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Literature summary for 4.6.1.24 extracted from

  • Trevino, S.R.; Gokulan, K.; Newsom, S.; Thurlkill, R.L.; Shaw, K.L.; Mitkevich, V.A.; Makarov, A.A.; Sacchettini, J.C.; Scholtz, J.M.; Pace, C.N.
    Asp79 makes a large, unfavorable contribution to the stability of RNase Sa (2005), J. Mol. Biol., 354, 967-978.
    View publication on PubMed
Search for more literature for 4.6.1.24

Crystallization (Commentary)

Crystallization (Comment) Organism
mutant enzyme Q94K, hanging-drop vapor-diffusion method at 18°C Kitasatospora aureofaciens

Protein Variants

Protein Variants Comment Organism
D33A Tm-value at pH 7.0 in Mops buffer is 16 °C lower than wild-type value. The stability of the mutant enzyme is 6 kcal/mol less than wild-type RNase Sa Kitasatospora aureofaciens
D79A Tm-value at pH 7.0 in Mops buffer is 9.2 °C higher than wild-type value. The stability of the mutant enzyme is 3.3 kcal/mol less than wild-type RNase Sa Kitasatospora aureofaciens
D79E Tm-value at pH 7.0 in Mops buffer is 0.8 °C lower than wild-type value. kcat/Km is identical to wild-type value Kitasatospora aureofaciens
D79F Tm-value at pH 7.0 in Mops buffer is 9.9 °C higher than wild-type value Kitasatospora aureofaciens
D79H Tm-value at pH 7.0 in Mops buffer is 5.6 °C higher than wild-type value Kitasatospora aureofaciens
D79I Tm-value at pH 7.0 in Mops buffer is 9.6 °C higher than wild-type value. kcat/Km is 1.3fold lower than wild-type value Kitasatospora aureofaciens
D79K Tm-value at pH 7.0 in Mops buffer is 7.6 °C higher than wild-type value. kcat/Km is 1.1fold lower than wild-type value Kitasatospora aureofaciens
D79L Tm-value at pH 7.0 in Mops buffer is 8.7 °C higher than wild-type value Kitasatospora aureofaciens
D79N Tm-value at pH 7.0 in Mops buffer is 5.5 °C higher than wild-type value. kcat/Km is 1.1fold lower than wild-type value Kitasatospora aureofaciens
D79R Tm-value at pH 7.0 in Mops buffer is 9.0 °C higher than wild-type value. kcat/Km is 1.1fold higher than wild-type value Kitasatospora aureofaciens
D79W Tm-value at pH 7.0 in Mops buffer is 7.6 °C higher than wild-type value. kcat/Km is 1.2fold lower than wild-type value Kitasatospora aureofaciens
D79Y Tm-value at pH 7.0 in Mops buffer is 9.6 °C higher than wild-type value Kitasatospora aureofaciens
Q94K Tm-value at pH 7.0 in Mops buffer is 0.8 °C higher than wild-type value. Crystal structure shows that the amino group of the Lys forms a hydrogen-bonded ion pair with the carboxyl group of Asp79. The stability of the mutant is about the same as the wild-type at pH 3, where Asp79 is uncharged, but 1 kcal/mol greater than that of wild-type RNase Sa at pH 8.5, where Asp79 is charged Kitasatospora aureofaciens

KM Value [mM]

KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
0.16
-
 poly(I) 25°C, pH 6.5, mutant enzyme D79E Kitasatospora aureofaciens
0.16
-
 poly(I) 25°C, pH 6.5, wild-type enzyme Kitasatospora aureofaciens
0.21
-
 poly(I) 25°C, pH 6.5, mutant enzyme D79N Kitasatospora aureofaciens
0.3
-
 poly(I) 25°C, pH 6.5, mutant enzyme D79R Kitasatospora aureofaciens
0.33
-
 poly(I) 25°C, pH 6.5, mutant enzyme D79K Kitasatospora aureofaciens
0.36
-
 poly(I) 25°C, pH 6.5, mutant enzyme D79I Kitasatospora aureofaciens
0.4
-
 poly(I) 25°C, pH 6.5, mutant enzyme D79W Kitasatospora aureofaciens

Organism

Organism UniProt Comment Textmining
Kitasatospora aureofaciens P05798
-
-

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
poly(I) + H2O
-
 Kitasatospora aureofaciens ?
-
 ?

Synonyms

Synonyms Comment Organism
Ribonuclease SA
-
 Kitasatospora aureofaciens
RNase Sa
-
 Kitasatospora aureofaciens

Turnover Number [1/s]

Turnover Number Minimum [1/s] Turnover Number Maximum [1/s] Substrate Comment Organism Structure
220
-
 poly(I) 25°C, pH 6.5, mutant enzyme D79E Kitasatospora aureofaciens
220
-
 poly(I) 25°C, pH 6.5, wild-type enzyme Kitasatospora aureofaciens
280
-
 poly(I) 25°C, pH 6.5, mutant enzyme D79N Kitasatospora aureofaciens
410
-
 poly(I) 25°C, pH 6.5, mutant enzyme D79I Kitasatospora aureofaciens
430
-
 poly(I) 25°C, pH 6.5, mutant enzyme D79K Kitasatospora aureofaciens
460
-
 poly(I) 25°C, pH 6.5, mutant enzyme D79R Kitasatospora aureofaciens
460
-
 poly(I) 25°C, pH 6.5, mutant enzyme D79W Kitasatospora aureofaciens