Regulatory effects of purine nucleotide analogs with liver glutamate dehydrogenase

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DOIResolve DOI: http://doi.org/10.1016/0005-2744(77)90239-X
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TypeArticle
Journal titleBiochimica et Biophysica Acta (BBA) - Enzymology
ISSN0005-2744
Volume482
Issue2
Pages251260
AbstractA total of 26 different purine nucleotides with specific modifications in the base moiety and/or in the polyphosphate chain as well as various combinations of nucleotides were tested as allosteric effectors of beef liver glutamate dehydrogenase (l-glutamate : NAD(P)+ oxidoreductase (deaminating), EC 1.4.1.3). The capacity of these nucleotide analogs to activate or to inhibit the glutamate dehydrogenase activity is expressed quantitatively and scaled between the extreme effects of ADP and GTP, respectively. The significance of distinct structural elements for the enzyme-effector interaction is discussed. While the inhibitory GTP site is less specific, accepting many natural and most modified nucleoside triphosphates as inhibitors, the activating ADP site shows a much higher specificity for nucleotides as activators.
Publication date
PublisherElsevier/North-Holland Biomedical Press
LanguageEnglish
AffiliationNational Research Council Canada
Peer reviewedYes
NPARC number23001279
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Record identifier86c9a8d9-ad44-4417-8e16-1dd7aa199ea5
Record created2017-01-13
Record modified2017-01-13
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