Cloned (Comment) | Organism |
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Aspergillus nidulans |
Crystallization (Comment) | Organism |
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in complex with substrate homologues delta-(L-alpha-aminoadipoyl)-L-homocysteinyl-D-valine and delta-(L-alpha-aminoadipoyl)-L-homocysteinyl-delta-S-methylcysteine. The complex with Fe(II) and delta-(L-alpha-aminoadipoyl)-L-homocysteinyl-D-valine shows diffuse electron density for several regions of the substrate, revealing considerable conformational freedom within the active site. The substrate is more clearly resolved in the complex delta-(L-alpha-aminoadipoyl)-L-homocysteinyl-delta-S-methylcysteine by virtue of thioether coordination to iron. delta-(L-alpha-aminoadipoyl)-L-homocysteinyl-delta-S-methylcysteine occupies two distinct conformations, both distorted relative to the natural substrate (L-alha-aminoadipoyl)-L-cysteinyl-D-valine, in order to accommodate the extra methylene group in the second residue | Aspergillus nidulans |
Organism | UniProt | Comment | Textmining |
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Aspergillus nidulans | P05326 | - |
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Aspergillus nidulans ATCC 38163 | P05326 | - |
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Substrates | Comment Substrates | Organism | Products | Comment (Products) | Rev. | Reac. |
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delta-(L-alpha-aminoadipoyl)-L-homocysteinyl-D-cysteine + O2 | - |
Aspergillus nidulans | (4S,7S)-7-[[(5S)-5-amino-5-carboxypentanoyl]amino]-6-oxohexahydropyrrolo[2,1-c][1,2,4]dithiazine-4-carboxylic acid + 2 H2O | product is a bicyclic gamma-lactam disulfide | ? | |
delta-(L-alpha-aminoadipoyl)-L-homocysteinyl-D-cysteine + O2 | - |
Aspergillus nidulans ATCC 38163 | (4S,7S)-7-[[(5S)-5-amino-5-carboxypentanoyl]amino]-6-oxohexahydropyrrolo[2,1-c][1,2,4]dithiazine-4-carboxylic acid + 2 H2O | product is a bicyclic gamma-lactam disulfide | ? | |
delta-(L-alpha-aminoadipoyl)-L-homocysteinyl-D-valine + O2 | - |
Aspergillus nidulans | (2S)-2-amino-6-([(3S)-1-[(1R)-1-carboxy-2-methylpropyl]-5-hydroxy-2-oxopyrrolidin-3-yl]mino)-6-oxohexanoic acid + ? | enzyme converts the homologated tripeptides delta-(L-alpha-aminoadipoyl)-L-homocysteinyl-D-valine and delta-(L-alpha-aminoadipoyl)-L-homocysteinyl-D-allylglycine into monocyclic hydroxy-lactam products, suggesting that the additional methylene unit in these substrates induces conformational changes that preclude second ring closure after initial lactam formation | ? | |
delta-(L-alpha-aminoadipoyl)-L-homocysteinyl-D-valine + O2 | - |
Aspergillus nidulans ATCC 38163 | (2S)-2-amino-6-([(3S)-1-[(1R)-1-carboxy-2-methylpropyl]-5-hydroxy-2-oxopyrrolidin-3-yl]mino)-6-oxohexanoic acid + ? | enzyme converts the homologated tripeptides delta-(L-alpha-aminoadipoyl)-L-homocysteinyl-D-valine and delta-(L-alpha-aminoadipoyl)-L-homocysteinyl-D-allylglycine into monocyclic hydroxy-lactam products, suggesting that the additional methylene unit in these substrates induces conformational changes that preclude second ring closure after initial lactam formation | ? | |
delta-(L-alpha-aminoadipoyl)-L-homocysteinyl-delta-S-methylcysteine + O2 | - |
Aspergillus nidulans | ? | enzyme converts the homologated tripeptides delta-(L-alpha-aminoadipoyl)-L-homocysteinyl-D-valine and delta-(L-alpha-aminoadipoyl)-L-homocysteinyl-D-allylglycine into monocyclic hydroxy-lactam products, suggesting that the additional methylene unit in these substrates induces conformational changes that preclude second ring closure after initial lactam formation | ? | |
delta-(L-alpha-aminoadipoyl)-L-homocysteinyl-delta-S-methylcysteine + O2 | - |
Aspergillus nidulans ATCC 38163 | ? | enzyme converts the homologated tripeptides delta-(L-alpha-aminoadipoyl)-L-homocysteinyl-D-valine and delta-(L-alpha-aminoadipoyl)-L-homocysteinyl-D-allylglycine into monocyclic hydroxy-lactam products, suggesting that the additional methylene unit in these substrates induces conformational changes that preclude second ring closure after initial lactam formation | ? |