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 isopenicillin N synthase with delta-(L-alpha-aminoadipoyl)-L-cysteinyl-D-methionine reveals thioether coordination to iron (2011), Arch. Biochem. Biophys., 516, 103-107.

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Crystallization (Commentary)

Crystallization (Comment)	Organism
crystal structure of the enzyme in complex with substrate analoge delta-(L-alpha-aminoadipoyl)-L-cysteinyl-D-methionine and Fe(II) at 1.40 A resolution reveals that the compound binds in the active site such that the sulfur atom of the methionine thioether binds to iron in the oxygen binding site at a distance of 2.57 A. The sulfur of the cysteinyl thiolate sits 2.36 A from the metal	Aspergillus nidulans

Inhibitors

Inhibitors	Comment	Organism	Structure
delta-(L-alpha-aminoadipoyl)-L-cysteinyl-D-methionine	substrate analogue, which incorporates a thioether in place of the valinyl sidechain. Crystal structure of the enzyme in complex with the compound and Fe(II) at 1.40 A resolution reveals that the compound binds in the active site such that the sulfur atom of the methionine thioether binds to iron in the oxygen binding site at a distance of 2.57 A. The sulfur of the cysteinyl thiolate sits 2.36 A from the metal	Aspergillus nidulans

Organism

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

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Release 2023.1 (January 2023)