Enzymatic synthesis of 2'-O-methylribonucleosides with a nucleoside hydrolase family enzyme from Lactobacillus buchneri LBK78.
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.
['Mitsukawa|Yuuki|Y|', 'Hibi|Makoto|M|', 'Matsutani|Narihiro|N|', 'Horinouchi|Nobuyuki|N|', 'Takahashi|Satomi|S|', 'Ogawa|Jun|J|']
D000241:Adenosine D055162:Biocatalysis D006868:Hydrolysis D007700:Kinetics D007778:Lactobacillus D009699:N-Glycosyl Hydrolases D014529:Uridine
Nucleoside hydrolase Lactobacillus buchneri Nucleic acid drugs Transribosylation 2′-O-Methylribonucleosides