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Literature summary extracted from

  • Valenzuela, S.V.; Lopez, S.; Biely, P.; Sanz-Aparicio, J.; Pastor, F.I.
    The glycoside hydrolase family 8 reducing-end xylose-releasing exo-oligoxylanase Rex8A from Paenibacillus barcinonensis BP-23 is active on branched xylooligosaccharides (2016), Appl. Environ. Microbiol., 82, 5116-5124 .
    View publication on PubMedView publication on EuropePMC

Cloned(Commentary)

EC Number Cloned (Comment) Organism
3.2.1.156 gene rex8A, DNA and amino acid sequence determination and analysis, sequence comparisons, recombinant expression of N-terminally His6-tagged wild-type and mutant enzymes in Escherichia coli strain BL21 Star (DE3) Paenibacillus barcinonensis

Protein Variants

EC Number Protein Variants Comment Organism
3.2.1.156 E70A site-directed mutagenesis Paenibacillus barcinonensis

KM Value [mM]

EC Number KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
3.2.1.156 1.64
-
xylotriose pH 7.0, 40°C, recombinant wild-type enzyme Paenibacillus barcinonensis

Localization

EC Number Localization Comment Organism GeneOntology No. Textmining
3.2.1.156 additional information the enzyme contains no signal peptide Paenibacillus barcinonensis
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-

Organism

EC Number Organism UniProt Comment Textmining
3.2.1.156 Paenibacillus barcinonensis A0A0S2UQQ5
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-
3.2.1.156 Paenibacillus barcinonensis BP-23 A0A0S2UQQ5
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-
3.2.1.156 Paenibacillus barcinonensis CECT 7022 A0A0S2UQQ5
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-
3.2.1.156 Paenibacillus barcinonensis DSM 15478 A0A0S2UQQ5
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-

Purification (Commentary)

EC Number Purification (Comment) Organism
3.2.1.156 recombinant His6-tagged wild-type and mutant enzymes from Escherichia coli strain BL21 Star (DE3) by nickel affinity chromatography to homogeneity Paenibacillus barcinonensis

Reaction

EC Number Reaction Comment Organism Reaction ID
3.2.1.156 beta-D-xylopyranosyl-(1-4)-beta-D-xylopyranosyl-(1-4)-beta-D-xylopyranosyl-(1-4)-beta-D-xylopyranose + H2O = 2 beta-D-xylopyranosyl-(1-4)-alpha-D-xylopyranose processivemodeof hydrolysis, overview. The xylooligosaccharides are progressively degraded from Xn to Xn-1 and then subsequently degraded in the same way to xylose and xylobiose Paenibacillus barcinonensis

Substrates and Products (Substrate)

EC Number Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
3.2.1.156 4-nitrophenyl-beta-D-xylopyranoside + H2O
-
Paenibacillus barcinonensis 4-nitrophenol + D-xylopyranose
-
?
3.2.1.156 4-nitrophenyl-beta-D-xylopyranoside + H2O
-
Paenibacillus barcinonensis CECT 7022 4-nitrophenol + D-xylopyranose
-
?
3.2.1.156 4-nitrophenyl-beta-D-xylopyranoside + H2O
-
Paenibacillus barcinonensis BP-23 4-nitrophenol + D-xylopyranose
-
?
3.2.1.156 4-nitrophenyl-beta-D-xylopyranoside + H2O
-
Paenibacillus barcinonensis DSM 15478 4-nitrophenol + D-xylopyranose
-
?
3.2.1.156 4-O-methyl-beta-D-glucuronosyl-(1->2)-beta-D-xylopyranosyl-(1->4)-beta-D-xylopyranosyl-(1->4)-D-xylose + H2O docking analysis of Rex8A with methyl-glucuronic acid branched oligomers. Mixtures containing the aldouronic acids 4-O-methyl-beta-D-glucuronosyl-(1->2)-beta-D-xylopyranosyl-(1->4)-beta-D-xylopyranosyl-(1->4)-D-xylose (MeGlcA3Xyl3) (aldotetraouronic acid) and beta-D-xylopyranosyl-(1->4)-beta-D-xylopyranosyl-(1->4)-[4-O-methyl-alpha-D-glucuronosyl-(1->2)]-beta-D-xylopyranosyl-(1->4)-beta-D-xylopyranosyl-(1->4)-D-xylose (MeGlcA3Xyl5) (aldohexaouronic acid) are prepared from beechwood 4-O-methyl-D-glucuronoxylan by xylanase treatment. Aldotetraouronic acid MeGlcA3Xyl3 consists of a xylotriose with a methyl-glucuronic acid substituent in the third xylose from the reducing end. The cleavage of this substrate to xylose and to an aldouronic acid shortened by one residue indicates that Rex8A accommodates the methyl-glucuronic acid-substituted xylopyranosyl residue in the -2 subsite of the catalytic cleft of the enzyme. Ligand accommodation in the catalytic site, a xylotriose decorated with a 4-O-MeGlcA moiety at O2 of the third xylose from the reducing end (MeGlcA3Xyl3) is modeled into the active-site channel Paenibacillus barcinonensis ?
-
?
3.2.1.156 4-O-methyl-beta-D-glucuronosyl-(1->2)-beta-D-xylopyranosyl-(1->4)-beta-D-xylopyranosyl-(1->4)-D-xylose + H2O docking analysis of Rex8A with methyl-glucuronic acid branched oligomers. Mixtures containing the aldouronic acids 4-O-methyl-beta-D-glucuronosyl-(1->2)-beta-D-xylopyranosyl-(1->4)-beta-D-xylopyranosyl-(1->4)-D-xylose (MeGlcA3Xyl3) (aldotetraouronic acid) and beta-D-xylopyranosyl-(1->4)-beta-D-xylopyranosyl-(1->4)-[4-O-methyl-alpha-D-glucuronosyl-(1->2)]-beta-D-xylopyranosyl-(1->4)-beta-D-xylopyranosyl-(1->4)-D-xylose (MeGlcA3Xyl5) (aldohexaouronic acid) are prepared from beechwood 4-O-methyl-D-glucuronoxylan by xylanase treatment. Aldotetraouronic acid MeGlcA3Xyl3 consists of a xylotriose with a methyl-glucuronic acid substituent in the third xylose from the reducing end. The cleavage of this substrate to xylose and to an aldouronic acid shortened by one residue indicates that Rex8A accommodates the methyl-glucuronic acid-substituted xylopyranosyl residue in the -2 subsite of the catalytic cleft of the enzyme. Ligand accommodation in the catalytic site, a xylotriose decorated with a 4-O-MeGlcA moiety at O2 of the third xylose from the reducing end (MeGlcA3Xyl3) is modeled into the active-site channel Paenibacillus barcinonensis CECT 7022 ?
-
?
3.2.1.156 4-O-methyl-beta-D-glucuronosyl-(1->2)-beta-D-xylopyranosyl-(1->4)-beta-D-xylopyranosyl-(1->4)-D-xylose + H2O docking analysis of Rex8A with methyl-glucuronic acid branched oligomers. Mixtures containing the aldouronic acids 4-O-methyl-beta-D-glucuronosyl-(1->2)-beta-D-xylopyranosyl-(1->4)-beta-D-xylopyranosyl-(1->4)-D-xylose (MeGlcA3Xyl3) (aldotetraouronic acid) and beta-D-xylopyranosyl-(1->4)-beta-D-xylopyranosyl-(1->4)-[4-O-methyl-alpha-D-glucuronosyl-(1->2)]-beta-D-xylopyranosyl-(1->4)-beta-D-xylopyranosyl-(1->4)-D-xylose (MeGlcA3Xyl5) (aldohexaouronic acid) are prepared from beechwood 4-O-methyl-D-glucuronoxylan by xylanase treatment. Aldotetraouronic acid MeGlcA3Xyl3 consists of a xylotriose with a methyl-glucuronic acid substituent in the third xylose from the reducing end. The cleavage of this substrate to xylose and to an aldouronic acid shortened by one residue indicates that Rex8A accommodates the methyl-glucuronic acid-substituted xylopyranosyl residue in the -2 subsite of the catalytic cleft of the enzyme. Ligand accommodation in the catalytic site, a xylotriose decorated with a 4-O-MeGlcA moiety at O2 of the third xylose from the reducing end (MeGlcA3Xyl3) is modeled into the active-site channel Paenibacillus barcinonensis BP-23 ?
-
?
3.2.1.156 4-O-methyl-beta-D-glucuronosyl-(1->2)-beta-D-xylopyranosyl-(1->4)-beta-D-xylopyranosyl-(1->4)-D-xylose + H2O docking analysis of Rex8A with methyl-glucuronic acid branched oligomers. Mixtures containing the aldouronic acids 4-O-methyl-beta-D-glucuronosyl-(1->2)-beta-D-xylopyranosyl-(1->4)-beta-D-xylopyranosyl-(1->4)-D-xylose (MeGlcA3Xyl3) (aldotetraouronic acid) and beta-D-xylopyranosyl-(1->4)-beta-D-xylopyranosyl-(1->4)-[4-O-methyl-alpha-D-glucuronosyl-(1->2)]-beta-D-xylopyranosyl-(1->4)-beta-D-xylopyranosyl-(1->4)-D-xylose (MeGlcA3Xyl5) (aldohexaouronic acid) are prepared from beechwood 4-O-methyl-D-glucuronoxylan by xylanase treatment. Aldotetraouronic acid MeGlcA3Xyl3 consists of a xylotriose with a methyl-glucuronic acid substituent in the third xylose from the reducing end. The cleavage of this substrate to xylose and to an aldouronic acid shortened by one residue indicates that Rex8A accommodates the methyl-glucuronic acid-substituted xylopyranosyl residue in the -2 subsite of the catalytic cleft of the enzyme. Ligand accommodation in the catalytic site, a xylotriose decorated with a 4-O-MeGlcA moiety at O2 of the third xylose from the reducing end (MeGlcA3Xyl3) is modeled into the active-site channel Paenibacillus barcinonensis DSM 15478 ?
-
?
3.2.1.156 additional information the enzyme efficiently hydrolyzes xylooligosaccharides and shows minor activity on polymeric xylan. The enzyme shows also catalytic activity on branched xylooligosaccharides, i.e. the release of xylose from the reducing end. Hydrolysis products from oligosaccharides and xylan are analyzed by thin-layer chromatography (TLC) and MALDI TOF/TOF mass spectrometry. No activity with xylobiose, low activity with xylan Paenibacillus barcinonensis ?
-
?
3.2.1.156 additional information the enzyme efficiently hydrolyzes xylooligosaccharides and shows minor activity on polymeric xylan. The enzyme shows also catalytic activity on branched xylooligosaccharides, i.e. the release of xylose from the reducing end. Hydrolysis products from oligosaccharides and xylan are analyzed by thin-layer chromatography (TLC) and MALDI TOF/TOF mass spectrometry. No activity with xylobiose, low activity with xylan Paenibacillus barcinonensis CECT 7022 ?
-
?
3.2.1.156 additional information the enzyme efficiently hydrolyzes xylooligosaccharides and shows minor activity on polymeric xylan. The enzyme shows also catalytic activity on branched xylooligosaccharides, i.e. the release of xylose from the reducing end. Hydrolysis products from oligosaccharides and xylan are analyzed by thin-layer chromatography (TLC) and MALDI TOF/TOF mass spectrometry. No activity with xylobiose, low activity with xylan Paenibacillus barcinonensis BP-23 ?
-
?
3.2.1.156 additional information the enzyme efficiently hydrolyzes xylooligosaccharides and shows minor activity on polymeric xylan. The enzyme shows also catalytic activity on branched xylooligosaccharides, i.e. the release of xylose from the reducing end. Hydrolysis products from oligosaccharides and xylan are analyzed by thin-layer chromatography (TLC) and MALDI TOF/TOF mass spectrometry. No activity with xylobiose, low activity with xylan Paenibacillus barcinonensis DSM 15478 ?
-
?
3.2.1.156 xylan + H2O very low activity, beechwood xylan, oat spelt xylan, or birchwood xylan Paenibacillus barcinonensis ?
-
?
3.2.1.156 xylan + H2O very low activity, beechwood xylan, oat spelt xylan, or birchwood xylan Paenibacillus barcinonensis CECT 7022 ?
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?
3.2.1.156 xylan + H2O very low activity, beechwood xylan, oat spelt xylan, or birchwood xylan Paenibacillus barcinonensis BP-23 ?
-
?
3.2.1.156 xylan + H2O very low activity, beechwood xylan, oat spelt xylan, or birchwood xylan Paenibacillus barcinonensis DSM 15478 ?
-
?
3.2.1.156 xylohexaose + H2O
-
Paenibacillus barcinonensis 4 D-xylose + xylobiose
-
?
3.2.1.156 xylopentaose + H2O
-
Paenibacillus barcinonensis 3 D-xylose + xylobiose
-
?
3.2.1.156 xylotetraose + H2O
-
Paenibacillus barcinonensis 2 D-xylose + xylobiose
-
?
3.2.1.156 xylotriose + H2O preferred substrate Paenibacillus barcinonensis D-xylose + xylobiose
-
?
3.2.1.156 xylotriose + H2O preferred substrate Paenibacillus barcinonensis CECT 7022 D-xylose + xylobiose
-
?
3.2.1.156 xylotriose + H2O preferred substrate Paenibacillus barcinonensis BP-23 D-xylose + xylobiose
-
?
3.2.1.156 xylotriose + H2O preferred substrate Paenibacillus barcinonensis DSM 15478 D-xylose + xylobiose
-
?

Subunits

EC Number Subunits Comment Organism
3.2.1.156 ? x * 44217, sequence calculation Paenibacillus barcinonensis

Synonyms

EC Number Synonyms Comment Organism
3.2.1.156 DFQ00_11062
-
Paenibacillus barcinonensis
3.2.1.156 reducing-end xylose-releasing exo-oligoxylanase
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Paenibacillus barcinonensis
3.2.1.156 Rex8A
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Paenibacillus barcinonensis

Temperature Optimum [°C]

EC Number Temperature Optimum [°C] Temperature Optimum Maximum [°C] Comment Organism
3.2.1.156 40
-
recombinant enzyme Paenibacillus barcinonensis

Turnover Number [1/s]

EC Number Turnover Number Minimum [1/s] Turnover Number Maximum [1/s] Substrate Comment Organism Structure
3.2.1.156 118.8
-
xylotriose pH 7.0, 40°C, recombinant wild-type enzyme Paenibacillus barcinonensis

pH Optimum

EC Number pH Optimum Minimum pH Optimum Maximum Comment Organism
3.2.1.156 7
-
recombinant enzyme Paenibacillus barcinonensis

pH Range

EC Number pH Minimum pH Maximum Comment Organism
3.2.1.156 4 10 activity range, profile overview Paenibacillus barcinonensis

pI Value

EC Number Organism Comment pI Value Maximum pI Value
3.2.1.156 Paenibacillus barcinonensis sequence calculation
-
5.25

General Information

EC Number General Information Comment Organism
3.2.1.156 evolution the enzyme belongs to the glycoside hydrolase family 8, GH8 Paenibacillus barcinonensis
3.2.1.156 additional information modeling of the three-dimensional structure of Rex8A shows an (alpha/alpha)6 barrel fold where the loops connecting the alpha-helices contour the active site. These loops, which show high sequence diversity among GH8 enzymes, shape a catalytic cleft with a -2 subsite that can accommodate methyl-glucuronic acid decorations. Putative proton donor is Glu70 and catalytic base is Asp265. Residues Leu320, His321, and Pro322 form the loop structure. Structural molecular modeling of Rex8A Paenibacillus barcinonensis
3.2.1.156 physiological function the enzyme is involved in depolymerization of glucuronoxylan, a major component of the lignocellulosic substrates. Rex8A is a reducing-end xylose-releasing exo-oligoxylanase that efficiently hydrolyzes xylose from neutral and acidic xylooligosaccharides generated by the action of other xylanases also secreted by the strain. The hydrolytic ability of Rex8A on branched oligomers can be crucial for the complete depolymerization of highly substituted xylans, which is indispensable to accomplish biomass deconstruction and to generate efficient catalysts Paenibacillus barcinonensis