2-O-α-D-glucosylglycerol phosphorylase from Bacillus selenitireducens MLS10 possessing hydrolytic activity on β-D-glucose 1-phosphate.

The 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 f...

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Autores principales:	Takanori Nihira, Yuka Saito, Ken'ichi Ohtsubo, Hiroyuki Nakai, Motomitsu Kitaoka
Formato:	article
Lenguaje:	EN
Publicado:	Public Library of Science (PLoS) 2014
Materias:	Medicine R Science Q
Acceso en línea:	https://doaj.org/article/3bfc6eba0d9642bd859a1c89435a4f4f
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spelling	oai:doaj.org-article:3bfc6eba0d9642bd859a1c89435a4f4f2021-11-18T08:36:23Z2-O-α-D-glucosylglycerol phosphorylase from Bacillus selenitireducens MLS10 possessing hydrolytic activity on β-D-glucose 1-phosphate.1932-620310.1371/journal.pone.0086548https://doaj.org/article/3bfc6eba0d9642bd859a1c89435a4f4f2014-01-01T00:00:00Zhttps://www.ncbi.nlm.nih.gov/pmc/articles/pmid/24466148/?tool=EBIhttps://doaj.org/toc/1932-6203The 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 k cat of 2.8 s(-1); moreover, such significant hydrolytic activity on sugar 1-phosphate had not been reported for any inverting phosphorylase. The H2 (18)O 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 k cat 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.Takanori NihiraYuka SaitoKen'ichi OhtsuboHiroyuki NakaiMotomitsu KitaokaPublic Library of Science (PLoS)articleMedicineRScienceQENPLoS ONE, Vol 9, Iss 1, p e86548 (2014)
institution	DOAJ
collection	DOAJ
language	EN
topic	Medicine R Science Q
spellingShingle	Medicine R Science Q Takanori Nihira Yuka Saito Ken'ichi Ohtsubo Hiroyuki Nakai Motomitsu Kitaoka 2-O-α-D-glucosylglycerol phosphorylase from Bacillus selenitireducens MLS10 possessing hydrolytic activity on β-D-glucose 1-phosphate.
description	The 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 k cat of 2.8 s(-1); moreover, such significant hydrolytic activity on sugar 1-phosphate had not been reported for any inverting phosphorylase. The H2 (18)O 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 k cat 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.
format	article
author	Takanori Nihira Yuka Saito Ken'ichi Ohtsubo Hiroyuki Nakai Motomitsu Kitaoka
author_facet	Takanori Nihira Yuka Saito Ken'ichi Ohtsubo Hiroyuki Nakai Motomitsu Kitaoka
author_sort	Takanori Nihira
title	2-O-α-D-glucosylglycerol phosphorylase from Bacillus selenitireducens MLS10 possessing hydrolytic activity on β-D-glucose 1-phosphate.
title_short	2-O-α-D-glucosylglycerol phosphorylase from Bacillus selenitireducens MLS10 possessing hydrolytic activity on β-D-glucose 1-phosphate.
title_full	2-O-α-D-glucosylglycerol phosphorylase from Bacillus selenitireducens MLS10 possessing hydrolytic activity on β-D-glucose 1-phosphate.
title_fullStr	2-O-α-D-glucosylglycerol phosphorylase from Bacillus selenitireducens MLS10 possessing hydrolytic activity on β-D-glucose 1-phosphate.
title_full_unstemmed	2-O-α-D-glucosylglycerol phosphorylase from Bacillus selenitireducens MLS10 possessing hydrolytic activity on β-D-glucose 1-phosphate.
title_sort	2-o-α-d-glucosylglycerol phosphorylase from bacillus selenitireducens mls10 possessing hydrolytic activity on β-d-glucose 1-phosphate.
publisher	Public Library of Science (PLoS)
publishDate	2014
url	https://doaj.org/article/3bfc6eba0d9642bd859a1c89435a4f4f
work_keys_str_mv	AT takanorinihira 2oadglucosylglycerolphosphorylasefrombacillusselenitireducensmls10possessinghydrolyticactivityonbdglucose1phosphate AT yukasaito 2oadglucosylglycerolphosphorylasefrombacillusselenitireducensmls10possessinghydrolyticactivityonbdglucose1phosphate AT kenichiohtsubo 2oadglucosylglycerolphosphorylasefrombacillusselenitireducensmls10possessinghydrolyticactivityonbdglucose1phosphate AT hiroyukinakai 2oadglucosylglycerolphosphorylasefrombacillusselenitireducensmls10possessinghydrolyticactivityonbdglucose1phosphate AT motomitsukitaoka 2oadglucosylglycerolphosphorylasefrombacillusselenitireducensmls10possessinghydrolyticactivityonbdglucose1phosphate
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2-O-α-D-glucosylglycerol phosphorylase from Bacillus selenitireducens MLS10 possessing hydrolytic activity on β-D-glucose 1-phosphate.

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