![]() 5'-Deoxyadenosine structure
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Common Name | 5'-Deoxyadenosine | ||
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CAS Number | 4754-39-6 | Molecular Weight | 251.24200 | |
Density | 1.93g/cm3 | Boiling Point | 595ºC at 760 mmHg | |
Molecular Formula | C10H13N5O3 | Melting Point | 210-212 °C | |
MSDS | USA | Flash Point | 313.6ºC |
Characterization of RimO, a new member of the methylthiotransferase subclass of the radical SAM superfamily.
Biochemistry 48(42) , 10162-74, (2009) RimO, encoded by the yliG gene in Escherichia coli, has been recently identified in vivo as the enzyme responsible for the attachment of a methylthio group on the beta-carbon of Asp88 of the small ribosomal protein S12 [Anton, B. P., Saleh, L., Benner, J. S.,... |
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The ONIOM Method and Its Applications.
Chem. Rev. 115 , 5678-796, (2015)
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Radical triplets and suicide inhibition in reactions of 4-thia-D- and 4-thia-L-lysine with lysine 5,6-aminomutase.
Biochemistry 48(34) , 8151-60, (2009) Lysine 5,6-aminomutase (5,6-LAM) catalyzes the interconversions of D- or L-lysine and the corresponding enantiomers of 2,5-diaminohexanoate, as well as the interconversion of L-beta-lysine and l-3,5-diaminohexanoate. The reactions of 5,6-LAM are 5'-deoxyadeno... |
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An automatic method to generate force-field parameters for hetero-compounds.
Acta Crystallogr. D Biol. Crystallogr. 59(Pt 2) , 274-89, (2003) A program, Hess2FF, has been developed that automatically constructs parameter and topology files to be used in crystallographic refinement for any molecule, based on a Hessian (force-constant) matrix estimated by any method. The program is tested by redefini... |
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Interconversion of (S)-glutamate and (2S,3S)-3-methylaspartate: a distinctive B(12)-dependent carbon-skeleton rearrangement.
J. Am. Chem. Soc. 123(33) , 7963-72, (2001) The interconversion of (S)-glutamate and (2S,3S)-3-methylaspartate catalyzed by B(12)-dependent glutamate mutase is discussed using results from high-level ab initio molecular orbital calculations. Evidence is presented regarding the possible role of coenzyme... |
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Hydrogen tunneling in adenosylcobalamin-dependent glutamate mutase: evidence from intrinsic kinetic isotope effects measured by intramolecular competition.
Biochemistry 49(14) , 3168-73, (2010) Hydrogen atom transfer reactions between the substrate and coenzyme are key mechanistic features of all adenosylcobalamin-dependent enzymes. For one of these enzymes, glutamate mutase, we have investigated whether hydrogen tunneling makes a significant contri... |
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Biotin synthase exhibits burst kinetics and multiple turnovers in the absence of inhibition by products and product-related biomolecules.
Biochemistry 49(46) , 9985-96, (2010) Biotin synthase (BS) is a member of the "SAM radical" superfamily of enzymes, which catalyze reactions in which the reversible or irreversible oxidation of various substrates is coupled to the reduction of the S-adenosyl-l-methionine (AdoMet) sulfonium to gen... |
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Radical SAM activation of the B12-independent glycerol dehydratase results in formation of 5'-deoxy-5'-(methylthio)adenosine and not 5'-deoxyadenosine.
Biochemistry 50 , 440-442, (2011) Activation of glycyl radical enzymes (GREs) by S-adenosylmethonine (AdoMet or SAM)-dependent enzymes has long been shown to proceed via the reductive cleavage of SAM. The AdoMet-dependent (or radical SAM) enzymes catalyze this reaction by using a [4Fe-4S] clu... |
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Inhibition of erythroblast growth and fetal hemoglobin production by ribofuranose-substituted adenosine derivatives.
Biochim. Biophys. Acta 1782(9) , 504-10, (2008) In vivo, inhibition of fetal hemoglobin (HbF) expression in humans around the time of birth causes the clinical manifestation of sickle cell and beta-thalassemia syndromes. Inhibition of HbF among cultured cells was recently described by the adenosine derivat... |
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NMR observations of 13C-enriched coenzyme B12 bound to the ribonucleotide reductase from Lactobacillus leichmannii.
Inorg. Chem. 45(23) , 9172-4, (2006) The 13C NMR resonance and one-bond 1H-13C coupling constants of coenzyme B12 enriched in 13C in the cobalt-bound carbon have been observed in the complex of the coenzyme with the B12-dependent ribonucleotide reductase from Lactobacillus leichmannii. Neither t... |