Kinetics of substrate transglycosylation by glycoside hydrolase family 3 glucan (1-->3)-beta-glucosidase from the white-rot fungus Phanerochaete chrysosporium.
Identifieur interne : 000870 ( Main/Corpus ); précédent : 000869; suivant : 000871Kinetics of substrate transglycosylation by glycoside hydrolase family 3 glucan (1-->3)-beta-glucosidase from the white-rot fungus Phanerochaete chrysosporium.
Auteurs : Rie Kawai ; Kiyohiko Igarashi ; Motomitsu Kitaoka ; Tadashi Ishii ; Masahiro SamejimaSource :
- Carbohydrate research [ 0008-6215 ] ; 2004.
English descriptors
- KwdEn :
- Carbohydrate Sequence (MeSH), Chromatography, Thin Layer (MeSH), Disaccharides (metabolism), Glucan 1,3-beta-Glucosidase (antagonists & inhibitors), Glucan 1,3-beta-Glucosidase (metabolism), Glycosylation (MeSH), Kinetics (MeSH), Oligosaccharides (MeSH), Phanerochaete (enzymology), Substrate Specificity (MeSH).
- MESH :
- chemical , antagonists & inhibitors : Glucan 1,3-beta-Glucosidase.
- chemical , metabolism : Disaccharides, Glucan 1,3-beta-Glucosidase.
- enzymology : Phanerochaete.
- Carbohydrate Sequence, Chromatography, Thin Layer, Glycosylation, Kinetics, Oligosaccharides, Substrate Specificity.
Abstract
To elucidate the interaction between substrate inhibition and substrate transglycosylation of retaining glycoside hydrolases (GHs), a steady-state kinetic study was performed for the GH family 3 glucan (1-->3)-beta-glucosidase from the white-rot fungus Phanerochaete chrysosporium, using laminarioligosaccharides as substrates. When laminaribiose was incubated with the enzyme, a transglycosylation product was detected by thin-layer chromatography. The product was purified by size-exclusion chromatography, and was identified as a 6-O-glucosyl-laminaribiose (beta-D-Glcp-(1-->6)-beta-D-Glcp-(1-->3)-D-Glc) by 1H NMR spectroscopy and electrospray ionization mass spectrometry analysis. In steady-state kinetic studies, an apparent decrease of laminaribiose hydrolysis was observed at high concentrations of the substrate, and the plots of glucose production versus substrate concentration were thus fitted to a modified Michaelis-Menten equation including hydrolytic and transglycosylation parameters (K(m), K(m2), k(cat), k(cat2)). The rate of 6-O-glucosyl-laminaribiose production estimated by high-performance anion-exchange chromatography coincided with the theoretical rate calculated using these parameters, clearly indicating that substrate inhibition of this enzyme is fully explained by substrate transglycosylation. Moreover, when K(m), k(cat), and affinity for glucosyl-enzyme intermediates (K(m2)) were estimated for laminarioligosaccharides (DP=3-5), the K(m) value of laminaribiose was approximately 5-9 times higher than those of the other oligosaccharides (DP=3-5), whereas the K(m2) values were independent of the DP of the substrates. The kinetics of transglycosylation by the enzyme could be well interpreted in terms of the subsite affinities estimated from the hydrolytic parameters (K(m) and k(cat)), and a possible mechanism of transglycosylation is proposed.
DOI: 10.1016/j.carres.2004.09.019
PubMed: 15582611
Links to Exploration step
pubmed:15582611Le document en format XML
<record><TEI><teiHeader><fileDesc><titleStmt><title xml:lang="en">Kinetics of substrate transglycosylation by glycoside hydrolase family 3 glucan (1-->3)-beta-glucosidase from the white-rot fungus Phanerochaete chrysosporium.</title>
<author><name sortKey="Kawai, Rie" sort="Kawai, Rie" uniqKey="Kawai R" first="Rie" last="Kawai">Rie Kawai</name>
<affiliation><nlm:affiliation>Department of Biomaterials Sciences, Graduate School of Agricultural and Life Sciences, The University of Tokyo, 1-1-1 Yayoi, Bunkyo-ku, Tokyo 113-8657, Japan.</nlm:affiliation>
</affiliation>
</author>
<author><name sortKey="Igarashi, Kiyohiko" sort="Igarashi, Kiyohiko" uniqKey="Igarashi K" first="Kiyohiko" last="Igarashi">Kiyohiko Igarashi</name>
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<author><name sortKey="Kitaoka, Motomitsu" sort="Kitaoka, Motomitsu" uniqKey="Kitaoka M" first="Motomitsu" last="Kitaoka">Motomitsu Kitaoka</name>
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<author><name sortKey="Ishii, Tadashi" sort="Ishii, Tadashi" uniqKey="Ishii T" first="Tadashi" last="Ishii">Tadashi Ishii</name>
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<author><name sortKey="Samejima, Masahiro" sort="Samejima, Masahiro" uniqKey="Samejima M" first="Masahiro" last="Samejima">Masahiro Samejima</name>
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<sourceDesc><biblStruct><analytic><title xml:lang="en">Kinetics of substrate transglycosylation by glycoside hydrolase family 3 glucan (1-->3)-beta-glucosidase from the white-rot fungus Phanerochaete chrysosporium.</title>
<author><name sortKey="Kawai, Rie" sort="Kawai, Rie" uniqKey="Kawai R" first="Rie" last="Kawai">Rie Kawai</name>
<affiliation><nlm:affiliation>Department of Biomaterials Sciences, Graduate School of Agricultural and Life Sciences, The University of Tokyo, 1-1-1 Yayoi, Bunkyo-ku, Tokyo 113-8657, Japan.</nlm:affiliation>
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<author><name sortKey="Igarashi, Kiyohiko" sort="Igarashi, Kiyohiko" uniqKey="Igarashi K" first="Kiyohiko" last="Igarashi">Kiyohiko Igarashi</name>
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<author><name sortKey="Kitaoka, Motomitsu" sort="Kitaoka, Motomitsu" uniqKey="Kitaoka M" first="Motomitsu" last="Kitaoka">Motomitsu Kitaoka</name>
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<author><name sortKey="Ishii, Tadashi" sort="Ishii, Tadashi" uniqKey="Ishii T" first="Tadashi" last="Ishii">Tadashi Ishii</name>
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<author><name sortKey="Samejima, Masahiro" sort="Samejima, Masahiro" uniqKey="Samejima M" first="Masahiro" last="Samejima">Masahiro Samejima</name>
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<series><title level="j">Carbohydrate research</title>
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<profileDesc><textClass><keywords scheme="KwdEn" xml:lang="en"><term>Carbohydrate Sequence (MeSH)</term>
<term>Chromatography, Thin Layer (MeSH)</term>
<term>Disaccharides (metabolism)</term>
<term>Glucan 1,3-beta-Glucosidase (antagonists & inhibitors)</term>
<term>Glucan 1,3-beta-Glucosidase (metabolism)</term>
<term>Glycosylation (MeSH)</term>
<term>Kinetics (MeSH)</term>
<term>Oligosaccharides (MeSH)</term>
<term>Phanerochaete (enzymology)</term>
<term>Substrate Specificity (MeSH)</term>
</keywords>
<keywords scheme="MESH" type="chemical" qualifier="antagonists & inhibitors" xml:lang="en"><term>Glucan 1,3-beta-Glucosidase</term>
</keywords>
<keywords scheme="MESH" type="chemical" qualifier="metabolism" xml:lang="en"><term>Disaccharides</term>
<term>Glucan 1,3-beta-Glucosidase</term>
</keywords>
<keywords scheme="MESH" qualifier="enzymology" xml:lang="en"><term>Phanerochaete</term>
</keywords>
<keywords scheme="MESH" xml:lang="en"><term>Carbohydrate Sequence</term>
<term>Chromatography, Thin Layer</term>
<term>Glycosylation</term>
<term>Kinetics</term>
<term>Oligosaccharides</term>
<term>Substrate Specificity</term>
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<front><div type="abstract" xml:lang="en">To elucidate the interaction between substrate inhibition and substrate transglycosylation of retaining glycoside hydrolases (GHs), a steady-state kinetic study was performed for the GH family 3 glucan (1-->3)-beta-glucosidase from the white-rot fungus Phanerochaete chrysosporium, using laminarioligosaccharides as substrates. When laminaribiose was incubated with the enzyme, a transglycosylation product was detected by thin-layer chromatography. The product was purified by size-exclusion chromatography, and was identified as a 6-O-glucosyl-laminaribiose (beta-D-Glcp-(1-->6)-beta-D-Glcp-(1-->3)-D-Glc) by 1H NMR spectroscopy and electrospray ionization mass spectrometry analysis. In steady-state kinetic studies, an apparent decrease of laminaribiose hydrolysis was observed at high concentrations of the substrate, and the plots of glucose production versus substrate concentration were thus fitted to a modified Michaelis-Menten equation including hydrolytic and transglycosylation parameters (K(m), K(m2), k(cat), k(cat2)). The rate of 6-O-glucosyl-laminaribiose production estimated by high-performance anion-exchange chromatography coincided with the theoretical rate calculated using these parameters, clearly indicating that substrate inhibition of this enzyme is fully explained by substrate transglycosylation. Moreover, when K(m), k(cat), and affinity for glucosyl-enzyme intermediates (K(m2)) were estimated for laminarioligosaccharides (DP=3-5), the K(m) value of laminaribiose was approximately 5-9 times higher than those of the other oligosaccharides (DP=3-5), whereas the K(m2) values were independent of the DP of the substrates. The kinetics of transglycosylation by the enzyme could be well interpreted in terms of the subsite affinities estimated from the hydrolytic parameters (K(m) and k(cat)), and a possible mechanism of transglycosylation is proposed.</div>
</front>
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<Title>Carbohydrate research</Title>
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<ArticleTitle>Kinetics of substrate transglycosylation by glycoside hydrolase family 3 glucan (1-->3)-beta-glucosidase from the white-rot fungus Phanerochaete chrysosporium.</ArticleTitle>
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<Abstract><AbstractText>To elucidate the interaction between substrate inhibition and substrate transglycosylation of retaining glycoside hydrolases (GHs), a steady-state kinetic study was performed for the GH family 3 glucan (1-->3)-beta-glucosidase from the white-rot fungus Phanerochaete chrysosporium, using laminarioligosaccharides as substrates. When laminaribiose was incubated with the enzyme, a transglycosylation product was detected by thin-layer chromatography. The product was purified by size-exclusion chromatography, and was identified as a 6-O-glucosyl-laminaribiose (beta-D-Glcp-(1-->6)-beta-D-Glcp-(1-->3)-D-Glc) by 1H NMR spectroscopy and electrospray ionization mass spectrometry analysis. In steady-state kinetic studies, an apparent decrease of laminaribiose hydrolysis was observed at high concentrations of the substrate, and the plots of glucose production versus substrate concentration were thus fitted to a modified Michaelis-Menten equation including hydrolytic and transglycosylation parameters (K(m), K(m2), k(cat), k(cat2)). The rate of 6-O-glucosyl-laminaribiose production estimated by high-performance anion-exchange chromatography coincided with the theoretical rate calculated using these parameters, clearly indicating that substrate inhibition of this enzyme is fully explained by substrate transglycosylation. Moreover, when K(m), k(cat), and affinity for glucosyl-enzyme intermediates (K(m2)) were estimated for laminarioligosaccharides (DP=3-5), the K(m) value of laminaribiose was approximately 5-9 times higher than those of the other oligosaccharides (DP=3-5), whereas the K(m2) values were independent of the DP of the substrates. The kinetics of transglycosylation by the enzyme could be well interpreted in terms of the subsite affinities estimated from the hydrolytic parameters (K(m) and k(cat)), and a possible mechanism of transglycosylation is proposed.</AbstractText>
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