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Literature summary 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.
    View publication on PubMed

Crystallization (Commentary)

EC Number Crystallization (Comment) Organism
2.3.1.251 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
2.3.1.251 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

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

Organism

EC Number Organism UniProt Comment Textmining
2.3.1.251 Escherichia coli P37001
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2.3.1.251 Salmonella enterica subsp. enterica serovar Typhimurium
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