Literature summary extracted from

Britton, K.; Langridge, S.; Baker, P.J.; Weeradechapon, K.; Sedelnikova, S.E.; De Lucas, J.R.; Rice, D.W.; Turner, G.
The crystal structure and active site location of isocitrate lyase from the fungus Aspergillus nidulans (2000), Structure, 8, 349-362.

Application

EC Number	Application	Comment	Organism
4.1.3.1	medicine	enzyme provides a potential target for drug design aimed at the control of parasitic infections	Aspergillus nidulans

Crystallization (Commentary)

EC Number	Crystallization (Comment)	Organism
4.1.3.1	complexed with glyoxylate and a divalent cation	Aspergillus nidulans

Metals/Ions

EC Number	Metals/Ions	Comment	Organism	Structure
4.1.3.1	Mg2+	dependent	Aspergillus nidulans

Natural Substrates/ Products (Substrates)

EC Number	Natural Substrates	Organism	Comment (Nat. Sub.)	Natural Products	Comment (Nat. Pro.)	Rev.	Reac.
4.1.3.1	isocitrate	Aspergillus nidulans	-	succinate + glyoxylate	-	r

Organism

EC Number	Organism	UniProt	Comment	Textmining
4.1.3.1	Aspergillus nidulans	-	-	-

Substrates and Products (Substrate)

EC Number	Substrates	Comment Substrates	Organism	Products	Comment (Products)	Rev.	Reac.
4.1.3.1	isocitrate	-	Aspergillus nidulans	succinate + glyoxylate	-	r

Subunits

EC Number	Subunits	Comment	Organism
4.1.3.1	tetramer	crystallization experiments	Aspergillus nidulans

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Release 2023.1 (January 2023)