scholarly journals One functional subunit is sufficient for catalytic activity and substrate specificity of Escherichia coli endoribonuclease III artificial heterodimers

FEBS Letters ◽  
2002 ◽  
Vol 518 (1-3) ◽  
pp. 93-96 ◽  
Author(s):  
Christian Conrad ◽  
Jens Guido Schmitt ◽  
Elena Evguenieva-Hackenberg ◽  
Gabriele Klug
Keyword(s):  
Escherichia Coli ◽  
Catalytic Activity ◽  
Substrate Specificity

3-D structure of the D153G mutant of Escherichia coli alkaline phosphatase: an enzyme with weaker magnesium binding and increased catalytic activity

1995 ◽  
Vol 8 (9) ◽  
pp. 865-871 ◽  
Author(s):  
Chris G. Dealwis ◽  
Liqing Chen ◽  
Catherine Brennan ◽  
Wlodek Mandecki ◽  
Cele Abad-Zapatero
Keyword(s):  
Escherichia Coli ◽  
Alkaline Phosphatase ◽  
Catalytic Activity ◽  
Magnesium Binding

Synthesis of γ-L-Glutamylalkylamides Catalyzed by Escherichia coli Having γ-Glutamyltranspeptidase Activity

2012 ◽  
Vol 550-553 ◽  
pp. 1177-1181
Author(s):  
Fei Zhang ◽  
Yin Liu ◽  
Pei Xin He
Keyword(s):  
Escherichia Coli ◽  
Substrate Specificity ◽  
Conversion Rate ◽  
Medicinal Value

γ-L-glutamyl alkylamines have potential medicinal value. In this research, five different γ-L-glutamyl alkylamines were synthesized. The result showed that substrate specificity of alkylamines, from high to low, is methylamine, ethylamine, n-propylamine, isopropylamine and n-butylamine. The reaction was optimal at pH 9.5 and 45°C, and the optimal substrate mole ratio of L-glutamine to alkylamine was 1:3 (mol/mol).Under these conditions, conversion rate of L-glutamine is about 90% (mol/mol)．

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