Evidence of isosteric and allosteric nucleotide inhibition of citrate synthease from multiple-inhibition studies
Keyword(s):
Citrate synthases from diverse organisms are inhibited by ATP and NADH. Evidence is presented, from multiple-inhibition studies on various citrate synthases, that ATP acts in all cases as an isosteric inhibitor at the acetyl-CoA site. On the other hand, NADH also acts isosterically with eukaryotic and Gram-positive bacterial citrate synthases, but behaves as an allosteric inhibitor specifically in the case of the Gram-negative bacterial enzyme. After desensitization to this allosteric inhibition, only the isosteric nucleotide inhibition, as found in other citrate syntheases, is observed.
1936 ◽
Vol 64
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pp. 19-28
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2006 ◽
Vol 50
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pp. 2261-2264
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1956 ◽
Vol 104
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pp. 829-845
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1997 ◽
Vol 41
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pp. 2209-2213
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1926 ◽
Vol 44
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pp. 11-20
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2020 ◽
pp. 25-28
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