EC Number   |
Substrates |
Organism |
Products |
Reversibility |
|---|
   1.21.3.1 | 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 |
? |
| 1.21.3.1 | 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 |
? |
| 1.21.3.1 | 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 |
? |
| 1.21.3.1 | 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 |
? |
| 1.21.3.1 | 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 |
? |
| 1.21.3.1 | 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 |
? |
| 1.21.3.1 | delta-(L-alpha-aminoadipyl)-L-cysteinyl-D-alpha-aminobutyrate + O2 |
wild-type and mutants, reaction mechanism |
Aspergillus nidulans |
? |
- |
ir |
| 1.21.3.1 | delta-(L-alpha-aminoadipyl)-L-cysteinyl-D-valine + O2 |
- |
Flavobacterium sp. |
isopenicillin N + H2O |
- |
r |
| 1.21.3.1 | delta-(L-alpha-aminoadipyl)-L-cysteinyl-D-valine + O2 |
- |
Amycolatopsis lactamdurans |
isopenicillin N + H2O |
- |
r |
| 1.21.3.1 | delta-(L-alpha-aminoadipyl)-L-cysteinyl-D-valine + O2 |
- |
Flavobacterium sp. SC 12.154 |
isopenicillin N + H2O |
- |
r |
