Enzymatic synthesis of 2'-O-methylribonucleosides with a nucleoside hydrolase family enzyme from Lactobacillus buchneri LBK78
| Autor: | Satomi Takahashi, Nobuyuki Horinouchi, Yuuki Mitsukawa, Jun Ogawa, Makoto Hibi, Narihiro Matsutani |
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| Rok vydání: | 2016 |
| Předmět: |
0301 basic medicine
Adenosine Stereochemistry Bioengineering 01 natural sciences Applied Microbiology and Biotechnology Nucleobase 03 medical and health sciences Hydrolysis Hydrolase otorhinolaryngologic diseases N-Glycosyl Hydrolases Uridine Lactobacillus buchneri chemistry.chemical_classification biology 010405 organic chemistry Substrate (chemistry) biology.organism_classification 0104 chemical sciences Kinetics Lactobacillus 030104 developmental biology Enzyme chemistry Biochemistry Nucleic acid Biocatalysis Nucleoside Biotechnology |
| Zdroj: | Journal of bioscience and bioengineering. 123(6) |
| ISSN: | 1347-4421 |
| Popis: | 2′-O-Methylribonucleosides (2′-OMe-NRs) are promising raw materials for the production of nucleic acid drugs. We previously reported that LbNH, a nucleoside hydrolase from Lactobacillus buchneri LBK78 (NITE P-01581), was the first enzyme found to act on 2′-OMe-NRs. In the present study, we determined that LbNH also has the transribosylation activity between 2′-OMe-NRs and nucleobases, in addition to the hydrolyzing activity towards 2′-OMe-NRs. When 2′-O-methyluridine (2′-OMe-UR) and adenine were reacted with LbNH, 2′-O-methyladenosine (2′-OMe-AR) was produced. LbNH preferred purine nucleobases as its acceptor substrates for the transribosylation with 2′-OMe-UR as a donor substrate. Kinetic analysis of LbNH revealed that adenine behaved as a mixed inhibitor of the hydrolysis of 2′-OMe-UR. Under the optimal reaction conditions, the maximum molar yield of enzymatic 2′-OMe-AR produced reached 0.97% towards 2′-OMe-UR, corresponding to 0.16 g/L. |
| Databáze: | OpenAIRE |
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