Crystal and molecular structure of 8-bromoguanosine and 8-bromoadenosine, two purine nucleosides in the syn conformation

Tavale, Sudam S.; Sobell, Henry M.

doi:10.1016/0022-2836(70)90222-6

Cited by 207 publications

(90 citation statements)

References 9 publications

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“…8-Substituted adenosine derivatives exhibit a syn conformation in crystals [19] as well as in solution [20]. Except for 8-mercapto-adenosine 5'-triphosphate (8), the 8-substituted ATP analogs (6, 7, 9) act as inhibitor with isoleucyl-tRNA synthetase, two of them (6,7) are noncompetitive, one (9) is of the uncompetitive type; probably they are also bound to the normal and additional ATP binding sites as is supposed for two noncompetitive inhibitors of phenylalanyl-tRNA synthetase from E. coli [21].…”

Section: Resultsmentioning

confidence: 99%

“…The triphosphates (1,2,(4)(5)(6)(7)(8)(9)(10)(11)(12)(13)(14)(15)(16)(17)(18)(19) were synthesized in the same way or obtained from the same sources as previously [l 1 1. A substance was considered as an inhibitor if in these tests more than 20 % decrease in I4C incorporated was observed. The temperature was kept at 37 "C during the tests.…”

Section: Triphosphatesmentioning

confidence: 99%

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Valyl‐tRNA, Isoleucyl‐tRNA and Tyrosyl‐tRNA Synthetase from Baker's Yeast

Freist¹,

Haar²,

Faulhammer³

et al. 1976

European Journal of Biochemistry

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Nineteen analogs of ATP have been tested in the aminoacylation reaction of valyl-tRNA, isoleucyltRNA and tyrosyl-tRNA synthetases from baker's yeast. Four compounds are substrates for valyltRNA and two for isoleucyl-tRNA synthetase, but there is no modified substrate for the tyrosyltRNA synthetase. There is one inhibitor for valyl-tRNA synthetase, eight compounds inhibit isoleucyl-tRNA synthetase and two compounds inhibit tyrosyl-tRNA synthetase. Their K , and Ki and V values have been determined.The substrate specificity shows that positions 2, 6, 7, 8, 9, 2', and 3' of ATP are important for catalytic action of these aminoacyl-tRNA synthetases.For the aminoacylation of tRNAs with amino acids by aminoacyl-tRNA synthetases a number of investigators report an absolute requirement of Mg2 + ions [I -51.ATP + aa + tRNA e aa-tRNA + AMP + PPi. Because Mg2+ and other divalent cations form definite complexes with ATP [6-lo], the requirement of Mg2+ ions in the reactions of aminoacyl-tRNA synthetases may be closely connected with the structure of the ATP-cation complex. In our previous work substrate specificities of phenylalanyl-tRNA and seryltRNA synthetases from baker's yeast with regard to ATP analogs showed some evidence for a metal ion-ATP complex as substrate in which the metal ion is coordinated to oxygen atoms of the phosphate moiety and to the N(7) atom of the adenine moiety [ I l l . In this complex ATP would have to exhibit an anti conformation. From studies with methionyl-tRNA synthetase and nucleoside analogs it was supposed that this synthetase perhaps uses a metal ion-ATP complex with coordination of the metal ion to the N(l) or N(3) atom of the adenine moiety and to phosphate oxygens [12]. This complex requires a syn conformation of ATP. Therefore further investigation of the substrate specificity with regard to ATP analogs in

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Section: Resultsmentioning

confidence: 99%

Section: Triphosphatesmentioning

confidence: 99%

Valyl‐tRNA, Isoleucyl‐tRNA and Tyrosyl‐tRNA Synthetase from Baker's Yeast

Freist¹,

Haar²,

Faulhammer³

et al. 1976

European Journal of Biochemistry

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“…The bulky substituent at C-8 ofthe adenine ring introduced some interactions with the H2C-5' of the ribose. These interactions can be minimised either by a 1 8 0 rotation around the glycosidic bond of the adenine ring [21] or by a conformational change at the ribose (C; endo -+ Ci endo). The rotation is determined in the case of 8-bromoadenosine and the conformational change of the ribose in the complex of liver alcohol dehydrogenase with br*ADPR [22].…”

Section: 91mentioning

confidence: 99%

NAD(P)+ Analogues: Tools for the Investigation of the Active Site of Oestradiol 17beta-Dehydrogenase from Human Placenta

Biellmann

Hirth

1975

Eur J Biochem

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Oestradiol‐17β: NAD+ 17‐oxidoreductase from human placenta can accept coenzyme analogues of NAD+ and NADP+ where the amide group is replaced by methyl ketone, nitrile or thioamide. The inhibition with analogues of NAD+ has been studied. The presence of a substituent at C‐3 of the pyridinium ring is necessary for the binding. The inhibition by C‐4 methylated analogues is very poor, and the effect of a methyl group at C‐5 depends on the substituent at C‐3. The 1,4,5,6‐tetra‐hydronicotinamide adenine dinucleotide is a competitive inhibitor. Nicotinamide 8‐bromoadenine dinucleotide and nicotinamide 8‐thioadenine dinucleotide are efficient hydrogen acceptors.

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“…8-Azido-ATP has a C-8 substitution on the adenine ring, which has been shown to restrict the molecule to a syn conformation, i.e. the purine and sugar rings are on the same side of the N-glycosidic bond [42]. In contrast, C-2 substitution does not seem to affect the rotation of the bond.…”

Section: Discussionmentioning

confidence: 99%

Analysis of a nucleotide-binding site of 5-lipoxygenase by affinity labelling: binding characteristics and amino acid sequences

Hammarberg

Rådmark

Samuelsson

et al. 2000

Biochemical Journal

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5-Lipoxygenase (5LO) catalyses the first two steps in the biosynthesis of leukotrienes, which are inflammatory mediators derived from arachidonic acid. 5LO activity is stimulated by ATP ; however, a consensus ATP-binding site or nucleotidebinding site has not been found in its protein sequence. In the present study, affinity and photoaffinity labelling of 5LO with 5h-p-fluorosulphonylbenzoyladenosine (FSBA) and 2-azido-ATP showed that 5LO bound to the ATP analogues quantitatively and specifically and that the incorporation of either analogue inhibited ATP stimulation of 5LO activity. The stoichiometry of the labelling was 1.4 mol of FSBA\mol of 5LO (of which ATP competed with 1 mol\mol) or 0.94 mol of 2-azido-ATP\mol of 5LO (of which ATP competed with 0.77 mol\mol). Labelling with FSBA prevented further labelling with 2-azido-ATP, indicating that the same binding site was occupied by both analogues. Other nucleotides (ADP, AMP, GTP, CTP and UTP) also competed with 2-azido-ATP labelling, suggesting that the site

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Crystal and molecular structure of 8-bromoguanosine and 8-bromoadenosine, two purine nucleosides in the syn conformation

Cited by 207 publications

References 9 publications

Valyl‐tRNA, Isoleucyl‐tRNA and Tyrosyl‐tRNA Synthetase from Baker's Yeast

Valyl‐tRNA, Isoleucyl‐tRNA and Tyrosyl‐tRNA Synthetase from Baker's Yeast

NAD(P)+ Analogues: Tools for the Investigation of the Active Site of Oestradiol 17beta-Dehydrogenase from Human Placenta

Analysis of a nucleotide-binding site of 5-lipoxygenase by affinity labelling: binding characteristics and amino acid sequences

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