Literature summary for 1.21.3.1 extracted from

Daruzzaman, A.; Clifton, I.J.; Adlington, R.M.; Baldwin, J.E.; Rutledge, P.J.
The interaction of isopenicillin N synthase with homologated substrate analogues delta-(L-alpha-aminoadipoyl)-L-homocysteinyl-D-Xaa characterised by protein crystallography (2013), ChemBioChem, 14, 599-606.

Cloned(Commentary)

Cloned (Comment)	Organism
-	Aspergillus nidulans

Crystallization (Commentary)

Crystallization (Comment)	Organism
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

Crystallization (Comment)

Organism

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

Organism	UniProt	Comment	Textmining
Aspergillus nidulans	P05326	-	-
Aspergillus nidulans ATCC 38163	P05326	-	-

Substrates and Products (Substrate)

Substrates	Comment Substrates	Organism	Products	Comment (Products)	Rev.
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	?