Literature summary for 4.1.3.3 extracted from

Campeotto, I.; Carr, S.B.; Trinh, C.H.; Nelson, A.S.; Berry, A.; Phillips, S.E.; Pearson, A.R.
Structure of an Escherichia coli N-acetyl-D-neuraminic acid lyase mutant, E192N, in complex with pyruvate at 1.45 A resolution (2009), Acta Crystallogr. Sect. F, 65, 1088-1090.

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Crystallization (Commentary)

Crystallization (Comment)	Organism
mutant enzyme E192N, in complex with pyruvate, sitting drop vapor diffusion method, using 100 mM Tris-HCl pH 8.2, 200 mM ammonium acetate, 18% PEG 3350	Escherichia coli

Protein Variants

Protein Variants	Comment	Organism
E192N	the mutant has a 6fold higher specificity (kcat/Km) for dipropylaminocarbonyl-substituted derivatives than wild type enzyme	Escherichia coli

Organism

Organism	UniProt	Comment	Textmining
Escherichia coli	P0A6L4	-	-

Purification (Commentary)

Purification (Comment)	Organism
-	Escherichia coli

Substrates and Products (Substrate)

Substrates	Comment Substrates	Organism	Products	Comment (Products)	Rev.	Reac.
N-acetylneuraminate	-	Escherichia coli	N-acetyl-D-mannosamine + pyruvate	-	r

Subunits

Subunits	Comment	Organism
homotetramer	x-ray crystallography	Escherichia coli

Synonyms

Synonyms	Comment	Organism
N-acetyl-D-neuraminic acid lyase	-	Escherichia coli
NAL	-	Escherichia coli

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Release 2023.1 (January 2023)