Location of the Catalytic Site for Phosphoenolpyruvate Formation within the Primary Structure of Clostridium symbiosum Pyruvate Phosphate Dikinase. 2. Site-Directed Mutagenesis of an Essential Arginine Contained within an Apparent P-Loop

Biochemistry ◽  
1995 ◽  
Vol 34 (7) ◽  
pp. 2188-2194 ◽  
Author(s):  
Linda Yankie ◽  
Yuan Xu ◽  
Debra Dunaway-Mariano
Keyword(s):  
Primary Structure ◽  
Catalytic Site ◽  
Site Directed Mutagenesis ◽  
Directed Mutagenesis ◽  
Pyruvate Phosphate Dikinase ◽  
Clostridium Symbiosum

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

scholarly journals Thimet oligopeptidase: site-directed mutagenesis disproves previous assumptions about the nature of the catalytic site

FEBS Letters ◽  
1998 ◽  
Vol 435 (1) ◽  
pp. 16-20 ◽  
Author(s):  
Jinq-May Chen ◽  
Richard A.E. Stevens ◽  
Paul W. Wray ◽  
Neil D. Rawlings ◽  
Alan J. Barrett
Keyword(s):  
Catalytic Site ◽  
Site Directed Mutagenesis ◽  
Directed Mutagenesis ◽  
Thimet Oligopeptidase

scholarly journals Characterization of the Catalytic Site of the ADP-RibosyltransferaseClostridium botulinumC2 Toxin by Site-directed Mutagenesis

1998 ◽  
Vol 273 (45) ◽  
pp. 29506-29511 ◽  
Author(s):  
Holger Barth ◽  
Jan C. Preiss ◽  
Fred Hofmann ◽  
Klaus Aktories
Keyword(s):  
Catalytic Site ◽  
Site Directed Mutagenesis ◽  
Directed Mutagenesis

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.

Exploration of the catalytic site of endopeptidase 24.11 by site-directed mutagenesis Histidine residues 583 and 587 are essential for catalysis

FEBS Letters ◽  
1988 ◽  
Vol 231 (1) ◽  
pp. 54-58 ◽  
Author(s):  
Alain Devault ◽  
Valérie Sales ◽  
Christiane Nault ◽  
Ann Beaumont ◽  
Bernard Roques ◽  
...  
Keyword(s):  
Catalytic Site ◽  
Site Directed Mutagenesis ◽  
Directed Mutagenesis ◽  
Histidine Residues ◽  
Endopeptidase 24.11

A conserved cysteine residue in yeast uroporphyrinogen decarboxylase is not essential for enzymatic activity

1997 ◽  
Vol 43 (8) ◽  
pp. 792-795 ◽  
Author(s):  
Celestino Di Flumeri ◽  
Nicholas H. Acheson ◽  
Teresa Keng
Keyword(s):  
Saccharomyces Cerevisiae ◽  
Enzymatic Activity ◽  
Mutant Strain ◽  
Cysteine Residue ◽  
Catalytic Site ◽  
Heme Biosynthesis ◽  
Site Directed Mutagenesis ◽  
Directed Mutagenesis ◽  
Decarboxylase Activity ◽  
Uroporphyrinogen Decarboxylase

Uroporphyrinogen decarboxylase catalyzes the fifth step of heme biosynthesis in Saccharomyces cerevisiae. Studies utilizing sulfhydryl-specific reagents suggest that the enzyme requires a cysteine residue within the catalytic site This hypothesis was tested directly by site-directed mutagenesis of highly conserved cysteine-52 to serine or alanine. Plasmids containing these mutations were able to complement a hem6 mutant strain. In addition, properties associated with decreased uroporphyrinogen decarboxylase activity were not detected in the mutant strain transformed with these mutant plasmids. These results suggest that the conserved cysteine-52 by itself is not essential for enzymatic activity.Key words: heme biosynthesis, uroporphyrinogen decarboxylase, site-directed mutagenesis.

Construction of a dimeric form of glutamate dehydrogenase from Clostridium symbiosum by site-directed mutagenesis

1996 ◽  
Vol 1297 (2) ◽  
pp. 149-158 ◽  
Author(s):  
Alessandra Pasquo ◽  
K.Linda Britton ◽  
Timothy J Stillman ◽  
Dave W Rice ◽  
Helmut Cölfen ◽  
...  
Keyword(s):  
Glutamate Dehydrogenase ◽  
Site Directed Mutagenesis ◽  
Directed Mutagenesis ◽  
Clostridium Symbiosum ◽  
Dimeric Form
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