scholarly journals Divergence of Substrate Specificity and Function in the Escherichia coli Hotdog-fold Thioesterase Paralogs YdiI and YbdB

Biochemistry ◽  
2014 ◽  
Vol 53 (29) ◽  
pp. 4775-4787 ◽  
Author(s):  
John A. Latham ◽  
Danqi Chen ◽  
Karen N. Allen ◽  
Debra Dunaway-Mariano
Keyword(s):  
Escherichia Coli ◽  
Substrate Specificity ◽  
And Function ◽  
Hotdog Fold

scholarly journals On the location and function of tyrosine beta 331 in the catalytic site of Escherichia coli F1-ATPase.

1992 ◽  
Vol 267 (3) ◽  
pp. 1712-1718 ◽  
Author(s):  
J Weber ◽  
R S Lee ◽  
E Grell ◽  
J G Wise ◽  
A E Senior
Keyword(s):  
Escherichia Coli ◽  
Catalytic Site ◽  
F1 Atpase ◽  
And Function

scholarly journals Micro-analysis of pure deoxyribonucleic acid-dependent ribonucleic acid polymerase from Escherichia coli. Action of heparin and rifampicin on structure and function

1970 ◽  
Vol 117 (3) ◽  
pp. 623-631 ◽  
Author(s):  
Volker Neuhoff ◽  
Wolf-Bernhard Schill ◽  
Hans Sternbach
Keyword(s):  
Escherichia Coli ◽  
Rna Polymerase ◽  
Rna Synthesis ◽  
Deoxyribonucleic Acid ◽  
Structure And Function ◽  
Disc Electrophoresis ◽  
Inhibitory Mechanism ◽  
And Function ◽  
Micro Analysis ◽  
Template Complex

By using micro disc electrophoresis and micro-diffusion techniques, the interaction of pure DNA-dependent RNA polymerase (EC 2.7.7.6) from Escherichia coli with the template, the substrates and the inhibitors heparin and rifampicin was investigated. The following findings were obtained: (1) heparin converts the 24S and 18S particles of the polymerase into the 13S form; (2) heparin inhibits RNA synthesis by dissociating the enzyme–template complex; (3) rifampicin does not affect the attachment of heparin to the enzyme; (4) the substrates ATP and UTP are bound by enzyme loaded with rifampicin; (5) rifampicin is bound by an enzyme–template complex to the same extent as by an RNA-synthesizing enzyme–template complex. From this it is concluded that the mechanism of the inhibition of RNA synthesis by rifampicin is radically different from that by heparin. As a working hypothesis to explain the inhibitory mechanism of rifampicin, it is assumed that it becomes very firmly attached to a position close to the synthesizing site and only blocks this when no synthesis is in progress.

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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