Literature summary extracted from

Albert, A.; Dhanaraj, V.; Genschel, U.; Khan, G.; Ramjee, M.K.; Pulido, R.; Sibanda, B.L.; von Delft, F.; Witty, M.; Blundell, T.L.; Smith, A.G.; Abell, C.
Crystal structure of aspartate decarboxylase at 2.2 A resolution provides evidence for an ester in protein self-processing (1998), Nat. Struct. Biol., 5, 289-293.

Activating Compound

EC Number	Activating Compound	Comment	Organism	Structure
4.1.1.11	Pyruvoyl group	catalytic pyruvoyl groups at three active sites and an ester at the fourth. The ester is an intermediate in the autocatalytic self-processing leading to formation of the pyruvoyl group	Escherichia coli

Crystallization (Commentary)

EC Number	Crystallization (Comment)	Organism
4.1.1.11	crystal structure at 2.2. A resolution	Escherichia coli

Organism

EC Number	Organism	UniProt	Comment	Textmining
4.1.1.11	Escherichia coli	-	-	-

Substrates and Products (Substrate)

EC Number	Substrates	Comment Substrates	Organism	Products	Comment (Products)	Rev.	Reac.
4.1.1.11	L-Aspartate	-	Escherichia coli	beta-Ala + CO2	-	?

Subunits

EC Number	Subunits	Comment	Organism
4.1.1.11	tetramer	crystallographic data. Tetramer with pseudofour-fold rotational symmetry. The subunits are six-stranded beta-barrels capped by small alpha-helices at each end. The active sites are located between adjacent subunits	Escherichia coli

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Release 2023.1 (January 2023)