A possible mechanism for the in vitro activation of L-serine deaminase activity in Escherichia coli K12

1990 ◽  
Vol 68 (4) ◽  
pp. 723-728 ◽  
Author(s):  
E. B. Newman ◽  
Caroline Walker ◽  
K. Ziegler-Skylakakis
Keyword(s):  
Escherichia Coli ◽  
Enzyme Activation ◽  
Free Radical Scavengers ◽  
Escherichia Coli K12 ◽  
Diethylene Triamine ◽  
In Vitro Activation ◽  
Diethylene Triamine Pentaacetic Acid ◽  
Serine Deaminase ◽  
Reversible Reduction

L-Serine deaminase is inactive in crude extracts of Escherichia coli K12, but can be activated by incubation with iron and dithiothreitol. This activation requires oxygen, and is inhibited by free radical scavengers and by diethylene triamine pentaacetic acid, which prevents Fe cycling. We suggest that in vitro activation of L-serine deaminase is catalyzed by an oxidant (perhaps hydroxyl radicals). Also, activation may be accompanied by a decrease in molecular weight and involve both a cleavage of the polypeptide chain and a reversible reduction of the molecule.Key words: enzyme activation, serine degradation.

In vitro studies on L-serine deaminase activity of Escherichia coli K12

1980 ◽  
Vol 58 (11) ◽  
pp. 1292-1297 ◽  
Author(s):  
E. B. Newman ◽  
V. Kapoor
Keyword(s):  
Escherichia Coli ◽  
Metal Ions ◽  
In Vitro Studies ◽  
Soluble Enzyme ◽  
E Coli ◽  
Escherichia Coli K12 ◽  
Substrate Analogues ◽  
Mammalian Enzyme ◽  
Serine Deaminase

Extracts of Escherichia coli K12 contain an enzyme which deaminates L-serine. This serine deaminase appears to be a soluble enzyme and is inhibited by substrate analogues, metal ions, and chelators. The activity, which is very unstable in vitro, is protected, and in some cases, even activated by substrate, substrate analogues, and by ferrous ion. The enzyme has proved unstable in all attempts at purification. It resembles closely the L-serine deaminase activity in other microorganisms, but is very different from the mammalian enzyme. As judged by comparison with organisms in which this enzyme serves as part of the principal carbon-handling pathway, L-serine deaminase activity is present in E. coli extracts in physiologically significant amounts.

Transcription of the argF and argI genes of the arginine biosynthetic regulon of Escherichia coli K12, performed in vitro

1977 ◽  
Vol 155 (1) ◽  
pp. 7-18 ◽  
Author(s):  
Don Sens ◽  
William Natter ◽  
Robert T. Garvin ◽  
Eric James
Keyword(s):  
Escherichia Coli ◽  
Escherichia Coli K12

scholarly journals Molybdoenzyme biosynthesis in Escherichia coli: in vitro activation of purified nitrate reductase from a chlB mutant.

1992 ◽  
Vol 174 (24) ◽  
pp. 7934-7940 ◽  
Author(s):  
C L Santini ◽  
C Iobbi-Nivol ◽  
C Romane ◽  
D H Boxer ◽  
G Giordano
Keyword(s):  
Escherichia Coli ◽  
Nitrate Reductase ◽  
In Vitro Activation

Evidence for the existence of three promoters for the deo operon of Escherichia coli K12 in vitro

1979 ◽  
Vol 133 (1) ◽  
pp. 1-17 ◽  
Author(s):  
Poul Valentin-Hansen ◽  
Karin Hammer-Jespersen ◽  
R.S. Buxton
Keyword(s):  
Escherichia Coli ◽  
Escherichia Coli K12 ◽  
Deo Operon
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