Primary Structure, Expression, and Site-Directed Mutagenesis of Inorganic Pyrophosphatase from Bacillus stearothermophilus

1999 ◽  
Vol 125 (1) ◽  
pp. 48-57 ◽  
Author(s):  
T. Satoh ◽  
H. Shinoda ◽  
K. Ishii ◽  
M. Koyama ◽  
N. Sakurai ◽  
...  
Keyword(s):  
Primary Structure ◽  
Bacillus Stearothermophilus ◽  
Site Directed Mutagenesis ◽  
Inorganic Pyrophosphatase ◽  
Directed Mutagenesis

Site-directed mutagenesis of Bacillus stearothermophilus lactate dehydrogenase

1987 ◽  
Vol 15 (1) ◽  
pp. 152-153 ◽  
Author(s):  
ANTHONY R. CLARKE ◽  
DALE B. WIGLEY ◽  
DAVID A. BARSTOW ◽  
WILLIAM N. CHIA ◽  
ADAM D. B. WALDMAN ◽  
...  
Keyword(s):  
Lactate Dehydrogenase ◽  
Bacillus Stearothermophilus ◽  
Site Directed Mutagenesis ◽  
Directed Mutagenesis

Site-Directed Mutagenesis of a Thermostable α-Amylase from Bacillus stearothermophilus: Putative Role of Three Conserved Residues1

1990 ◽  
Vol 107 (2) ◽  
pp. 267-272 ◽  
Author(s):  
Mauno Vihinen ◽  
Pauli Olikka ◽  
Jukka Niskanen ◽  
Peter Meyer ◽  
IIari Suominen ◽  
...  
Keyword(s):  
Bacillus Stearothermophilus ◽  
Site Directed Mutagenesis ◽  
Directed Mutagenesis ◽  
Putative Role

A Novel PCR Site-Directed Mutagenesis to Modify Structure of Erabutoxin B

2011 ◽  
Vol 183-185 ◽  
pp. 605-610
Author(s):  
Fang Hui Wu ◽  
Yan Jun Li ◽  
Ting Song Yang ◽  
Tian Yi Ying
Keyword(s):  
Primary Structure ◽  
Site Directed Mutagenesis ◽  
Directed Mutagenesis ◽  
Function Structure ◽  
One Step ◽  
Ld50 Value ◽  
The One ◽  
Erabutoxin B ◽  
Structure Of Proteins ◽  
Modify Structure

Objective: A convenient PCR was used for site-directed mutagenesis to modify structure of proteins or peptides, For function-structure studies of proteins or peptides. Method: the one-step PCR site-directed mutagenesis strategy can introduce mutation of gene through 5/-end of primer, which was applied on peptide Erabutoxin B (EB) to produce three mutants of EB, the activity of mutants was detected by LD50 value of mice. Result: S8Y, R33D, K47R three mutants of EB were obtained by one-step PCR, LD50 of mutants indicated that the activity of mutants decreased in different degree, the activity of R33D was nearly deprived. Conclusion: one-step PCR site-directed mutagenesis was convenien and efficient, it can be applied on restructuring the primary structure of proteins or peptides.

scholarly journals Increasing the thermostability of the neutral proteinase of Bacillus stearothermophilus by improvement of internal hydrogen-bonding

1992 ◽  
Vol 285 (2) ◽  
pp. 625-628 ◽  
Author(s):  
V G Eijsink ◽  
G Vriend ◽  
J R Van der Zee ◽  
B Van den Burg ◽  
G Venema
Keyword(s):  
Molecular Dynamics ◽  
Hydrogen Bond ◽  
Bacillus Stearothermophilus ◽  
Site Directed Mutagenesis ◽  
Internal Cavity ◽  
Directed Mutagenesis ◽  
Neutral Proteinase ◽  
Internal Hydrogen ◽  
Internal Hydrogen Bond ◽  
Dynamics Simulations

In an attempt to increase the thermostability of the neutral proteinase of Bacillus stearothermophilus the buried Ala-170 was replaced by serine. Molecular-dynamics simulations showed that Ser-170 stabilizes the enzyme by formation of an internal hydrogen bond. In addition, the hydroxy group of Ser-170 could contribute to stability by filling an internal cavity. After the introduction of the mutation, using site-directed-mutagenesis techniques, an increase in stability of 0.7 +/- 0.1 degrees C was obtained.

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