Irreversible enzyme inhibitors 98 Hydrophobic interactions with succinoadenylate kinosynthetase and 9-substituted adenines

Baker, B. R.; Erickson, Edward H.

doi:10.1002/jps.2600560905

Cited by 3 publications

(1 citation statement)

References 29 publications

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“…The metabolic differences observed may also be based on the stereochemical properties of these compounds, as it was shown from studies using 9-substituted adenines as irreversible enzyme inhibitors, the stereochemistry of these compounds plays a very important role (28,29). Thus it was found that the 9-benzyl derivative fits into the hydrophobic region of succinoadenylate kinosynthetase, and adenosine deaminase better than the methyl analogue.…”

Section: Discussionmentioning

confidence: 96%

Biological N-oxidation of adenine and 9-alkyl derivatives

Lam

Devı́nsky

Gorrod

1987

European Journal of Drug Metabolism and Pharmacokinetics

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In vitro metabolism of adenine, 9-methyladenine, and 9-benzyladenine using hepatic microsomes of hamster, mouse and rat was investigated. The results indicated that adenine was apparently not susceptible to microsomal N-oxidation. N-oxidation of 9-methyladenine was also not detected, whereas N-demethylation was observed with hepatic microsomes derived from hamster and rat but not from mouse. With 9-benzyladenine, both 1-N-oxide formation and N-debenzylation occurred with microsomes of all species in various amounts. N-Hydroxylation of the 6-amino group was not observed with any substrate in any species. Metabolic results are discussed in relation to chemical structure, electronic, lipophilic and steric factors.

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Section: Discussionmentioning

confidence: 96%

Biological N-oxidation of adenine and 9-alkyl derivatives

Lam

Devı́nsky

Gorrod

1987

European Journal of Drug Metabolism and Pharmacokinetics

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Wechselwirkungen der nichtfunktionellen Coenzymbindungsstelle in Dehydrogenasen mit [Nicotinamid‐ribofuranosyl]‐[ω‐(adenin‐9‐yl)‐n‐alkyl]‐pyrophosphaten

Jeck

Wilhelm

1973

Justus Liebigs Ann. Chem.

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Die [Nicotinamid-ribofuranosyl]-[w-(adenin-9-yl)-n-alkyl]-pyrophosphate 1-41)werden durch Kondensation der ~~(Adenin-9-yl)-n-aIkyl-phosphate mit Nicotinamidmononucleotid gewonnen. Die Coenzymanalogen zeigen nahezu gleiche physikalische und chemische Eigenschaften wie Nicotinamid-adenin-dinucleotid (NAD 2) Interactions of the Nonfunctional Coenzyme Binding Site in Dehydrogenases with [Nicotinamide-ribofuranosyl] [w-(Adenine-9-yl)-n-alkyl] PyrophosphatesThe [nicotinamide-ribofuranosyl] [o>-(adenine-9-yl)-n-alkyl] pyrophosphates 1-41) are obtained by condensation of ct~-(adenine-9-yl)-n-alkyl phosphates with nicotinamide mononucleotide. The coenzyme analogues show nearly identical physical and chemical properties as nicotinamide-adenine dinucleotide (NAD)2). The intramolecular interaction between adenine and the quaternary nicotinamide system is less compared to NADe and depends on the length of the hydrocarbon chains which in the models connect the adenine ring to the pyrophosphate *) Korrespondenz bitte an diesen Autor richten. 1) 1: n-alkyl = athyl, 2 : n-alkyl = n-propyl, 3: n-alkyl = n-butyl und 4: n-alkyl = n-pentyl. NAD-Oxidoreduktase (EC 1.1.1.37); Glutamat-Dehydrogenase = L-Glutamat: NAD(P)-Oxidoreduktase (desaminierend) (EC 1.4.1.3) ; Pyrophosphatase aus Nuju Niveu36) = Dinucleotid-nucleotidhydrolase (EC 3.6.1.9) ; NADo = Nicotinamid-adenin-dinucleotid, NADH = Dihydronicotinamid-adenin-dinucleotid.

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