Characterization of an Exo-β-1,3-<scp>D</scp>-galactanase from<i>Streptomyces avermitilis</i>NBRC14893 Acting on Arabinogalactan-Proteins

Ichinose, Hitomi; Kotake, Toshihisa; Tsumuraya, Yoichi; Kaneko, Satoshi

doi:10.1271/bbb.60365

Cited by 28 publications

(30 citation statements)

References 22 publications

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“…To date, all characterized exo-␤-1,3-galactanases have greater activity toward ␤-1,3-galactan than ␤-1,3/␤-1,6-galactan from Prototheca zopfii, LWAG, gum arabic, and radish roots (1,(3)(4)(5)(6)(7)21). BLLJ_1840 has low sequence identities (27% to 28%) with other exo-␤-1,3-galactanases.…”

Section: Discussionmentioning

confidence: 99%

“…In particular, exo-␤-1,3-galactanase hydrolyzes the ␤-1,3-galactan backbone, bypassing ␤-1,6-galactan side chains, and consequently releases galactose, ␤-1,6-galactooligosaccharides, and their derivatives (1,2). Exo-␤-1,3-galactanases, which belong to glycoside hydrolase family 43 (GH43), have been cloned and characterized from several sources, including bacteria and fungi (1,(3)(4)(5)(6)(7).…”

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confidence: 99%

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Bifidobacterium longum subsp. longum Exo-β-1,3-Galactanase, an Enzyme for the Degradation of Type II Arabinogalactan

Fujita

Sakaguchi

Sakamoto

et al. 2014

Appl Environ Microbiol

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Type II arabinogalactan (AG-II) is a suitable carbohydrate source for Bifidobacterium longum subsp. longum, but the degradative enzymes have never been characterized. In this study, we characterized an exo-␤-1,3-galactanase, BLLJ_1840, belonging to glycoside hydrolase family 43 from B. longum subsp. longum JCM1217. The recombinant BLLJ_1840 expressed in Escherichia coli hydrolyzed ␤-1,3-linked galactooligosaccharides but not ␤-1,4-and ␤-1,6-linked galactooligosaccharides. The enzyme also hydrolyzed larch wood arabinogalactan (LWAG), which comprises a ␤-1,3-linked galactan backbone with ␤-1,6-linked galactan side chains. The k cat /K m ratio of dearabinosylated LWAG was 24-fold higher than that of ␤-1,3-galactan. BLLJ_1840 is a novel type of exo-␤-1,3-galactanase with a higher affinity for the ␤-1,6-substituted ␤-1,3-galactan than for nonsubstituted ␤-1,3-galactan. BLLJ_1840 has 27% to 28% identities with other characterized exo-␤-1,3-galactanases from bacteria and fungi. The homologous genes are conserved in several strains of B. longum subsp. longum and B. longum subsp. infantis but not in other bifidobacteria. Transcriptional analysis revealed that BLLJ_1840 is intensively induced with BLLJ_1841, an endo-␤-1,6-galactanase candidate, in the presence of LWAG. This is the first report of exo-␤-1,3-galactanase in bifidobacteria, which is an enzyme used for the acquisition of AG-II in B. longum subsp. longum.

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Section: Discussionmentioning

confidence: 99%

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Bifidobacterium longum subsp. longum Exo-β-1,3-Galactanase, an Enzyme for the Degradation of Type II Arabinogalactan

Fujita

Sakaguchi

Sakamoto

et al. 2014

Appl Environ Microbiol

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“…We cloned two kinds of galactanases: exo-␤-1,3-galactanase (EC 3.2.1.145) from Phanerochaete chrysosporium and endo-␤-1,6-galactanase (EC 3.2.1.164) from Trichoderma viride, and demonstrated that the enzymes were novel and could be classified as glycoside hydrolase family 43 (GH43) and family 5 (GH5), respectively (7-9) (see the CAZy website). Genes encoding proteins similar to such enzymes were also identified in the Streptomyces avermitilis genome (10,11).…”

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confidence: 99%

A β-l-Arabinopyranosidase from Streptomyces avermitilis Is a Novel Member of Glycoside Hydrolase Family 27

Ichinose

Fujimoto

Honda

et al. 2009

Journal of Biological Chemistry

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Arabinogalactan proteins (AGPs) are a family of plant cell surface proteoglycans and are considered to be involved in plant growth and development. Because AGPs are very complex molecules, glycoside hydrolases capable of degrading AGPs are powerful tools for analyses of the AGPs. We previously reported such enzymes from Streptomyces avermitilis. Recently, a ␤-Larabinopyranosidase was purified from the culture supernatant of the bacterium, and its corresponding gene was identified. The primary structure of the protein revealed that the catalytic module was highly similar to that of glycoside hydrolase family 27 (GH27) ␣-D-galactosidases. The recombinant protein was successfully expressed as a secreted 64-kDa protein using a Streptomyces expression system. The specific activity toward p-nitrophenyl-␤-L-arabinopyranoside was 18 mol of arabinose/min/mg, which was 67 times higher than that toward pnitrophenyl-␣-D-galactopyranoside. The enzyme could remove 0.1 and 45% L-arabinose from gum arabic or larch arabinogalactan, respectively. X-ray crystallographic analysis reveals that the protein had a GH27 catalytic domain, an antiparallel ␤-domain containing Greek key motifs, another antiparallel ␤-domain forming a jellyroll structure, and a carbohydrate-binding module family 13 domain. Comparison of the structure of this protein with that of ␣-D-galactosidase showed a single amino acid substitution (aspartic acid to glutamic acid) in the catalytic pocket of ␤-L-arabinopyranosidase, and a space for the hydroxymethyl group on the C-5 carbon of D-galactose bound to ␣-galactosidase was changed in ␤-L-arabinopyranosidase. Mutagenesis study revealed that the residue is critical for modulating the enzyme activity. This is the first report in which ␤-L-arabinopyranosidase is classified as a new member of the GH27 family.Arabinogalactan proteins (AGPs) 3 are a family of complex proteoglycans widely distributed in plants (1, 2). AGPs are also found in tree exudate gums and coniferous woods (3) and are characterized by the presence of large amounts of carbohydrate components rich in galactose (all the sugars in the present study are in the D-configuration unless otherwise specified) and L-arabinose and by protein components rich in hydroxyproline, serine, threonine, alanine, and glycine (4). Type II arabinogalactans and short oligosaccharides are the two types of carbohydrates attached to the AGP backbone. Type II arabinogalactans have ␤-1,3-linked galactosyl backbones in mono-or oligo-␤-1,6-galactosyl and/or L-arabinosyl side chains (2, 5). L-Arabinose and lesser amounts of other auxiliary sugars such as glucuronic acid, L-rhamnose, and L-fucose are attached to the side chains primarily at nonreducing termini (2). Molecular and biochemical evidence indicates that AGPs have specific functions during root formation, promotion of somatic embryogenesis, and attraction of pollen tubes to the style (6). However, because many putative protein cores exist and the structures of the carbohydrate moieties are complex, it has been difficult...

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“…These enzymes hydrolyze -1,3-galactan and -1,6-galactan, respectively, which constitute the backbone of the type II arabinogalactan present in AGP sugar linkages. [69][70][71] When the bacterium was cultivated with gum arabic (a kind of AGP) as carbon source, L-arabinose was released from the AGPs, and this led to the isolation of a novel -L-arabinopyranosidase, SaArap27. The sequence of the SaArap27-encoding gene indicated that the protein possessed 614 amino acid residues (after removal of a putative N-terminal signal peptide) and a molecular weight of 64 kDa.…”

Section: Cbm13 Of Streptomyces Avermitilis -L-arabinopyranosidasementioning

confidence: 99%

Structure and Function of Carbohydrate-Binding Module Families 13 and 42 of Glycoside Hydrolases, Comprising a β-Trefoil Fold

Fujimoto

2013

Bioscience, Biotechnology, and Biochemistry

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Characterization of an Exo-β-1,3-D-galactanase fromStreptomyces avermitilisNBRC14893 Acting on Arabinogalactan-Proteins

Cited by 28 publications

References 22 publications

Bifidobacterium longum subsp. longum Exo-β-1,3-Galactanase, an Enzyme for the Degradation of Type II Arabinogalactan

Bifidobacterium longum subsp. longum Exo-β-1,3-Galactanase, an Enzyme for the Degradation of Type II Arabinogalactan

A β-l-Arabinopyranosidase from Streptomyces avermitilis Is a Novel Member of Glycoside Hydrolase Family 27

Structure and Function of Carbohydrate-Binding Module Families 13 and 42 of Glycoside Hydrolases, Comprising a β-Trefoil Fold

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