Literature summary for 4.1.1.11 extracted from

Webb, M.E.; Lobley, C.M.; Soliman, F.; Kilkenny, M.L.; Smith, A.G.; Blundell, T.L.; Abell, C.
Structure of Escherichia coli aspartate alpha-decarboxylase Asn72Ala: probing the role of Asn72 in pyruvoyl cofactor formation (2012), Acta Crystallogr. Sect. F, 68, 414-417.

Cloned(Commentary)

Cloned (Comment)	Organism
gene panD, expression of enzyme mutant N72A in Escherichia coli strain C41 (DE3)	Escherichia coli

Crystallization (Commentary)

Crystallization (Comment)	Organism
purified recombinant mutant N72A, hanging drop vapour diffusion method, mixing of 0.001 ml of 19 mg /ml protein in 50 mM Tris-HCl, pH 8.0, with 0.001 ml of reservoir solution containing 1.6 M ammonium sulfate, pH 4.0, and equilibration against 0.5 ml of reservoir solution, 19°C, 3 days, cryoprotection by 1.8 M ammonium sulfate, 0.1 M citric acid, 30% glycerol pH 4.0 using 5% increments in glycerol concentration to prevent crystal dissolution, X-ray diffraction structure determination and analysis at 1.7 A resolution	Escherichia coli

Crystallization (Comment)

Organism

purified recombinant mutant N72A, hanging drop vapour diffusion method, mixing of 0.001 ml of 19 mg /ml protein in 50 mM Tris-HCl, pH 8.0, with 0.001 ml of reservoir solution containing 1.6 M ammonium sulfate, pH 4.0, and equilibration against 0.5 ml of reservoir solution, 19°C, 3 days, cryoprotection by 1.8 M ammonium sulfate, 0.1 M citric acid, 30% glycerol pH 4.0 using 5% increments in glycerol concentration to prevent crystal dissolution, X-ray diffraction structure determination and analysis at 1.7 A resolution

Escherichia coli

Protein Variants

Protein Variants	Comment	Organism
N72A	site-directed mutagenesis, in the Asn72Ala mutant the C-terminal region residues are ordered, in contrast to the wild-type enzyme, owing to an interaction with the active site of the neighbouring symmetry-related multimer	Escherichia coli

Natural Substrates/ Products (Substrates)

Natural Substrates	Organism	Comment (Nat. Sub.)	Natural Products	Comment (Nat. Pro.)	Rev.	Reac.
L-aspartate	Escherichia coli	-	beta-alanine + CO2	-	?

Organism

Organism	UniProt	Comment	Textmining
Escherichia coli	P0A790	-	-

Purification (Commentary)

Purification (Comment)	Organism
recombinant enzyme mutant N72A from Escherichia coli strain C41 (DE3) to homogeneity	Escherichia coli

Substrates and Products (Substrate)

Substrates	Comment Substrates	Organism	Products	Comment (Products)	Rev.	Reac.
L-aspartate	-	Escherichia coli	beta-alanine + CO2	-	?

Synonyms

Synonyms	Comment	Organism
ADC	-	Escherichia coli
Aspartate alpha-decarboxylase	-	Escherichia coli

Cofactor

Cofactor	Comment	Organism	Structure
pyruvoyl cofactor	the pyruvoyl group is required for catalysis	Escherichia coli

General Information

General Information	Comment	Organism
evolution	the enzyme is a member of a small class of pyruvoyl-dependent decarboxylases, in which the enzyme-bound pyruvoyl cofactor is generated via the autocatalytic rearrangement of a serine residue via an ester intermediate	Escherichia coli