Enzymic properties of 8-bromoadenine nucleotides

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DOIResolve DOI: http://doi.org/10.1021/bi00589a009
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TypeArticle
Journal titleBiochemistry
ISSN0006-2960
1520-4995
Volume18
Issue22
Pages48184826
Abstract8-Bromoadenine nucleotides were tested as potential substrates and/or inhibitors of mitochondrial processes in intact or disrupted organelles, as substrates of various phosphotransferases, and as allosteric effectors in the reactions catalyzed by phosphofructokinase, isocitrate dehydrogenase, glutamate dehydrogenase, and fructose- 1,6-bisphosphatase. 8-BrATP and 8-BrADP are not recognized by the translocase system located in the inner mitochondrial membrane and cannot be used as substrates in oxidative phosphorylation and related reactions catalyzed by beef heart submitochondrial membranes. This confirms the high specificity for adenine nucleotides of the mammalian systems involved in energyyielding and energy-requiring reactions. However, 8-BrATP and 8-BrADP are able to substitute for the natural adenine nucleotides in reactions catalyzed by many phosphotransferases, although their capacity as phosphate donors and acceptors is generally much reduced. On the other hand, in almost all investigated cases, the 8-bromoadenine nucleotides have lost the capability of the natural adenine nucleotides to act as allosteric effectors, indicating that the structural requirements for allosteric activity are more stringent than those for catalytic activity.
Publication date
LanguageEnglish
AffiliationNational Research Council Canada
Peer reviewedYes
NPARC number23001738
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Record identifierae837389-b4b0-44c0-ad81-74273e0806fd
Record created2017-03-24
Record modified2017-03-24
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