Increasing the thermal stability of the water-soluble pyrroloquinoline quinone glucose dehydrogenase by single amino acid replacement

2000 ◽  
Vol 26 (7) ◽  
pp. 491-496 ◽  
Author(s):  
Koji Sode ◽  
Takafumi Ootera ◽  
Miki Shirahane ◽  
Arief Budi Witarto ◽  
Satoshi Igarashi ◽  
...  
Keyword(s):  
Thermal Stability ◽  
Amino Acid ◽  
Glucose Dehydrogenase ◽  
Pyrroloquinoline Quinone ◽  
Amino Acid Replacement ◽  
Water Soluble ◽  
Single Amino Acid ◽  
Thermal Stability Of

Effect of single amino acid substitutions on the thermal stability of the .alpha. subunit of tryptophan synthase

Biochemistry ◽  
1980 ◽  
Vol 19 (7) ◽  
pp. 1290-1293 ◽  
Author(s):  
C. R. Matthews ◽  
M. M. Crisanti ◽  
G. L. Gepner ◽  
G. Velicelebi ◽  
J. M. Sturtevant
Keyword(s):  
Thermal Stability ◽  
Amino Acid ◽  
Alpha Subunit ◽  
Single Amino Acid ◽  
Amino Acid Substitutions ◽  
Tryptophan Synthase ◽  
Thermal Stability Of

scholarly journals Additivity of the Stabilization Effect of Single Amino Acid Substitutions in Triple Mutants of Recombinant Formate Dehydrogenase from the Soybean Glycine max

Acta Naturae ◽  
2015 ◽  
Vol 7 (3) ◽  
pp. 55-64 ◽  
Author(s):  
A. A. Alekseeva ◽  
I. S. Kargov ◽  
S. Yu. Kleimenov ◽  
S. S. Savin ◽  
V I. Tishkov
Keyword(s):  
Thermal Stability ◽  
Glycine Max ◽  
Amino Acid ◽  
Formate Dehydrogenase ◽  
Single Amino Acid ◽  
Inactivation Kinetics ◽  
Amino Acid Substitutions ◽  
Stabilization Effect ◽  
The Stability ◽  
Thermal Stability Of

Recently, we demonstrated that the amino acid substitutions Ala267Met and Ala267Met/Ile272Val (Alekseeva et al., Biochemistry, 2012), Phe290Asp, Phe290Asn and Phe290Ser (Alekseeva et al., Prot. Eng. Des. Select, 2012) in recombinant formate dehydrogenase from soya Glycine max (SoyFDH) lead to a significant (up to 30-100 times) increase in the thermal stability of the enzyme. The substitutions Phe290Asp, Phe290Asn and Phe290Ser were introduced into double mutant SoyFDH Ala267Met/Ile272Val by site-directed mutagenesis. Combinations of three substitutions did not lead to a noticeable change in the catalytic properties of the mutant enzymes. The stability of the resultant triple mutants was studied through thermal inactivation kinetics and differential scanning calorimetry. The thermal stability of the new mutant SoyFDHs was shown to be much higher than that of their precursors. The stability of the best mutant SoyFDH Ala267Met/Ile272Val/Phe290Asp turned out to be comparable to that of the most stable wild-type formate dehydrogenases from other sources. The results obtained with both methods indicate a great synergistic contribution of individual amino acid substitutions to the common stabilization effect.

scholarly journals A Single Amino Acid Mutation Enhances the Thermal Stability of Escherichia coli Malate Dehydrogenase

1994 ◽  
Vol 224 (1) ◽  
pp. 249-255 ◽  
Author(s):  
Christopher R. Goward ◽  
Julie Miller ◽  
David J. Nicholls ◽  
Laurence I. Irons ◽  
Michael D. Scawen ◽  
...  
Keyword(s):  
Escherichia Coli ◽  
Thermal Stability ◽  
Amino Acid ◽  
Malate Dehydrogenase ◽  
Single Amino Acid ◽  
Amino Acid Mutation ◽  
Single Amino Acid Mutation ◽  
Thermal Stability Of
Sign in / Sign up

Export Citation Format

Share Document