enzyme homology structure modeling and molecular dynamics simulations, overview. Nucleophilic attack on C1' by the carboxylate of the catalytic residue Glu85. Pro11 and Pro42 play a prominent role in making up the active site cavity where one of the Asp79 carboxylate oxygens and the carboxamide nitrogen of Asn113 recognize the O5' of the sugar moiety of the substrate while the backbone NH of Ala10 hydrogen bonds to O3'. The heteroaromatic ring of the nucleobase thus gets sandwiched between the phenyl rings of Phe12 and Phe13, on one side and the hydrophobic sidechains of Phe56 and Leu119 on the opposite side. The Met120 side chain sulfur appears close to the H1' atom, which suggests that it likely plays a role, together with the carboxylate of Asp62, in stabilization of the oxocarbenium reaction intermediate
enzyme homology structure modeling and molecular dynamics simulations, overview. Nucleophilic attack on C1' by the carboxylate of the catalytic residue Glu85. Pro11 and Pro42 play a prominent role in making up the active site cavity where one of the Asp79 carboxylate oxygens and the carboxamide nitrogen of Asn113 recognize the O5' of the sugar moiety of the substrate while the backbone NH of Ala10 hydrogen bonds to O3'. The heteroaromatic ring of the nucleobase thus gets sandwiched between the phenyl rings of Phe12 and Phe13, on one side and the hydrophobic sidechains of Phe56 and Leu119 on the opposite side. The Met120 side chain sulfur appears close to the H1' atom, which suggests that it likely plays a role, together with the carboxylate of Asp62, in stabilization of the oxocarbenium reaction intermediate
enzyme homology structure modeling and molecular dynamics simulations, overview. Nucleophilic attack on C1' by the carboxylate of the catalytic residue Glu85. Pro11 and Pro42 play a prominent role in making up the active site cavity where one of the Asp79 carboxylate oxygens and the carboxamide nitrogen of Asn113 recognize the O5' of the sugar moiety of the substrate while the backbone NH of Ala10 hydrogen bonds to O3'. The heteroaromatic ring of the nucleobase thus gets sandwiched between the phenyl rings of Phe12 and Phe13, on one side and the hydrophobic sidechains of Phe56 and Leu119 on the opposite side. The Met120 side chain sulfur appears close to the H1' atom, which suggests that it likely plays a role, together with the carboxylate of Asp62, in stabilization of the oxocarbenium reaction intermediate
enzyme homology structure modeling and molecular dynamics simulations, overview. Nucleophilic attack on C1' by the carboxylate of the catalytic residue Glu85. Pro11 and Pro42 play a prominent role in making up the active site cavity where one of the Asp79 carboxylate oxygens and the carboxamide nitrogen of Asn113 recognize the O5' of the sugar moiety of the substrate while the backbone NH of Ala10 hydrogen bonds to O3'. The heteroaromatic ring of the nucleobase thus gets sandwiched between the phenyl rings of Phe12 and Phe13, on one side and the hydrophobic sidechains of Phe56 and Leu119 on the opposite side. The Met120 side chain sulfur appears close to the H1' atom, which suggests that it likely plays a role, together with the carboxylate of Asp62, in stabilization of the oxocarbenium reaction intermediate
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PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
recombinant N-terminally His6-tagged enzyme AvNRT from Escherichia coli strain BL21(DE3) by nickel affinity chromatography and preparative gel filtration
the enzyme is a thermophilic and halotolerant biocatalyst that is successfully employed in the synthesis of different purine ribonucleoside analogues, potential of AvNRT as an industrial biocatalyst for the synthesis of nucleoside analogues
the enzyme is a thermophilic and halotolerant biocatalyst that is successfully employed in the synthesis of different purine ribonucleoside analogues, potential of AvNRT as an industrial biocatalyst for the synthesis of nucleoside analogues
the enzyme is a thermophilic and halotolerant biocatalyst that is successfully employed in the synthesis of different purine ribonucleoside analogues, potential of AvNRT as an industrial biocatalyst for the synthesis of nucleoside analogues