Vol 9: 2-O-D-Glucosylglycerol Phosphorylase from Bacillus selenitireducens MLS10 Possessing Hydrolytic Activity on -D-Glucose 1-Phosphate.Report as inadecuate



 Vol 9: 2-O-D-Glucosylglycerol Phosphorylase from Bacillus selenitireducens MLS10 Possessing Hydrolytic Activity on -D-Glucose 1-Phosphate.


Vol 9: 2-O-D-Glucosylglycerol Phosphorylase from Bacillus selenitireducens MLS10 Possessing Hydrolytic Activity on -D-Glucose 1-Phosphate. - Download this document for free, or read online. Document in PDF available to download.

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This article is from PLoS ONE, volume 9.AbstractThe glycoside hydrolase family GH 65 is a family of inverting phosphorylases that act on α-glucosides. A GH65 protein Bsel 2816 from Bacillus selenitireducens MLS10 exhibited inorganic phosphate Pi-dependent hydrolysis of kojibiose at the rate of 0.43 s−1. No carbohydrate acted as acceptor for the reverse phosphorolysis using β-d-glucose 1-phosphate βGlc1P as donor. During the search for a suitable acceptor, we found that Bsel 2816 possessed hydrolytic activity on βGlc1P with a kcat of 2.8 s−1; moreover, such significant hydrolytic activity on sugar 1-phosphate had not been reported for any inverting phosphorylase. The H218O incorporation experiment and the anomeric analysis during the hydrolysis of βGlc1P revealed that the hydrolysis was due to the glucosyl-transferring reaction to a water molecule and not a phosphatase-type reaction. Glycerol was found to be the best acceptor to generate 2-O-α-d-glucosylglycerol GG at the rate of 180 s−1. Bsel 2816 phosphorolyzed GG through sequential Bi-Bi mechanism with a kcat of 95 s−1. We propose 2-O-α-d-glucopyranosylglycerol: phosphate β-d-glucosyltransferase as the systematic name and 2-O-α-d-glucosylglycerol phosphorylase as the short name for Bsel 2816. This is the first report describing a phosphorylase that utilizes polyols, and not carbohydrates, as suitable acceptor substrates.



Author: Nihira, Takanori; Saito, Yuka; Ohtsubo, Ken'ichi; Nakai, Hiroyuki; Kitaoka, Motomitsu

Source: https://archive.org/







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