Literature summary for 4.1.3.1 extracted from

Britton, K.L.; Abeysinghe, I.S.B.; Baker, P.J.; Barynin, V.; Diehl, P.; Langridge, S.J.; McFadden, B.A.; Sedelnikova, S.E.; Stillman, T.J.; Weeradechapon, K.; Rice, D.W.
The structure and domain organization of Escherichia coli isocitrate lyase (2001), Acta Crystallogr. Sect. D, D57, 1209-1218.

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Crystallization (Commentary)

Crystallization (Comment)	Organism
hanging drop vapor diffusion method	Escherichia coli

Protein Variants

Protein Variants	Comment	Organism
A219C	similar catalytic properties as the wild-type enzyme	Escherichia coli

Localization

Localization	Comment	Organism	GeneOntology No.	Textmining
cytoplasm	-	Escherichia coli	5737	-

Natural Substrates/ Products (Substrates)

Natural Substrates	Organism	Comment (Nat. Sub.)	Natural Products	Comment (Nat. Pro.)	Rev.	Reac.
isocitrate	Escherichia coli	first step in glyoxylate-bypass pathway	succinate + glyoxylate	-	?

Organism

Organism	UniProt	Comment	Textmining
Escherichia coli	-	-	-

Purification (Commentary)

Purification (Comment)	Organism
-	Escherichia coli

Substrates and Products (Substrate)

Substrates	Comment Substrates	Organism	Products	Comment (Products)	Rev.	Reac.
isocitrate	-	Escherichia coli	succinate + glyoxylate	-	?
isocitrate	first step in glyoxylate-bypass pathway	Escherichia coli	succinate + glyoxylate	-	?

Subunits

Subunits	Comment	Organism
tetramer	monomers are identical, crystallization experiments	Escherichia coli

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Release 2023.1 (January 2023)