Literature summary for 2.3.1.251 extracted from

Iyer, B.R.; Mahalakshmi, R.
Residue-dependent thermodynamic cost and barrel plasticity balances activity in the PhoPQ-activated enzyme PagP of Salmonella typhimurium (2015), Biochemistry, 22, 5712-5722.

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Crystallization (Commentary)

Crystallization (Comment)	Organism
molecular dynamics simulation and comparison of Salmonella typhimurium and Escherichia coli enzymes. In vitro lipase activity of the Salmonella enzyme is 15-20fold higher than for the Escherichia coli enzyme. Protein stability correlates inversely with activity: the Escherichia coli PagP equilibrium free energy is 2fold higher	Salmonella enterica subsp. enterica serovar Typhimurium
molecular dynamics simulation and comparison of Salmonella typhimurium and Escherichia coli enzymes. In vitro lipase activity of the Salmonella enzyme is 15-20fold higher than for the Escherichia coli enzyme. Protein stability correlates inversely with activity: the Escherichia coli PagP equilibrium free energy is 2fold higher	Escherichia coli

Protein Variants

Protein Variants	Comment	Organism
K91S	mutation leads to 2fold reduction in the protein stability by about 3.45 kcal/mol	Salmonella enterica subsp. enterica serovar Typhimurium
L57Q	mutation leads to destabilizization by about 3.5 kcal/mol	Escherichia coli
Q57L	presence of Leu confers an added 2.2 kcal/mol stabilization	Salmonella enterica subsp. enterica serovar Typhimurium
S91K	mutation leads to stabilizization by about 3.0 kcal/mol	Escherichia coli

Organism

Organism	UniProt	Comment	Textmining
Escherichia coli	P37001	-	-
Salmonella enterica subsp. enterica serovar Typhimurium	-	-	-

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Release 2023.1 (January 2023)