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Literature summary 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

Crystallization (Commentary)

EC Number Crystallization (Comment) Organism
3.4.19.3 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

EC Number Protein Variants Comment Organism
3.4.19.3 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
3.4.19.3 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
3.4.19.3 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
3.4.19.3 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
3.4.19.3 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

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

EC Number Temperature Stability Minimum [°C] Temperature Stability Maximum [°C] Comment Organism
3.4.19.3 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
3.4.19.3 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
3.4.19.3 79
-
 peak temperature on the differential scanning calorimetry is 78.9°C, pH 3.04 cysteine-free mutant enzyme C142S/C188S Pyrococcus furiosus
3.4.19.3 89
-
 peak temperature on the differential scanning calorimetry is 77.6°C, pH 7.3, cysteine-free mutant enzyme C142S/C188S Pyrococcus furiosus
3.4.19.3 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
3.4.19.3 102
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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

EC Number pH Stability pH Stability Maximum Comment Organism
3.4.19.3 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
3.4.19.3 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