Literature summary extracted from

Lee, S.; Park, E.H.; Ko, H.J.; Bang, W.G.; Kim, H.Y.; Kim, K.H.; Choi, I.G.
Crystal structure analysis of a bacterial aryl acylamidase belonging to the amidase signature enzyme family (2015), Biochem. Biophys. Res. Commun., 467, 268-274 .

Cloned(Commentary)

EC Number	Cloned (Comment)	Organism
3.5.1.13	cloned in a modified pET21 vector encoding a 6x-histidine tag at the carboxyl terminus and overexpressed in Escherichia coli BL21 (DE3)	bacterium CSBL00001

Crystallization (Commentary)

EC Number	Crystallization (Comment)	Organism
3.5.1.13	sitting-drop vapor diffusion method at room temperature. Structures of the enzyme are determined in its native form and in complex with the analgesic acetanilide, p-acetaminophenol, at 1.70 A and 1.73 A resolutions, respectively. The overall structural fold of the enzyme is identified as an alpha/beta fold class, exhibiting an open twisted beta-sheet core surrounded by alpha-helices	bacterium CSBL00001

Organism

EC Number	Organism	UniProt	Comment	Textmining
3.5.1.13	bacterium CSBL00001	C3UWD1	-	-

Purification (Commentary)

EC Number	Purification (Comment)	Organism
3.5.1.13	-	bacterium CSBL00001

Subunits

EC Number	Subunits	Comment	Organism
3.5.1.13	monomer	is functionally active	bacterium CSBL00001

Synonyms

EC Number	Synonyms	Comment	Organism
3.5.1.13	AAA	-	bacterium CSBL00001

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Release 2023.1 (January 2023)