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Literature summary for 3.4.19.3 extracted from

  • Kaushik, J.K.; Iimura, S.; Ogasahara, K.; Yamagata, Y.; Segawa, S.; Yutani, K.
    Completely buried, non-ion-paired glutamic acid contributes favorably to the conformational stability of pyrrolidone carboxyl peptidases from hyperthermophiles (2006), Biochemistry, 45, 7100-7112.
    View publication on PubMed
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Crystallization (Commentary)

Crystallization (Comment) Organism
PCP-0SH polar mutants C142S/C188S/E192D andC142S/C188S/E192Q crystallize at a 6.5% PEG4000, while the apolar mutants C142S/C188S/E192A, C142S/C188S/E192I and C142S/C188S/E192V crystallize at a 5.7-6.0% PEG4000. The protein molecules crystallize in two different space groups. E192Q and E192V form isomorphic monoclinic crystals in the space group P2(1), which agree with those of the wild-type PCP and cysteine-free PCP-0SH (C142S/C188S), while E192A, E192D, and E192I form orthorhombic crystals in the space group P2(1)2(1)2(1). In both crystal systems, four subunit (monomer) molecules are contained in the asymmetric unit. A systematic analysis of individual structures indicates that the mutation does not have any significant effect on the overall structure Pyrococcus furiosus

Protein Variants

Protein Variants Comment Organism
C142S/C188S/E192A at acidic pH the mutant enzyme is less stable than cysteine-free mutant C142S/C188S. At alkaline pH the mutant enzyme is more stable than cysteine-free mutant C142S/C188S. The thermal stability of the mutant enzyme at pH 2.15, pH 3.04 and pH 7.3 is less than that of the cysteine-free mutant enzyme C142S/C188S. At pH 8.7 and 9.6 the thermal stability of mutant enzyme is higher than that of the cysteine-free mutant C142S/C188S Pyrococcus furiosus
C142S/C188S/E192D at acidic pH the mutant enzyme is less stable than cysteine-free mutant C142S/C188S. The thermal stability of the mutant enzyme at pH 2.15, pH 3.04, pH 7.3, pH 8.7 and pH 9.6 is less than that of the cysteine-free mutant enzyme C142S/C188S Pyrococcus furiosus
C142S/C188S/E192I at acidic pH the mutant enzyme is less stable than cysteine-free mutant C142S/C188S. At alkaline pH the mutant enzyme is more stable than cysteine-free mutant C142S/C188S. The thermal stability of the mutant enzyme at pH 2.15, pH 3.04 and pH 7.3 is less than that of the cysteine-free mutant enzyme C142S/C188S. At pH 8.7 and 9.6 the thermal stability of mutant enzyme is higher than that of the cysteine-free mutant C142S/C188S Pyrococcus furiosus
C142S/C188S/E192Q at acidic pH the mutant enzyme is less stable than cysteine-free mutant C142S/C188S. At alkaline pH the mutant enzyme is more stable than cysteine-free mutant C142S/C188S. The thermal stability of the mutant enzyme at pH 2.15, pH 3.04 and pH 7.3 is less than that of the cysteine-free mutant enzyme C142S/C188S. At pH 8.7 and 9.6 the thermal stability of mutant enzyme is higher than that of the cysteine-free mutant C142S/C188S Pyrococcus furiosus
C142S/C188S/E192V at acidic pH the mutant enzyme is less stable than cysteine-free mutant C142S/C188S. At alkaline pH the mutant enzyme is more stable than cysteine-free mutant C142S/C188S. The thermal stability of the mutant enzyme at pH 2.15, pH 3.04 and pH 7.3 is less than that of the cysteine-free mutant enzyme C142S/C188S. At pH 8.7 and 9.6 the thermal stability of mutant enzyme is higher than that of the cysteine-free mutant C142S/C188S Pyrococcus furiosus

Organism

Organism UniProt Comment Textmining
Pyrococcus furiosus O73944
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Temperature Stability [°C]

Temperature Stability Minimum [°C] Temperature Stability Maximum [°C] Comment Organism
additional information
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 the thermal stability of the mutant enzymes C142S/C188S/E192A, C142S/C188S/E192I, C142S/C188S/E192V, C142S/C188S/E192D and C142S/C188S/E192Q at pH 2.15, pH 3.04 and pH 7.3 is less than that of the cysteine-free mutant enzyme C142S/C188S. At pH 8.7 and 9.6 the thermal stability of mutant enzymes C142S/C188S/E192A, C142S/C188S/E192I, C142S/C188S/E192V and C142S/C188S/E192Q is higher than that of the cysteine-free mutant C142S/C188S. The thermal stability of mutant enzyme C142S/C188S/E192D at pH 8.7 and 9.6 is less than that of cysteine-free mutant enzyme C142S/C188S Pyrococcus furiosus
59
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 peak temperature on the differential scanning calorimetry is 59.3°C, pH 2.15, cysteine-free mutant enzyme C142S/C188S Pyrococcus furiosus
79
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 peak temperature on the differential scanning calorimetry is 78.9°C, pH 3.04 cysteine-free mutant enzyme C142S/C188S Pyrococcus furiosus
89
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 peak temperature on the differential scanning calorimetry is 77.6°C, pH 7.3, cysteine-free mutant enzyme C142S/C188S Pyrococcus furiosus
89
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 peak temperature on the differential scanning calorimetry is 88.8°C, pH 8,7, cysteine-free mutant enzyme C142S/C188S Pyrococcus furiosus
102
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 peak temperature on the differential scanning calorimetry is 101.7°C, pH 9,6, cysteine-free mutant enzyme C142S/C188S Pyrococcus furiosus

pH Stability

pH Stability pH Stability Maximum Comment Organism
2.4
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 at acidic pH the mutant enzymes C142S/C188S/E192A, C142S/C188S/E192I, C142S/C188S/E192V, C142S/C188S/E192D and C142S/C188S/E192Q are less stable than cysteine-free mutant C142S/C188S Pyrococcus furiosus
10.5
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 at alkaline pH the mutant enzyme enzymes C142S/C188S/E192A, C142S/C188S/E192I, C142S/C188S/E192V and C142S/C188S/E192Q are more stable than cysteine-free mutant C142S/C188S Pyrococcus furiosus