Get 20M+ Full-Text Papers For Less Than $1.50/day. Start a 7-Day Trial for You or Your Team.

Learn More →

Regulation of Purine Ribonucleotide Synthesis by End Product InhibitionIII. Effect of Purine Nucleotides on Succino-AMP Synthetase of Bacillus subtilis

Regulation of Purine Ribonucleotide Synthesis by End Product InhibitionIII. Effect of Purine... Abstract 1. Succino-AMP synthetase (EC 6.3.4.4) was partially purified from the adenine starved cells of a Bacillus subtilis mutant which was derived from K strain and lacking succino-AMP; YASE (ec 4.3.2.2). The enzyme was stablizied by the presence of 1 mM dithiothreitol. Optimum pH for activity was about 7.5. Apparent Michaelis constants for IMP, GTP and L-aspartic acid were 34μM, 73 μM and 680μM, respectively. 2. The enzyme was inhibited strongly by the end products, AMP and ADP. Complete inhibition was obtained by 0.3mM AMP. This inhibition by AMP was competitive to GTP, noncompetitive to L-aspartic acid and of a mixed type to IMP. Both the Lineweaver-Burk plots in the presence of AMP and rate-AMP concentration curve were normal. Succino-AMP, GDP and inorganic orthophosphate, which are the direct product of the reaction, were also inhibitory at higher concentrations. This content is only available as a PDF. © by the Journal of Biochemistry http://www.deepdyve.com/assets/images/DeepDyve-Logo-lg.png The Journal of Biochemistry Oxford University Press

Regulation of Purine Ribonucleotide Synthesis by End Product InhibitionIII. Effect of Purine Nucleotides on Succino-AMP Synthetase of Bacillus subtilis

ISHII,, Kenji; SHIIO,, Isamu
The Journal of Biochemistry , Volume 68 (2) – Aug 1, 1970
Download PDF
6 pages

Loading next page...
 
/lp/oxford-university-press/regulation-of-purine-ribonucleotide-synthesis-by-end-product-0PLO81DZv1

References (0)

References for this paper are not available at this time. We will be adding them shortly, thank you for your patience.

Publisher
Oxford University Press
Copyright
© by the Journal of Biochemistry
ISSN
0021-924X
eISSN
1756-2651
DOI
10.1093/oxfordjournals.jbchem.a129343
Publisher site
See Article on Publisher Site

Abstract

Abstract 1. Succino-AMP synthetase (EC 6.3.4.4) was partially purified from the adenine starved cells of a Bacillus subtilis mutant which was derived from K strain and lacking succino-AMP; YASE (ec 4.3.2.2). The enzyme was stablizied by the presence of 1 mM dithiothreitol. Optimum pH for activity was about 7.5. Apparent Michaelis constants for IMP, GTP and L-aspartic acid were 34μM, 73 μM and 680μM, respectively. 2. The enzyme was inhibited strongly by the end products, AMP and ADP. Complete inhibition was obtained by 0.3mM AMP. This inhibition by AMP was competitive to GTP, noncompetitive to L-aspartic acid and of a mixed type to IMP. Both the Lineweaver-Burk plots in the presence of AMP and rate-AMP concentration curve were normal. Succino-AMP, GDP and inorganic orthophosphate, which are the direct product of the reaction, were also inhibitory at higher concentrations. This content is only available as a PDF. © by the Journal of Biochemistry

Journal

The Journal of Biochemistry – Oxford University Press

Published: Aug 1, 1970

There are no references for this article.