
- |
Substrates | Comment Substrates | Organism | Products | Comment (Products) | Rev. | Reac. |
---|---|---|---|---|---|---|
delta-(L-alpha-aminoadipoyl)-L-cysteinyl-O-methyl-D-allo-threonine + O2 | - |
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 | ? |