scholarly journals A hybrid proteolytic fragment of Escherichia coli aspartokinase I-homoserine dehydrogenase I. Structure, inhibition pattern, dissociation properties, and generation of two homodimers.

1983 ◽  
Vol 258 (22) ◽  
pp. 13570-13574
Author(s):  
A Fazel ◽  
Y Guillou ◽  
G N Cohen
Keyword(s):  
Escherichia Coli ◽  
Homoserine Dehydrogenase ◽  
Proteolytic Fragment ◽  
Inhibition Pattern

S-Adenosylethionine as an inhibitor of tRNA methylation

1969 ◽  
Vol 47 (5) ◽  
pp. 561-565 ◽  
Author(s):  
B. G. Moore ◽  
R. C. Smith
Keyword(s):  
Escherichia Coli ◽  
Preliminary Data ◽  
Kinetic Data ◽  
Competitive Inhibition ◽  
Inhibition Kinetics ◽  
Inhibition Reaction ◽  
Inhibition Pattern ◽  
Methylase Activity

S-Adenosylethionine was shown to inhibit the methylation of tRNA by S-adenosylmethionine. Lineweaver–Burk plots of kinetic data suggested that the inhibition was competitive. Another known inhibitor of tRNA methylation, adenine, also exhibited competitive inhibition kinetics. A derivative of S-adenosylethionine, ethylthioadenosine, also inhibited the reaction and displayed a competitive inhibition pattern. These data were obtained using Escherichia coli K12W6 as a source of methyl-deficient tRNA and methylase enzymes. Preliminary data indicate that S-adenosylethionine is even a better inhibitor of rat methylases.Methylase activity of ethionine-fed rats was elevated, which suggested that the inhibition reaction with S-adenosylethionine and the increased methylase activity may proceed by two different pathways.

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