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Enzyme Nomenclature
Information on EC 3.2.1.185 - non-reducing end beta-L-arabinofuranosidase
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EC Tree
3.2.1.185 non-reducing end beta-L-arabinofuranosidaseIUBMB Comments
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
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Word Map
- 3.2.1.185
-
bifidobacterium
- longum
- glycoside
- disaccharide
- l-arabinose
-
anomeric
- l-arabinofuranose
- hydrolases
- azide
- oligosaccharides
-
1-alkanols
- actinomycetes
-
transglycosylates
The expected taxonomic range for this enzyme is: Bacteria, Archaea
Reaction Schemes
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SYNONYM 
ORGANISM
UNIPROT
COMMENTARY 
LITERATURE
GH 127 beta-L-arabinofuranosidase
GH127 beta-L-arabinofuranosidase
HypBA1
xcv2724
XeHypBA1
HypBA1
-
-
-
-
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REACTION
REACTION DIAGRAM
COMMENTARY
ORGANISM
UNIPROT
LITERATURE
beta-L-arabinofuranosyl-(1->2)-beta-L-arabinofuranose + H2O = 2 beta-L-arabinofuranose
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-
-
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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
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SUBSTRATE
PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate)
(Substrate)
LITERATURE
(Substrate)
(Substrate)
COMMENTARY
(Product)
(Product)
LITERATURE
(Product)
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
beta-L-arabinofuranosyl-(1->2)-beta-L-arabinofuranosyl-L-hydroxyproline + H2O
2 beta-L-arabinofuranose + L-hydroxyproline
-
-
-
?
beta-L-arabinofuranosyl-(1->2)-beta-L-arabinofuranose + H2O
2 beta-L-arabinofuranose
-
enzyme liberates L-arabinose from the L-arabinofuranose (Ara)-beta1,2-Ara disaccharide
-
?
beta-L-arabinofuranosyl-(1->2)-beta-L-arabinofuranose + H2O
2 beta-L-arabinofuranose
-
-
-
?
beta-L-arabinofuranosyl-(1->2)-beta-L-arabinofuranose + H2O
2 beta-L-arabinofuranose
-
-
-
?
beta-L-arabinofuranosyl-(1->2)-beta-L-arabinofuranose + H2O
2 beta-L-arabinofuranose
Xanthomonas euvesicatoria UPB139
-
-
-
?
beta-L-arabinofuranosyl-L-hydroxyproline + H2O
beta-L-arabinofuranose + L-hydroxyproline
-
-
-
?
beta-L-arabinofuranosyl-L-hydroxyproline + H2O
beta-L-arabinofuranose + L-hydroxyproline
-
-
-
?
beta-L-arabinofuranosyl-L-hydroxyproline + H2O
beta-L-arabinofuranose + L-hydroxyproline
-
-
-
?
beta-L-arabinofuranosyl-L-hydroxyproline + H2O
beta-L-arabinofuranose + L-hydroxyproline
Xanthomonas euvesicatoria UPB139
-
-
-
?
additional information
?
-
in addition, enzyme transglycosylates 1-alkanols with retention of the anomeric configuration
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-
?
additional information
?
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-
in addition, enzyme transglycosylates 1-alkanols with retention of the anomeric configuration
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-
?
additional information
?
-
no substrates: 4-nitrophenyl-alpha-L-arabinopyranoside, 4-nitrophenyl-alpha-L-arabinofuranoside, 4-nitrophenyl-beta-L-arabinopyranoside, or (beta-L-arabinofuranosyl)4-L-hydroxyproline
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-
?
additional information
?
-
-
no substrates: 4-nitrophenyl-alpha-L-arabinopyranoside, 4-nitrophenyl-alpha-L-arabinofuranoside, 4-nitrophenyl-beta-L-arabinopyranoside, or (beta-L-arabinofuranosyl)4-L-hydroxyproline
-
-
?
additional information
?
-
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
-
-
?
additional information
?
-
-
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
-
-
?
additional information
?
-
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
-
-
?
additional information
?
-
Xanthomonas euvesicatoria UPB139
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
-
-
?
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NATURAL SUBSTRATE
NATURAL PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate)
(Substrate)
LITERATURE
(Substrate)
(Substrate)
COMMENTARY
(Product)
(Product)
LITERATURE
(Product)
(Product)
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
beta-L-arabinofuranosyl-(1->2)-beta-L-arabinofuranose + H2O
2 beta-L-arabinofuranose
-
-
-
?
beta-L-arabinofuranosyl-(1->2)-beta-L-arabinofuranose + H2O
2 beta-L-arabinofuranose
-
-
-
?
beta-L-arabinofuranosyl-(1->2)-beta-L-arabinofuranose + H2O
2 beta-L-arabinofuranose
Xanthomonas euvesicatoria UPB139
-
-
-
?
beta-L-arabinofuranosyl-L-hydroxyproline + H2O
beta-L-arabinofuranose + L-hydroxyproline
-
-
-
?
beta-L-arabinofuranosyl-L-hydroxyproline + H2O
beta-L-arabinofuranose + L-hydroxyproline
-
-
-
?
beta-L-arabinofuranosyl-L-hydroxyproline + H2O
beta-L-arabinofuranose + L-hydroxyproline
Xanthomonas euvesicatoria UPB139
-
-
-
?
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KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
0.85
beta-L-arabinofuranosyl-(1->2)-beta-L-arabinofuranose
wild-type, pH 4.5, 37°C
0.31
beta-L-arabinofuranosyl-(1->2)-beta-L-arabinofuranosyl-L-hydroxyproline
wild-type, pH 4.5, 37°C
0.43
beta-L-arabinofuranosyl-L-hydroxyproline
wild-type, pH 4.5, 37°C
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TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
2
beta-L-arabinofuranosyl-(1->2)-beta-L-arabinofuranose
wild-type, pH 4.5, 37°C
6.3
beta-L-arabinofuranosyl-(1->2)-beta-L-arabinofuranosyl-L-hydroxyproline
wild-type, pH 4.5, 37°C
0.013
beta-L-arabinofuranosyl-L-hydroxyproline
wild-type, pH 4.5, 37°C
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kcat/KM VALUE [1/mMs-1]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
2.3
beta-L-arabinofuranosyl-(1->2)-beta-L-arabinofuranose
wild-type, pH 4.5, 37°C
20
beta-L-arabinofuranosyl-(1->2)-beta-L-arabinofuranosyl-L-hydroxyproline
wild-type, pH 4.5, 37°C
0.03
beta-L-arabinofuranosyl-L-hydroxyproline
wild-type, pH 4.5, 37°C
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SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
4.5
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TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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ORGANISM
COMMENTARY
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
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LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY
GeneOntology No.
LITERATURE
SOURCE
additional information
additional information
the enzyme contains a 43 amino-acid signal peptide
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brenda
additional information
-
the enzyme contains a 43 amino-acid signal peptide
-
brenda
additional information
-
the enzyme contains a 43 amino-acid signal peptide
-
-
brenda
additional information
Xanthomonas euvesicatoria UPB139
-
the enzyme contains a 43 amino-acid signal peptide
-
-
brenda
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GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
evolution
malfunction
physiological function
evolution
the enzyme belongs to the glycosyl hydrolase family 127, GH127
evolution
-
the enzyme belongs to the glycosyl hydrolase family 127, GH127
-
evolution
Xanthomonas euvesicatoria UPB139
-
the enzyme belongs to the glycosyl hydrolase family 127, GH127
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malfunction
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
malfunction
-
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
-
malfunction
Xanthomonas euvesicatoria UPB139
-
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
-
physiological function
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
physiological function
-
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
-
physiological function
Xanthomonas euvesicatoria UPB139
-
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
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Show AA Sequence and Transmembrane Helices (416 entries)
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PDB
SCOP
CATH
UNIPROT
ORGANISM
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MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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SUBUNIT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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PROTEIN VARIANTS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
additional information
additional information
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
additional information
-
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
additional information
-
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
-
additional information
Xanthomonas euvesicatoria UPB139
-
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
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EXPRESSION
ORGANISM
UNIPROT
LITERATURE
the operon is upregulated by transcription factor HrpX
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REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Fujita, K.; Takashi, Y.; Obuchi, E.; Kitahara, K.; Suganuma, T.
Characterization of a novel ?-L-Arabinofuranosidase in Bifidobacterium longum: functional elucidation of A DUF1680 family member
J. Biol. Chem.
286
38079-38085
2011
Bifidobacterium longum (E8MGH8), Bifidobacterium longum
brenda
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
PLoS ONE
13
e0201982
2018
Xanthomonas euvesicatoria (Q3BS08), Xanthomonas euvesicatoria, Xanthomonas euvesicatoria 85-10 (Q3BS08), Xanthomonas euvesicatoria UPB139 (Q3BS08)
brenda
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Release 2023.1 (January 2023)
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