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Information on EC 3.2.1.156 - oligosaccharide reducing-end xylanase
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3.2.1.156 oligosaccharide reducing-end xylanaseIUBMB Comments
The enzyme, originally isolated from the bacterium Bacillus halodurans C-125, releases the xylose unit at the reducing end of oligosaccharides ending with the structure beta-D-xylopyranosyl-(1->4)-beta-D-xylopyranosyl-(1->4)-beta-D-xylopyranose, leaving the new reducing end in the alpha configuration. It is specific for the beta anomers of xylooligosaccharides whose degree of polymerization is equal to or greater than 3.
The penultimate residue must be beta-D-xylopyranose, but replacing either of the flanking residues with glucose merely slows the rate greatly.
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Word Map
- 3.2.1.156
- glycoside
- xylooligosaccharides
- xylanases
- halodurans
-
subsite
- adolescentis
- xylotriose
-
bifidobacterium
-
pseudoalteromonas
-
glycosynthase
- haloplanktis
- glucuronoxylan
-
prebiotic
- endo-xylanase
- xylopentaose
- hemicelluloses
- xylohexaose
- xylosidase
- arabinoxylan
-
deconstruction
-
beechwood
- xylotetraose
-
heteroxylans
-
paenibacillus
- biotechnology
The enzyme appears in viruses and cellular organisms
Reaction Schemes
Synonyms
rex8a, reducing-end xylose-releasing exo-oligoxylanase, rxyn8, reducing end xylose-releasing exo-oligoxylanase, phxyl, oligosaccharide reducing-end xylanase, gh8 xylanase, 
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SYNONYM 
ORGANISM
UNIPROT
COMMENTARY 
LITERATURE
BaRex8A
BhRex8A
DFQ00_11062
GH8 xylanase
oligosaccharide reducing-end xylanase
reducing end xylose-releasing exo-oligoxylanase
reducing-end xylose-releasing exo-oligoxylanase
reducing-end xylose-releasing exooligoxylanase
Rex
Rex8A
RexA
XYLA
additional information
Halalkalibacterium halodurans
-
Rex is an inverting xylanolytic enzyme belonging to the glycohydrolase family 8, GH8
reducing end xylose-releasing exo-oligoxylanase
Halalkalibacterium halodurans C-125
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-
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reducing-end xylose-releasing exo-oligoxylanase
Halalkalibacterium halodurans C-125
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-
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reducing-end xylose-releasing exo-oligoxylanase
-
-
reducing-end xylose-releasing exo-oligoxylanase
-
-
Rex
Halalkalibacterium halodurans C-125
-
-
-
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REACTION
REACTION DIAGRAM
COMMENTARY
ORGANISM
UNIPROT
LITERATURE
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
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
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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
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
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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
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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
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REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
hydrolysis of O-glycosyl bond
hydrolysis of O-glycosyl bond
Halalkalibacterium halodurans C-125
-
-
-
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SYSTEMATIC NAME
IUBMB Comments
beta-D-xylopyranosyl-(1->4)-beta-D-xylopyranose reducing-end xylanase
The enzyme, originally isolated from the bacterium Bacillus halodurans C-125, releases the xylose unit at the reducing end of oligosaccharides ending with the structure beta-D-xylopyranosyl-(1->4)-beta-D-xylopyranosyl-(1->4)-beta-D-xylopyranose, leaving the new reducing end in the alpha configuration. It is specific for the beta anomers of xylooligosaccharides whose degree of polymerization is equal to or greater than 3.
The penultimate residue must be beta-D-xylopyranose, but replacing either of the flanking residues with glucose merely slows the rate greatly.
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CAS REGISTRY NUMBER
COMMENTARY
55126-95-9
-
879497-03-7
-
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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
1-O-fluoro-4-O-alpha-D-xylopyranosyl-beta-D-xylopyranose + H2O
alpha-D-xylopyranose + 1-O-fluoro-beta-D-xylopyranose
2-nitrohenyl Xylbeta(1-4)Xylbeta(1-4)Xylbeta(1-4)Xyl + H2O
2-nitrophenol + Xylbeta(1-4)Xylbeta(1-4)Xylbeta(1-4)Xyl
-
-
-
?
2-nitrophenyl Xylbeta(1-4)Xylbeta(1-4)Xylbeta(1-4)Xylbeta + H2O
2-nitrophenyl beta-D-xylopyranose + Xylbeta(1-4)Xylbeta(1-4)Xylbeta
2-nitrophenyl Xylbeta(1-4)Xylbeta(1-4)Xylbeta(1-4)Xylbeta(1-4)Xylbeta + H2O
2-nitrophenyl Xylbeta(1-4)Xylbeta + Xylbeta(1-4)Xylbeta(1-4)Xyl
2-nitrophenyl Xylbeta(1-4)Xylbeta(1-4)Xylbeta(1-4)Xylbeta(1-4)Xylbeta(1-4)Xylbeta + H2O
2-nitrophenyl Xylbeta(1-4)Xylbeta(1-4)Xylbeta + Xylbeta(1-4)Xylbeta(1-4)Xyl
-
the enzyme cleaves the substrate exclusively at the third xylosidic bond from the reducing end
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-
?
4-O-methyl-beta-D-glucuronosyl-(1->2)-beta-D-xylopyranosyl-(1->4)-beta-D-xylopyranosyl-(1->4)-D-xylose + H2O
?
alpha-xylobiosyl fluoride + D-xylose
alpha-xylobiose + HF + D-xylose
Halalkalibacterium halodurans
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-
-
-
?
alpha-xylobiosylfluoride + H2O + xylose
alpha-xylobiose + HF + xylose
Halalkalibacterium halodurans
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presence of xylose is required, some mutants in D263 also produce xylotriose
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?
beta-D-xylopyranosyl-(1-4)-beta-D-xylopyranosyl-(1-4)-beta-D-xylopyranose + H2O
beta-D-xylopyranosyl-(1-4)-alpha-D-xylopyranose
beta-D-xylopyranosyl-(1-4)-beta-D-xylopyranosyl-(1-4)-beta-D-xylopyranosyl-(1-4)-beta-D-xylopyranose + H2O
?
Halalkalibacterium halodurans
-
-
-
-
?
beta-D-xylopyranosyl-(1-4)-beta-D-xylopyranosyl-(1-4)-beta-D-xylopyranosyl-(1-4)-beta-D-xylopyranosyl-(1-4)-beta-D-xylopyranose + H2O
?
Halalkalibacterium halodurans
-
-
-
-
?
beta-D-xylopyranosyl-(1-4)-beta-D-xylopyranosyl-(1-4)-beta-D-xylopyranosyl-(1-4)-beta-D-xylopyranosyl-(1-4)-beta-D-xylopyranosyl-(1-4)-beta-D-xylopyranose + H2O
?
Halalkalibacterium halodurans
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-
-
-
?
xylooligosaccharides + H2O
D-xylose + Xylbeta(1-4)Xyl
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-
?
xylopentaose + H2O
xylotetraose + xylobiose
the recombinant enzyme constitutively hydrolyzes a xylose residue from Xn when n is above 2, until the final products are (n-2)X1 and X2
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?
1-O-fluoro-4-O-alpha-D-xylopyranosyl-beta-D-xylopyranose + H2O
alpha-D-xylopyranose + 1-O-fluoro-beta-D-xylopyranose
Halalkalibacterium halodurans
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-
-
-
?
1-O-fluoro-4-O-alpha-D-xylopyranosyl-beta-D-xylopyranose + H2O
alpha-D-xylopyranose + 1-O-fluoro-beta-D-xylopyranose
Halalkalibacterium halodurans
-
Rex is an inverting glycohydrolase, that shows the Hehre resynthesis-hydrolysis mechanism, overview. Residue Y198 forms a hydrogen bond with nucleophilic water
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?
2-nitrophenyl Xylbeta(1-4)Xylbeta(1-4)Xylbeta(1-4)Xylbeta + H2O
2-nitrophenyl beta-D-xylopyranose + Xylbeta(1-4)Xylbeta(1-4)Xylbeta
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?
2-nitrophenyl Xylbeta(1-4)Xylbeta(1-4)Xylbeta(1-4)Xylbeta + H2O
2-nitrophenyl beta-D-xylopyranose + Xylbeta(1-4)Xylbeta(1-4)Xylbeta
Halalkalibacterium halodurans
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?
2-nitrophenyl Xylbeta(1-4)Xylbeta(1-4)Xylbeta(1-4)Xylbeta + H2O
2-nitrophenyl beta-D-xylopyranose + Xylbeta(1-4)Xylbeta(1-4)Xylbeta
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?
2-nitrophenyl Xylbeta(1-4)Xylbeta(1-4)Xylbeta(1-4)Xylbeta + H2O
2-nitrophenyl beta-D-xylopyranose + Xylbeta(1-4)Xylbeta(1-4)Xylbeta
-
the enzyme has a strong preference for hydrolysis of the third xylosidic bond from the non-reducing end of the substrate
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?
2-nitrophenyl Xylbeta(1-4)Xylbeta(1-4)Xylbeta(1-4)Xylbeta(1-4)Xylbeta + H2O
2-nitrophenyl Xylbeta(1-4)Xylbeta + Xylbeta(1-4)Xylbeta(1-4)Xyl
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-
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?
2-nitrophenyl Xylbeta(1-4)Xylbeta(1-4)Xylbeta(1-4)Xylbeta(1-4)Xylbeta + H2O
2-nitrophenyl Xylbeta(1-4)Xylbeta + Xylbeta(1-4)Xylbeta(1-4)Xyl
Halalkalibacterium halodurans
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-
-
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?
2-nitrophenyl Xylbeta(1-4)Xylbeta(1-4)Xylbeta(1-4)Xylbeta(1-4)Xylbeta + H2O
2-nitrophenyl Xylbeta(1-4)Xylbeta + Xylbeta(1-4)Xylbeta(1-4)Xyl
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?
2-nitrophenyl Xylbeta(1-4)Xylbeta(1-4)Xylbeta(1-4)Xylbeta(1-4)Xylbeta + H2O
2-nitrophenyl Xylbeta(1-4)Xylbeta + Xylbeta(1-4)Xylbeta(1-4)Xyl
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?
2-nitrophenyl xylohexaose + H2O
?
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the enzyme hydrolyzes 2-nitrophenyl xylohexaose mainly at the second and third xylosidic bonds from the reducing end of the substrate
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?
4-nitrophenyl-beta-D-xylopyranoside + H2O
4-nitrophenol + D-xylopyranose
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?
4-nitrophenyl-beta-D-xylopyranoside + H2O
4-nitrophenol + D-xylopyranose
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?
4-nitrophenyl-beta-D-xylopyranoside + H2O
4-nitrophenol + D-xylopyranose
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?
4-nitrophenyl-beta-D-xylopyranoside + H2O
4-nitrophenol + D-xylopyranose
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?
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
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?
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
-
-
?
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
-
-
?
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
-
-
?
arabinofuranosyl-xylotriose + H2O
D-xylose + xylobiose + ?
good substrate
-
-
?
arabinofuranosyl-xylotriose + H2O
D-xylose + xylobiose + ?
good substrate
-
-
?
arabinofuranosyl-xylotriose + H2O
D-xylose + xylobiose + ?
good substrate
-
-
?
arabinofuranosyl-xylotriose + H2O
D-xylose + xylobiose + ?
good substrate
-
-
?
arabinofuranosyl-xylotriose + H2O
D-xylose + xylobiose + ?
good substrate
-
-
?
arabinofuranosyl-xylotriose + H2O
D-xylose + xylobiose + ?
Halalkalibacterium halodurans
good substrate
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-
?
arabinofuranosyl-xylotriose + H2O
D-xylose + xylobiose + ?
Halalkalibacterium halodurans DSM 181973
good substrate
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-
?
beta-D-glucopyranosyl-(1-4)-beta-D-xylopyranosyl-(1-4)-beta-D-xylopyranose + H2O
?
Halalkalibacterium halodurans
-
1.1% of the activity with beta-D-xylopyranosyl-(1-4)-beta-D-xylopyranosyl-(1-4)-beta-D-xylopyranose
-
-
?
beta-D-glucopyranosyl-(1-4)-beta-D-xylopyranosyl-(1-4)-beta-D-xylopyranose + H2O
?
Halalkalibacterium halodurans C-125
-
1.1% of the activity with beta-D-xylopyranosyl-(1-4)-beta-D-xylopyranosyl-(1-4)-beta-D-xylopyranose
-
-
?
beta-D-xylopyranosyl-(1-4)-beta-D-xylopyranosyl-(1-4)-beta-D-deoxyxylopyranose + H2O
?
Halalkalibacterium halodurans
-
3.2% of the activity with beta-D-xylopyranosyl-(1-4)-beta-D-xylopyranosyl-(1-4)-beta-D-xylopyranose
-
-
?
beta-D-xylopyranosyl-(1-4)-beta-D-xylopyranosyl-(1-4)-beta-D-deoxyxylopyranose + H2O
?
Halalkalibacterium halodurans C-125
-
3.2% of the activity with beta-D-xylopyranosyl-(1-4)-beta-D-xylopyranosyl-(1-4)-beta-D-xylopyranose
-
-
?
beta-D-xylopyranosyl-(1-4)-beta-D-xylopyranosyl-(1-4)-beta-D-glucopyranose + H2O
?
Halalkalibacterium halodurans
-
0.5% of the activity with beta-D-xylopyranosyl-(1-4)-beta-D-xylopyranosyl-(1-4)-beta-D-xylopyranose
-
-
?
beta-D-xylopyranosyl-(1-4)-beta-D-xylopyranosyl-(1-4)-beta-D-glucopyranose + H2O
?
Halalkalibacterium halodurans C-125
-
0.5% of the activity with beta-D-xylopyranosyl-(1-4)-beta-D-xylopyranosyl-(1-4)-beta-D-xylopyranose
-
-
?
beta-D-xylopyranosyl-(1-4)-beta-D-xylopyranosyl-(1-4)-beta-D-xylopyranose + ?
?
Halalkalibacterium halodurans
-
-
-
-
?
beta-D-xylopyranosyl-(1-4)-beta-D-xylopyranosyl-(1-4)-beta-D-xylopyranose + ?
?
Halalkalibacterium halodurans C-125
-
-
-
-
?
beta-D-xylopyranosyl-(1-4)-beta-D-xylopyranosyl-(1-4)-beta-D-xylopyranose + H2O
beta-D-xylopyranosyl-(1-4)-alpha-D-xylopyranose
Halalkalibacterium halodurans
-
the enzyme acts rapidly on the beta-anomer of beta-D-xylopyranosyl-(1-4)-beta-D-xylopyranosyl-(1-4)-beta-D-xylopyranose, leaving the new reducing end in the alpha configuration. It also acts on longer oligosaccharides that have this structure at their reducing ends. The penulimate residue must be xylose, but replacing either of the other two residues with glucose merely slows the rate greatly
-
-
?
beta-D-xylopyranosyl-(1-4)-beta-D-xylopyranosyl-(1-4)-beta-D-xylopyranose + H2O
beta-D-xylopyranosyl-(1-4)-alpha-D-xylopyranose
Halalkalibacterium halodurans C-125
-
the enzyme acts rapidly on the beta-anomer of beta-D-xylopyranosyl-(1-4)-beta-D-xylopyranosyl-(1-4)-beta-D-xylopyranose, leaving the new reducing end in the alpha configuration. It also acts on longer oligosaccharides that have this structure at their reducing ends. The penulimate residue must be xylose, but replacing either of the other two residues with glucose merely slows the rate greatly
-
-
?
xylan + H2O
?
beechwood xylan or wheat flour arabinoxylan, low activity
-
-
?
xylan + H2O
?
beechwood xylan or wheat flour arabinoxylan, low activity
-
-
?
xylan + H2O
?
beechwood xylan or wheat flour arabinoxylan, low activity
-
-
?
xylan + H2O
?
beechwood xylan or wheat flour arabinoxylan, low activity
-
-
?
xylan + H2O
?
beechwood xylan or wheat flour arabinoxylan, low activity
-
-
?
xylan + H2O
?
Halalkalibacterium halodurans
beechwood xylan or wheat flour arabinoxylan, low to moderate activity
-
-
?
xylan + H2O
?
Halalkalibacterium halodurans DSM 181973
beechwood xylan or wheat flour arabinoxylan, low to moderate activity
-
-
?
xylan + H2O
?
very low activity, beechwood xylan, oat spelt xylan, or birchwood xylan
-
-
?
xylan + H2O
?
very low activity, beechwood xylan, oat spelt xylan, or birchwood xylan
-
-
?
xylan + H2O
?
very low activity, beechwood xylan, oat spelt xylan, or birchwood xylan
-
-
?
xylan + H2O
?
very low activity, beechwood xylan, oat spelt xylan, or birchwood xylan
-
-
?
xylotriose + H2O
D-xylose + xylobiose
preferred substrate
-
-
?
xylotriose + H2O
D-xylose + xylobiose
preferred substrate
-
-
?
xylotriose + H2O
D-xylose + xylobiose
preferred substrate
-
-
?
xylotriose + H2O
D-xylose + xylobiose
preferred substrate
-
-
?
xylotriose + H2O
D-xylose + xylobiose
preferred substrate
-
-
?
xylotriose + H2O
D-xylose + xylobiose
Halalkalibacterium halodurans
preferred substrate
-
-
?
xylotriose + H2O
D-xylose + xylobiose
Halalkalibacterium halodurans DSM 181973
preferred substrate
-
-
?
xylotriose + H2O
D-xylose + xylobiose
preferred substrate
-
-
?
xylotriose + H2O
D-xylose + xylobiose
preferred substrate
-
-
?
xylotriose + H2O
D-xylose + xylobiose
preferred substrate
-
-
?
xylotriose + H2O
D-xylose + xylobiose
preferred substrate
-
-
?
additional information
?
-
-
the enzyme hydrolyzes xylotriose through xylohexaose to a mixture of xylose and xylobiose, identification by thin layer chromatography
-
-
?
additional information
?
-
-
the enzyme hydrolyzes xylotriose through xylohexaose to a mixture of xylose and xylobiose, identification by thin layer chromatography
-
-
?
additional information
?
-
the enzyme does not hydrolyze xylobiose
-
-
?
additional information
?
-
-
the enzyme does not hydrolyze xylobiose
-
-
?
additional information
?
-
xylooligomers are the preferred substrates of the processive Rex8As. Rex8As hydrolyse xylooligomers to xylose and xylobiose
-
-
?
additional information
?
-
-
xylooligomers are the preferred substrates of the processive Rex8As. Rex8As hydrolyse xylooligomers to xylose and xylobiose
-
-
?
additional information
?
-
the enzyme acts synergistically in combination with GH10 or GH11 xylanase. Low activity with an aldouronic acids mixture. No activity with 4-nitrophenyl-beta-D-xylopyranoside and 4-nitrophenyl-alpha-D-arabinofuranoside
-
-
?
additional information
?
-
-
the enzyme acts synergistically in combination with GH10 or GH11 xylanase. Low activity with an aldouronic acids mixture. No activity with 4-nitrophenyl-beta-D-xylopyranoside and 4-nitrophenyl-alpha-D-arabinofuranoside
-
-
?
additional information
?
-
xylooligomers are the preferred substrates of the processive Rex8As. Rex8As hydrolyse xylooligomers to xylose and xylobiose
-
-
?
additional information
?
-
the enzyme acts synergistically in combination with GH10 or GH11 xylanase. Low activity with an aldouronic acids mixture. No activity with 4-nitrophenyl-beta-D-xylopyranoside and 4-nitrophenyl-alpha-D-arabinofuranoside
-
-
?
additional information
?
-
xylooligomers are the preferred substrates of the processive Rex8As. Rex8As hydrolyse xylooligomers to xylose and xylobiose
-
-
?
additional information
?
-
the enzyme acts synergistically in combination with GH10 or GH11 xylanase. Low activity with an aldouronic acids mixture. No activity with 4-nitrophenyl-beta-D-xylopyranoside and 4-nitrophenyl-alpha-D-arabinofuranoside
-
-
?
additional information
?
-
xylooligomers are the preferred substrates of the processive Rex8As. Rex8As hydrolyse xylooligomers to xylose and xylobiose
-
-
?
additional information
?
-
the enzyme acts synergistically in combination with GH10 or GH11 xylanase. Low activity with an aldouronic acids mixture. No activity with 4-nitrophenyl-beta-D-xylopyranoside and 4-nitrophenyl-alpha-D-arabinofuranoside
-
-
?
additional information
?
-
xylooligomers are the preferred substrates of the processive Rex8As. Rex8As hydrolyse xylooligomers to xylose and xylobiose
-
-
?
additional information
?
-
the enzyme acts synergistically in combination with GH10 or GH11 xylanase. Low activity with an aldouronic acids mixture. No activity with 4-nitrophenyl-beta-D-xylopyranoside and 4-nitrophenyl-alpha-D-arabinofuranoside
-
-
?
additional information
?
-
Halalkalibacterium halodurans
-
the enzyme may play a role as a key enzyme in intracellular xylan metabolism by cleaving xylooligosaccharides that are produced by the action of other intracellular enzymes from the arabino/glucurono-xylooligosaccharides
-
-
?
additional information
?
-
Halalkalibacterium halodurans
-
the enzyme hydrolyzes xylooligosaccharides whoses degree of polymerization is greater than or equal to 3, releasing the xylose unit at the reducing end
-
-
?
additional information
?
-
Halalkalibacterium halodurans
-
Rex is an inverting xylanolytic enzyme belonging to the glycohydrolase family 8, GH8, hydrolyzing xylooligosacchrides to release xylose from its reducing end
-
-
?
additional information
?
-
Halalkalibacterium halodurans
the reducing-end xylose-releasing exo-oligoxylanase is an inverting glycohydrolase, active site structure of wild-type enzyme and glycosynthase Rex mutant enzymes, overview
-
-
?
additional information
?
-
Halalkalibacterium halodurans
-
no activity towards xyloheptaose, xylooctaose, and xylononaose
-
-
?
additional information
?
-
Halalkalibacterium halodurans
xylooligomers are the preferred substrates of the processive Rex8As. Rex8As hydrolyse xylooligomers to xylose and xylobiose
-
-
?
additional information
?
-
Halalkalibacterium halodurans
the enzyme acts synergistically in combination with GH10 or GH11 xylanase. 4-Nitrophenyl-beta-D-xylopyranoside and 4-nitrophenyl-alpha-D-arabinofuranoside are a poor substrates. Low activity with an aldouronic acids mixture
-
-
?
additional information
?
-
Halalkalibacterium halodurans C-125
-
the enzyme may play a role as a key enzyme in intracellular xylan metabolism by cleaving xylooligosaccharides that are produced by the action of other intracellular enzymes from the arabino/glucurono-xylooligosaccharides
-
-
?
additional information
?
-
Halalkalibacterium halodurans C-125
-
the enzyme hydrolyzes xylooligosaccharides whoses degree of polymerization is greater than or equal to 3, releasing the xylose unit at the reducing end
-
-
?
additional information
?
-
Halalkalibacterium halodurans DSM 181973
xylooligomers are the preferred substrates of the processive Rex8As. Rex8As hydrolyse xylooligomers to xylose and xylobiose
-
-
?
additional information
?
-
Halalkalibacterium halodurans DSM 181973
the enzyme acts synergistically in combination with GH10 or GH11 xylanase. 4-Nitrophenyl-beta-D-xylopyranoside and 4-nitrophenyl-alpha-D-arabinofuranoside are a poor substrates. Low activity with an aldouronic acids mixture
-
-
?
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
-
-
?
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
-
-
?
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
-
-
?
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
-
-
?
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
-
-
?
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
-
-
?
additional information
?
-
-
no activity with xylotriose, xylotetraose, and xylopentaose
-
-
?
additional information
?
-
-
no activity towards xylotriose and xylotetraose
-
-
?
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NATURAL SUBSTRATE
NATURAL PRODUCT
REACTION DIAGRAM