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Zarubin, Iu P; Il’icheva, I. A.; Пурыгин, П. П.; Florent'ev, V. L.

doi:10.1023/a:1019587623516

Cited by 3 publications

(6 citation statements)

References 27 publications

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“…We presumed in our previous work [8] that this compound might be a weak analogue of substrate, because the distribution of electrostatic potential calculated in vacuum by STO-3G method turned out to be similar for adenosine and for this nucleoside. The similarity is also preserved in the active site of ADA, since the polarization effects only slightly change the electrostatic potential map.…”

Section: Resultsmentioning

confidence: 96%

“…The 1ADD coordinates from PDB database (the complex of ADA with 1-deazaadenosine) [7] were used for the modeling the complexes. The structure consists of 349 amino acid residues, Zn 2+ ion, 110 water molecules, and a 1-deazaadenosine molecule.…”

Section: Resultsmentioning

confidence: 99%

“…The amino acids of the active site are indicated in the file http:// www.biochem.ucl.ac.uk/bsm/pdbsum/1add/main.html of the 1ADD structure (these are His15, His17, Asp19, Leu58, Phe61, Leu62, Phe65, Arg101, Tyr102, Ser103, Leu106, Met155, Ala183, Glu184, His214, Glu217, His238, Asp295, and Asp296). The water molecules participating in the conformational rearrangements have the following numbers in the PDB file: 4,9,10,12,15,17,18,19,20,35,36,42,76, 77, 78, 82 and 83. Hence, the process of optimization of the complex altogether comprises coordinates of 363 atoms of the enzyme and all the atoms of the nucleosides bound in the active site.…”

Section: Resultsmentioning

confidence: 99%

“…Previously, we have started the study of conformational and electronic properties of a series of isosteric adenosine analogues [7][8][9]. All the derivatives of this series have an intact β -D -ribofuranose residue linked to a purine heterocycle in which some or other positions in cycle are modified, while retaining the location of NH 2 group in position 6 .…”

Section: Introductionmentioning

confidence: 99%

“…1-13 in Table 1) in free state in the pseudorotational N and S areas [7][8][9]. Moreover, the distribution of electrostatic potential was obtained for each of these compounds in the conformation, we called active; i.e., this conformation is most closely similar to the conformation of 1-deazaadenosine complexes with ADA.…”

Section: Introductionmentioning

confidence: 99%

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Theoretical Study of the Structure of Adenosine Deaminase Complexes with Adenosine Analogues: I. Aza-, Deaza-, and Isomeric Azadeazaanalogues of Adenosine

et al. 2005

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The conformational models of the active site of adenosine deaminase (ADA) and its complexes in the basic state with adenosine and 13 isosteric analogues of the aza, deaza, and azadeaza series were constructed. The optimization of the conformational energy of the active site and the nucleoside bound with it in the complex was achieved in the force field of the whole enzyme (the 1ADD structure was used) within the molecular mechanics model using the AMBER 99 potentials. The stable conformational states of each of the complexes, as well as the optimal conformation of the ADA in the absence of ligand, were determined. It was proved that the conformational state that is close to the structure of the ADA complex with 1-deazaadenosine (1ADD) known from the X-ray study corresponds to one of the local minima of the potential surface. Another, a significantly deeper minimum was determined; it differs from the first minimum by the mutual orientation of side chains of amino acid residues. A similar conformational state is optimal for the ADA active site in the absence of the bound ligand. A qualitative correlation exists between the values of potential energies of the complexes in this conformation and the enzymatic activity of ADA toward the corresponding nucleosides. The dynamics of conformational conversions of the active site after the binding of substrate or its analogues, as well as the possibility of the estimation of the inhibitory properties of nucleosides on the basis of calculations, are discussed.

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Section: Resultsmentioning

confidence: 96%

Section: Resultsmentioning

confidence: 99%

Section: Resultsmentioning

confidence: 99%

Section: Introductionmentioning

confidence: 99%

Section: Introductionmentioning

confidence: 99%

See 3 more Smart Citations

Theoretical Study of the Structure of Adenosine Deaminase Complexes with Adenosine Analogues: I. Aza-, Deaza-, and Isomeric Azadeazaanalogues of Adenosine

et al. 2005

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Synthesis of Modified Purine Nucleosides and Related Compounds Mediated by Adenosine Deaminase (ADA) and Adenylate Deaminase (AMPDA)

Santaniello¹,

Ciuffreda²,

Alessandrini³

2005

Synthesis

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Adenosine deaminase (ADA) and adenylic acid deaminase (AMPDA) are enzymes that catalyze the hydrolytic deamination of various purine nucleosides. In light of recent reports, ADA and AMPDA may be considered as valuable biocatalysts in nucleoside chemistry. Here, they can find many synthetic applications in the transformation of purine nucleosides that are modified in the base or the ribose moiety. Their use can be extended to carbocyclonucleosides or acyclonucleosides as well.

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A Concise Synthesis of 25-Hydroxycholesterol from Hyodesoxycholic Acid

Jin

Wang

Sun

et al. 2018

Journal of Chemical Research

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A simple, efficient and economical method has been developed for the synthesis of 25-hydroxycholesterol in seven steps from hyodesoxycholic acid with an overall yield of 39%. The preparation of the 3β-tetrahydropyranyloxychol-5-en-24-al from 3β-tetrahydropyranyloxychol-5-en-24-oic acid methyl ester with di-isobutylaluminium hydride was achieved instead of using the conventional two-step reaction, thus avoiding the use of the toxic oxidant CrO3. The terminal product was obtained by hydroxybromination of desmosterol with N-bromosuccinimide/H20, followed by reduction and deprotection of the halohydrins with LiAlH4. This simplified route gave an increased overall yield and used economical and environmentally benign reagents.

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Untitled

Cited by 3 publications

References 27 publications

Theoretical Study of the Structure of Adenosine Deaminase Complexes with Adenosine Analogues: I. Aza-, Deaza-, and Isomeric Azadeazaanalogues of Adenosine

Theoretical Study of the Structure of Adenosine Deaminase Complexes with Adenosine Analogues: I. Aza-, Deaza-, and Isomeric Azadeazaanalogues of Adenosine

Synthesis of Modified Purine Nucleosides and Related Compounds Mediated by Adenosine Deaminase (ADA) and Adenylate Deaminase (AMPDA)

A Concise Synthesis of 25-Hydroxycholesterol from Hyodesoxycholic Acid

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