Literature summary for 2.5.1.47 extracted from

Tian, H.; Guan, R.; Salsi, E.; Campanini, B.; Bettati, S.; Kumar, V.P.; Karsten, W.E.; Mozzarelli, A.; Cook, P.F.
Identification of the structural determinants for the stability of substrate and aminoacrylate external Schiff bases in O-acetylserine sulfhydrylase-A (2010), Biochemistry, 49, 6093-6103.

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Protein Variants

Protein Variants	Comment	Organism
N71A	mutant exhibits formation of the alpha-aminoacrylate intermediate, but the rate constant for its formation from the external Schiff base is decreased by 1 order of magnitude compared to that of the wild type	Salmonella enterica
Q142A	mutant is unable to form the alpha-aminoacrylate intermediate but produces pyruvate at a rate much greater than that of the wild-type enzyme	Salmonella enterica
S69A	mutant exhibits formation of the alpha-aminoacrylate intermediate, but the rate constant for its formation from the external Schiff base is decreased by 1 order of magnitude compared to that of the wild type	Salmonella enterica
T68A	mutant is unable to form the alpha-aminoacrylate intermediate but produces pyruvate at a rate much greater than that of the wild-type enzyme	Salmonella enterica

Organism

Organism	UniProt	Comment	Textmining
Salmonella enterica	P0A1E3	subsp. enterica serovar Typhimurium	-

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Release 2023.1 (January 2023)