Synthesis of regioisomeric methyl α-l-arabinofuranobiosides

Kawabata, Yasuyuki; Kaneko, Satoshi; Kusakabe, Isao; Gama, Yasuo

doi:10.1016/0008-6215(94)00290-v

Cited by 43 publications

(23 citation statements)

References 17 publications

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“…␣-1,5-L-Arabinofuranooligosaccharides with degrees of polymerization ranging from 2 to 5 were obtained from Megazyme (Wicklow, Ireland). Methyl 2-O-, methyl 3-O-, and methyl 5-O-␣-L-arabinofuranosyl-␣-Larabinofuranosides (L-arabinofuranobioses) were prepared as previously reported (22).…”

Section: Methodsmentioning

confidence: 99%

Crystal Structure of an Exo-1,5-α-l-arabinofuranosidase from Streptomyces avermitilis Provides Insights into the Mechanism of Substrate Discrimination between Exo- and Endo-type Enzymes in Glycoside Hydrolase Family 43*

Fujimoto

Ichinose

Maehara

et al. 2010

Journal of Biological Chemistry

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Exo-1,5-␣-L-arabinofuranosidases belonging to glycoside hydrolase family 43 have strict substrate specificity. These enzymes hydrolyze only the ␣-1,5-linkages of linear arabinan and arabino-oligosaccharides in an exo-acting manner. The enzyme from Streptomyces avermitilis contains a core catalytic domain belonging to glycoside hydrolase family 43 and a C-terminal arabinan binding module belonging to carbohydrate binding module family 42. We determined the crystal structure of intact exo-1,5-␣-L-arabinofuranosidase. The catalytic module is composed of a 5-bladed ␤-propeller topologically identical to the other family 43 enzymes. The arabinan binding module had three similar subdomains assembled against one another around a pseudo-3-fold axis, forming a ␤-trefoil-fold. A sugar complex structure with ␣-1,5-L-arabinofuranotriose revealed three subsites in the catalytic domain, and a sugar complex structure with ␣-L-arabinofuranosyl azide revealed three arabinose-binding sites in the carbohydrate binding module. A mutagenesis study revealed that substrate specificity was regulated by residues Asn-159, Tyr-192, and Leu-289 located at the aglycon side of the substrate-binding pocket. The exo-acting manner of the enzyme was attributed to the strict pocket structure of subsite ؊1, formed by the flexible loop region Tyr-281-Arg-294 and the side chain of Tyr-40, which occupied the positions corresponding to the catalytic glycon cleft of GH43 endo-acting enzymes.L-Arabinose residues are widely distributed in plant cell walls, where they are present in polymers such as arabinans, arabinoxylans, arabinogalactans, and arabinogalactan proteins (1). Research on plant cell walls is becoming a necessity because worldwide attention has now focused on bioethanol production to combat global warming and to improve global energy security. Because of competition between food and fuel, lignocellulose is expected to be used as a material for fuel ethanol production in the future. Generally, lignocellulose contains cellulose, which makes up ϳ40% of the total amount of cell wall components, together with ϳ20% hemicellulose, which is mainly composed of pentoses such as xylose and arabinose (2). Hemicelluloses often become bad factors in bioethanol production because the efficiency of ethanol conversion from pentoses is significantly lower than that from hexoses (3, 4).In contrast, L-arabinose is used as a functional sugar in the food industry. This sugar has a sweet taste and selectively inhibits intestinal sucrase activity in a noncompetitive manner and consequently suppresses plasma glucose increase due to sucrose ingestion (5-7). Therefore, L-arabinose may also be useful in preventing excess sucrose utilization.Because the structure of L-arabinose-containing polysaccharides is highly variable and complex, a wide variety of ␣-L-arabinofuranosidases (EC 3.2.1.55) that have various substrate specificities are necessary for the hydrolysis of such polysaccharides and for the production of L-arabinose. We have previously purified some ␣-L-arabi...

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Section: Methodsmentioning

confidence: 99%

Crystal Structure of an Exo-1,5-α-l-arabinofuranosidase from Streptomyces avermitilis Provides Insights into the Mechanism of Substrate Discrimination between Exo- and Endo-type Enzymes in Glycoside Hydrolase Family 43*

Fujimoto

Ichinose

Maehara

et al. 2010

Journal of Biological Chemistry

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“…p-Nitrophenyl (pNP)-glycosides were purchased from Sigma-Aldrich, MO, USA; sugar beet arabinan and wheat arabinoxylan were purchased from Megazyme, Ireland; larch wood arabinogalactan was purchased from Tokyo Chemical Industry, Japan; and L-arabinose was purchased from Wako Chemicals, Japan. Synthetic 1-O-methylated arabinobioses (Araf␣1,2Araf␣1-OMe, Araf␣1,3Araf␣1-OMe, and Araf␣1,5Araf␣1-OMe) were gifts from S. Kaneko, University of the Ryukyus, Japan (43). Other chemicals were obtained from Nacalai Tesque Inc., Japan.…”

Section: Methodsmentioning

confidence: 99%

Two Novel α- l -Arabinofuranosidases from Bifidobacterium longum subsp. longum Belonging to Glycoside Hydrolase Family 43 Cooperatively Degrade Arabinan

Komeno

Hayamizu

Fujita

et al. 2019

Appl Environ Microbiol

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Arabinose-containing poly- or oligosaccharides are suitable carbohydrate sources for Bifidobacterium longum subsp. longum. However, their degradation pathways are poorly understood. In this study, we cloned and characterized the previously uncharacterized glycoside hydrolase family 43 (GH43) enzymes B. longum subsp. longum ArafC (BlArafC; encoded by BLLJ_1852) and B. longum subsp. longum ArafB (BlArafB; encoded by BLLJ_1853) from B. longum subsp. longum JCM 1217. Both enzymes exhibited α-l-arabinofuranosidase activity toward p-nitrophenyl-α-l-arabinofuranoside but no activity toward p-nitrophenyl-β-d-xylopyranoside. The specificities of the two enzymes for l-arabinofuranosyl linkages were different. BlArafC catalyzed the hydrolysis of α1,2- and α1,3-l-arabinofuranosyl linkages found on the side chains of both arabinan and arabinoxylan. It released l-arabinose 100 times faster from arabinan than from arabinoxylan but did not act on arabinogalactan. On the other hand, BlArafB catalyzed the hydrolysis of the α1,5-l-arabinofuranosyl linkage found on the arabinan backbone. It released l-arabinose from arabinan but not from arabinoxylan or arabinogalactan. Coincubation of BlArafC and BlArafB revealed that these two enzymes are able to degrade arabinan in a synergistic manner. Both enzyme activities were suppressed with EDTA treatment, suggesting that they require divalent metal ions. The GH43 domains of BlArafC and BlArafB are classified into GH43 subfamilies 27 and 22, respectively, but show very low similarity (less than 15% identity) with other biochemically characterized members in the corresponding subfamilies. The B. longum subsp. longum strain lacking the GH43 gene cluster that includes BLLJ_1850 to BLLJ_1853 did not grow in arabinan medium, suggesting that BlArafC and BlArafB are important for assimilation of arabinan. IMPORTANCE We identified two novel α-l-arabinofuranosidases, BlArafC and BlArafB, from B. longum subsp. longum JCM 1217, both of which are predicted to be extracellular membrane-bound enzymes. The former specifically acts on α1,2/3-l-arabinofuranosyl linkages, while the latter acts on the α1,5-l-arabinofuranosyl linkage. These enzymes cooperatively degrade arabinan and are required for the efficient growth of bifidobacteria in arabinan-containing medium. The genes encoding these enzymes are located side by side in a gene cluster involved in metabolic pathways for plant-derived polysaccharides, which may confer adaptability in adult intestines.

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“…Nihon Syokuhin Kakoh (Fuji, Japan) supplied corn hull arabinoxylan. Sugar-beet arabinan and arabinoxylo-oligosaccharides, and methyl 2-O-, methyl 3-O-and methyl 5-O-a-Larabinofuranosyl-a-L-arabinofuranosides (arabinofuranobiosides) were prepared as described previously (Kawabata et al 1995;Yoshida et al 1990). …”

Section: Substratesmentioning

confidence: 99%

Characterization of .ALPHA.-L-arabinofuranosidase related to the secondary cell walls formation in Arabidopsis thaliana

Ichinose

Nishikubo

Demura

et al. 2010

Plant Biotechnology

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Synthesis of regioisomeric methyl α-l-arabinofuranobiosides

Cited by 43 publications

References 17 publications

Crystal Structure of an Exo-1,5-α-l-arabinofuranosidase from Streptomyces avermitilis Provides Insights into the Mechanism of Substrate Discrimination between Exo- and Endo-type Enzymes in Glycoside Hydrolase Family 43*

Crystal Structure of an Exo-1,5-α-l-arabinofuranosidase from Streptomyces avermitilis Provides Insights into the Mechanism of Substrate Discrimination between Exo- and Endo-type Enzymes in Glycoside Hydrolase Family 43*

Two Novel α- l -Arabinofuranosidases from Bifidobacterium longum subsp. longum Belonging to Glycoside Hydrolase Family 43 Cooperatively Degrade Arabinan

Characterization of .ALPHA.-L-arabinofuranosidase related to the secondary cell walls formation in Arabidopsis thaliana

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