The enzyme, which was identified in the bacterium Bifidobacterium longum JCM1217, removes the β-L-arabinofuranose residue from the non-reducing end of multiple substrates, including β-L-arabinofuranosyl-hydroxyproline (Ara-Hyp), Ara2-Hyp, Ara3-Hyp, and β-L-arabinofuranosyl-(1→2)-1-O-methyl-β-L-arabinofuranose.In the presence of 1-alkanols, the enzyme demonstrates transglycosylation activity, retaining the anomeric configuration of the arabinofuranose residue. cf. EC 3.2.1.55, non-reducing end α-L-arabinofuranosidase
The expected taxonomic range for this enzyme is: Bacteria, Archaea
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SYSTEMATIC NAME
IUBMB Comments
beta-L-arabinofuranoside non-reducing end beta-L-arabinofuranosidase
The enzyme, which was identified in the bacterium Bifidobacterium longum JCM1217, removes the beta-L-arabinofuranose residue from the non-reducing end of multiple substrates, including beta-L-arabinofuranosyl-hydroxyproline (Ara-Hyp), Ara2-Hyp, Ara3-Hyp, and beta-L-arabinofuranosyl-(1->2)-1-O-methyl-beta-L-arabinofuranose.In the presence of 1-alkanols, the enzyme demonstrates transglycosylation activity, retaining the anomeric configuration of the arabinofuranose residue. cf. EC 3.2.1.55, non-reducing end alpha-L-arabinofuranosidase
Substrates: no substrates: 4-nitrophenyl-alpha-L-arabinopyranoside, 4-nitrophenyl-alpha-L-arabinofuranoside, 4-nitrophenyl-beta-L-arabinopyranoside, or (beta-L-arabinofuranosyl)4-L-hydroxyproline Products: -
Substrates: no substrates: 4-nitrophenyl-alpha-L-arabinopyranoside, 4-nitrophenyl-alpha-L-arabinofuranoside, 4-nitrophenyl-beta-L-arabinopyranoside, or (beta-L-arabinofuranosyl)4-L-hydroxyproline Products: -
Substrates: substrate specificity, overview. Enzyme XeHypBA1 prefers Ara-Hyp as a substrate and liberates L-arabinose and is only slightly active on beta-Ara2, but does not use Ara4-Hyp and Ara3-Hyp at all. Ara2-Hyp is completely degraded in its dansylated form, but only partially when unmodified Products: -
Substrates: substrate specificity, overview. Enzyme XeHypBA1 prefers Ara-Hyp as a substrate and liberates L-arabinose and is only slightly active on beta-Ara2, but does not use Ara4-Hyp and Ara3-Hyp at all. Ara2-Hyp is completely degraded in its dansylated form, but only partially when unmodified Products: -
Substrates: substrate specificity, overview. Enzyme XeHypBA1 prefers Ara-Hyp as a substrate and liberates L-arabinose and is only slightly active on beta-Ara2, but does not use Ara4-Hyp and Ara3-Hyp at all. Ara2-Hyp is completely degraded in its dansylated form, but only partially when unmodified Products: -
Substrates: substrate specificity, overview. Enzyme XeHypBA1 prefers Ara-Hyp as a substrate and liberates L-arabinose and is only slightly active on beta-Ara2, but does not use Ara4-Hyp and Ara3-Hyp at all. Ara2-Hyp is completely degraded in its dansylated form, but only partially when unmodified Products: -
single deletion mutants of genes XCV2724, XCV2728, and XCV2729 and the triple deletion mutant remain pathogenic, and mutations of the operon or the single genes have no effect on nonhost resistance, either, indicating that these three enzymes are not involved in either pathogenicity or nonhost resistance reactions
single deletion mutants of genes XCV2724, XCV2728, and XCV2729 and the triple deletion mutant remain pathogenic, and mutations of the operon or the single genes have no effect on nonhost resistance, either, indicating that these three enzymes are not involved in either pathogenicity or nonhost resistance reactions
single deletion mutants of genes XCV2724, XCV2728, and XCV2729 and the triple deletion mutant remain pathogenic, and mutations of the operon or the single genes have no effect on nonhost resistance, either, indicating that these three enzymes are not involved in either pathogenicity or nonhost resistance reactions
enzymes XCV2724, XCV2728, and XCV2729 in Xanthomonas euvesicatoria degrade the arabinofuranooligosaccharides present on hydroxyproline (Hyp)-rich glycoproteins (HRGPs) such as extensin and solanaceous lectins in plant cell walls. These enzymes work coordinately to degrade the oligosaccharides. The main oligosaccharide structure of Ara4-Hyp on the HRGPs is degraded to Ara3-Hyp, then to Ara-Hyp, and finally to Ara monosaccharides by the action of these three enzymes. Structure of arabino-oligosaccharides on extensin and solanaceous lectins in plant cell walls, overview. HRGPs containing oligosaccharide substrates have been reported to contribute to plant defense. The enzyme is not involved in either pathogenicity or nonhost resistance reactions
enzymes XCV2724, XCV2728, and XCV2729 in Xanthomonas euvesicatoria degrade the arabinofuranooligosaccharides present on hydroxyproline (Hyp)-rich glycoproteins (HRGPs) such as extensin and solanaceous lectins in plant cell walls. These enzymes work coordinately to degrade the oligosaccharides. The main oligosaccharide structure of Ara4-Hyp on the HRGPs is degraded to Ara3-Hyp, then to Ara-Hyp, and finally to Ara monosaccharides by the action of these three enzymes. Structure of arabino-oligosaccharides on extensin and solanaceous lectins in plant cell walls, overview. HRGPs containing oligosaccharide substrates have been reported to contribute to plant defense. The enzyme is not involved in either pathogenicity or nonhost resistance reactions
enzymes XCV2724, XCV2728, and XCV2729 in Xanthomonas euvesicatoria degrade the arabinofuranooligosaccharides present on hydroxyproline (Hyp)-rich glycoproteins (HRGPs) such as extensin and solanaceous lectins in plant cell walls. These enzymes work coordinately to degrade the oligosaccharides. The main oligosaccharide structure of Ara4-Hyp on the HRGPs is degraded to Ara3-Hyp, then to Ara-Hyp, and finally to Ara monosaccharides by the action of these three enzymes. Structure of arabino-oligosaccharides on extensin and solanaceous lectins in plant cell walls, overview. HRGPs containing oligosaccharide substrates have been reported to contribute to plant defense. The enzyme is not involved in either pathogenicity or nonhost resistance reactions
construction of a single-gene deletion mutant, DELTAxehypBA1 and a triple-gene deletion mutant DELTAxehypBA1-BA2-AA. The mutants remain pathogenic, and mutations of the operon or the single genes XCV2724, XCV2728, and XCV2729 have no effect on nonhost resistance, either, indicating that these three enzymes are not involved in either pathogenicity or nonhost resistance reactions
construction of a single-gene deletion mutant, DELTAxehypBA1 and a triple-gene deletion mutant DELTAxehypBA1-BA2-AA. The mutants remain pathogenic, and mutations of the operon or the single genes XCV2724, XCV2728, and XCV2729 have no effect on nonhost resistance, either, indicating that these three enzymes are not involved in either pathogenicity or nonhost resistance reactions
construction of a single-gene deletion mutant, DELTAxehypBA1 and a triple-gene deletion mutant DELTAxehypBA1-BA2-AA. The mutants remain pathogenic, and mutations of the operon or the single genes XCV2724, XCV2728, and XCV2729 have no effect on nonhost resistance, either, indicating that these three enzymes are not involved in either pathogenicity or nonhost resistance reactions
construction of a single-gene deletion mutant, DELTAxehypBA1 and a triple-gene deletion mutant DELTAxehypBA1-BA2-AA. The mutants remain pathogenic, and mutations of the operon or the single genes XCV2724, XCV2728, and XCV2729 have no effect on nonhost resistance, either, indicating that these three enzymes are not involved in either pathogenicity or nonhost resistance reactions
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CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
gene XCV2724, belongs to operon xehypBA2-AA containing genes XCV2724, XCV2728, and XCV2729, DNA and amino acid sequence determination and analysis, and genetic structure, recombinant expression of wild-type and mutant enzymes without the signal peptide in Escherichia coli strain BL21(DE3), recombinant expression of the operon in transgenic Solanum lycopersicum strain Micro-Tom
Nakamura, M.; Yasukawa, Y.; Furusawa, A.; Fuchiwaki, T.; Honda, T.; Okamura, Y.; Fujita, K.; Iwai, H.
Functional characterization of unique enzymes in Xanthomonas euvesicatoria related to degradation of arabinofurano-oligosaccharides on hydroxyproline-rich glycoproteins