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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
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
Halalkalibacterium halodurans
-
-
-
-
?
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
?
-
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
?
-
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
?
-
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
-
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
xylooligomers are the preferred substrates of the processive Rex8As. Rex8As hydrolyse xylooligomers to xylose and xylobiose
-
-
?
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
-
-
?
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KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
0.005
beta-D-xylopyranosyl-(1-4)-beta-D-xylopyranosyl-(1-4)-beta-D-xylopyranosyl-(1-4)-beta-D-xylopyranose
Halalkalibacterium halodurans
-
-
0.0044
beta-D-xylopyranosyl-(1-4)-beta-D-xylopyranosyl-(1-4)-beta-D-xylopyranosyl-(1-4)-beta-D-xylopyranosyl-(1-4)-beta-D-xylopyranose
Halalkalibacterium halodurans
-
-
0.0185
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
Halalkalibacterium halodurans
-
-
1.64
xylotriose
pH 7.0, 40°C, recombinant wild-type enzyme
0.0024
beta-D-xylopyranosyl-(1-4)-beta-D-xylopyranosyl-(1-4)-beta-D-xylopyranose
Halalkalibacterium halodurans
-
-
0.0344
beta-D-xylopyranosyl-(1-4)-beta-D-xylopyranosyl-(1-4)-beta-D-xylopyranose
Halalkalibacterium halodurans
-
mutant enzyme H319A
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TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
162
beta-D-xylopyranosyl-(1-4)-beta-D-xylopyranosyl-(1-4)-beta-D-xylopyranosyl-(1-4)-beta-D-xylopyranose
Halalkalibacterium halodurans
-
-
73
beta-D-xylopyranosyl-(1-4)-beta-D-xylopyranosyl-(1-4)-beta-D-xylopyranosyl-(1-4)-beta-D-xylopyranosyl-(1-4)-beta-D-xylopyranose
Halalkalibacterium halodurans
-
-
175
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
Halalkalibacterium halodurans
-
-
118.8
xylotriose
pH 7.0, 40°C, recombinant wild-type enzyme
21
beta-D-xylopyranosyl-(1-4)-beta-D-xylopyranosyl-(1-4)-beta-D-xylopyranose
Halalkalibacterium halodurans
-
mutant enzyme H319A
163
beta-D-xylopyranosyl-(1-4)-beta-D-xylopyranosyl-(1-4)-beta-D-xylopyranose
Halalkalibacterium halodurans
-
-
1455
wheat flour arabinoxylan
-
apparent value, at pH 6.0, 40°C
-
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kcat/KM VALUE [1/mMs-1]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
30
2-nitrophenyl Xylbeta(1-4)Xylbeta(1-4)Xylbeta(1-4)Xylbeta(1-4)Xylbeta
Halalkalibacterium halodurans
-
apparent value, at pH 6.0, 40°C
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pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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pH RANGE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
4 - 10
5.3 - 8.2
Halalkalibacterium halodurans
-
pH 5.3: about 60% of maximal activity, pH 8.2: about 50% of maximal activity
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TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
40
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TEMPERATURE RANGE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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pI VALUE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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ORGANISM
COMMENTARY
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
Halalkalibacterium halodurans
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SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
SOURCE
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LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY
GeneOntology No.
LITERATURE
SOURCE
additional information
additional information
the enzyme contains no signal peptide
-
brenda
additional information
-
the enzyme contains no signal peptide
-
brenda
additional information
-
the enzyme contains no signal peptide
-
-
brenda
additional information
-
the enzyme contains no signal peptide
-
-
brenda
additional information
-
the enzyme contains no signal peptide
-
-
brenda
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GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
evolution
physiological function
additional information
evolution
the enzyme belongs to the glycoside hydrolase family 8, GH8
evolution
-
the enzyme belongs to the glycoside hydrolase family 8, GH8
-
evolution
-
the enzyme belongs to the glycoside hydrolase family 8, GH8
-
evolution
-
the enzyme belongs to the glycoside hydrolase family 8, GH8
-
physiological function
Rex8As are key enzymes in the efficient saccharification of heteroxylan into xylose, a major component of lignocellulosic substrates
physiological function
Halalkalibacterium halodurans
Rex8As are key enzymes in the efficient saccharification of heteroxylan into xylose, a major component of lignocellulosic substrates
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
physiological function
-
Rex8As are key enzymes in the efficient saccharification of heteroxylan into xylose, a major component of lignocellulosic substrates
-
physiological function
Halalkalibacterium halodurans DSM 181973
-
Rex8As are key enzymes in the efficient saccharification of heteroxylan into xylose, a major component of lignocellulosic substrates
-
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
-
physiological function
-
Rex8As are key enzymes in the efficient saccharification of heteroxylan into xylose, a major component of lignocellulosic substrates
-
physiological function
-
Rex8As are key enzymes in the efficient saccharification of heteroxylan into xylose, a major component of lignocellulosic substrates
-
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
-
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
-
physiological function
-
Rex8As are key enzymes in the efficient saccharification of heteroxylan into xylose, a major component of lignocellulosic substrates
-
additional information
-
three conserved catalytic residues are Glu90, Asp148, and Asp286
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
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
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
-
additional information
-
three conserved catalytic residues are Glu90, Asp148, and Asp286
-
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
-
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
-
Show AA Sequence and Transmembrane Helices (108 entries)
Please use the AA Sequence and Transmembrane Helices Search for a specific query.
Please use the AA Sequence and Transmembrane Helices Search for a specific query.
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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
additional information
?
Halalkalibacterium halodurans DSM 181973
-
x * 44200, SDS-PAGE
-
additional information
-
secondary and quarternary structure analysis, gel filtration and circular dichroism spectroscopy, overview
additional information
-
secondary and quarternary structure analysis, gel filtration and circular dichroism spectroscopy, overview
-
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CRYSTALLIZATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
hanging-drop vapour-diffusion method using 13.6 mg/ml Rex, 5.6% v/v polyethylene glycol 4000, 70 mM sodium acetate pH 4.6 and 30% v/v glycerol. The crystals belong to the space group P2(1)2(1)2(1), with unit-cell parameters a = 52.69, b = 86.02, c = 87.92 A
Halalkalibacterium halodurans
-
mutants of reducing-end xylose-releasing exooligoxylanase with glycosynthase activity, X-ray diffraction structure determination and analysis at 1.39-2.10 A resolution
Halalkalibacterium halodurans
xylose-enzyme complex is prepared by cocrystallization using a reservoir solution containing 10 mM xylose. The xylobiose complex of the E70A mutant enzyme is prepared by cocrystallization using a reservoir solution containing 10 mM xylotriose
Halalkalibacterium halodurans
-
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PROTEIN VARIANTS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
D128A
Halalkalibacterium halodurans
-
specific activity is 290fold lower than that of the wild-type enzyme
D263A
D263C
D263G
D263L
Halalkalibacterium halodurans
-
conversion of glycosynthase from converting enzyme, synthesis of some xylotriose from xylobiose + HF + xylose
D263N
D263S
D263T
Halalkalibacterium halodurans
-
conversion of glycosynthase from converting enzyme, synthesis of some xylotriose from xylobiose + HF + xylose
D263V
Halalkalibacterium halodurans
-
conversion of glycosynthase from converting enzyme, synthesis of some xylotriose from xylobiose + HF + xylose
D263X
Halalkalibacterium halodurans
-
construction of a D263 mutant library by saturation mutagenesis
D70A
Halalkalibacterium halodurans
-
specific activity is 1545fold lower than that of the wild-type enzyme
H319A
Halalkalibacterium halodurans
-
mutation causes a drastic decrease in activity towards the substrate beta-D-xylopyranosyl-(1-4)-beta-D-xylopyranosyl-(1-4)-beta-D-xylopyranose
Y198F
Y198F/D263N
Halalkalibacterium halodurans
-
Y198F/D263N showed 20 times less F- releasing activity than Y198F, which is comparable to that of the corresponding single mutant, D263N. Km: 6.0 (xylose), kcat: 0.42/sec (xylose)
D128A
Halalkalibacterium halodurans C-125
-
specific activity is 290fold lower than that of the wild-type enzyme
-
D263A
Halalkalibacterium halodurans C-125
-
specific activity is 4421fold lower than that of the wild-type enzyme
-
D70A
Halalkalibacterium halodurans C-125
-
specific activity is 1545fold lower than that of the wild-type enzyme
-
H319A
Halalkalibacterium halodurans C-125
-
mutation causes a drastic decrease in activity towards the substrate beta-D-xylopyranosyl-(1-4)-beta-D-xylopyranosyl-(1-4)-beta-D-xylopyranose
-
E70A
additional information
Halalkalibacterium halodurans
-
method for construction of a mutant engineered reducing-end xylose-releasing exooligoxylanase, with mutation of residues Y198 and D263, that acts as a glycosynthase, reaction mechanism and modelling, overview. Glycosynthases are engineered glycoside hydrolases, that catalyze the synthesis of glycoside from glycosyl-fluoride donors and suitable acceptors, overview
D263A
Halalkalibacterium halodurans
-
specific activity is 4421fold lower than that of the wild-type enzyme
D263A
Halalkalibacterium halodurans
-
conversion of glycosynthase from converting enzyme, synthesis of some xylotriose from xylobiose + HF + xylose
D263C
Halalkalibacterium halodurans
-
conversion of glycosynthase from converting enzyme, synthesis of xylotriose from xylobiose + HF + xylose, highest glycosynthase activity of mutants tested
D263C
Halalkalibacterium halodurans
construction of a mutant engineered reducing-end xylose-releasing exooligoxylanase, that acts as a glycosynthase. Glycosynthases are engineered glycoside hydrolases, that catalyze the synthesis of glycoside from glycosyl-fluoride donors and suitable acceptors, crystal structure determination, overview
D263C
Halalkalibacterium halodurans
-
saturation mutagenesis, the mutant accumulates high amounts of xylotriose, but reduced F- releasing activity compared to the wild-type enzyme
D263G
Halalkalibacterium halodurans
-
conversion of glycosynthase from converting enzyme, synthesis of some xylotriose from xylobiose + HF + xylose
D263G
Halalkalibacterium halodurans
construction of a mutant engineered reducing-end xylose-releasing exooligoxylanase, that acts as a glycosynthase. Glycosynthases are engineered glycoside hydrolases, that catalyze the synthesis of glycoside from glycosyl-fluoride donors and suitable acceptors, crystal structure determination, overview
D263N
Halalkalibacterium halodurans
-
conversion of glycosynthase from converting enzyme, synthesis of xylotriose from xylobiose + HF + xylose, second highest glycosynthase activity of mutants tested
D263N
Halalkalibacterium halodurans
-
mutations at D263 results in decreased F- releasing activity
D263N
Halalkalibacterium halodurans
construction of a mutant engineered reducing-end xylose-releasing exooligoxylanase, that acts as a glycosynthase. Glycosynthases are engineered glycoside hydrolases, that catalyze the synthesis of glycoside from glycosyl-fluoride donors and suitable acceptors, crystal structure determination, overview
D263S
Halalkalibacterium halodurans
construction of a mutant engineered reducing-end xylose-releasing exooligoxylanase, that acts as a glycosynthase. Glycosynthases are engineered glycoside hydrolases, that catalyze the synthesis of glycoside from glycosyl-fluoride donors and suitable acceptors, crystal structure determination, overview
Y198F
Halalkalibacterium halodurans
-
a mutation in the tyrosine residue changing it into phenylalanine causes a drastic decrease in the hydrolytic activity and a small increase in F- releasing activity from alpha-xylobiosyl fluoride in the presence of xylose. As a result of the high F- releasing activity and low hydrolytic activity, Y198F of Rex accumulates a large amount of product during the glycosynthase reaction. Km: 14.8 (xylose), kcat: 11.9/sec (xylose)
Y198F
Halalkalibacterium halodurans
construction of a mutant engineered reducing-end xylose-releasing exooligoxylanase, that acts as a glycosynthase. Glycosynthases are engineered glycoside hydrolases, that catalyze the synthesis of glycoside from glycosyl-fluoride donors and suitable acceptors, crystal structure determination, overview
Y198F
Halalkalibacterium halodurans
-
saturation mutagenesis, the mutant shows highly reduced hydrolytic activity and slightly increased F- releasing activity from alpha-xylobiosyl fluoride in presence of xylose compared to the wild-type enzyme
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pH STABILITY
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
5 - 9.8
Halalkalibacterium halodurans
-
30°C, 30 min, stable
659431
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TEMPERATURE STABILITY
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
40
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GENERAL STABILITY
ORGANISM
UNIPROT
LITERATURE
purified enzyme is stable for at least 4 months at 4°C in 25 mM sodium acetate buffer, pH 5.0
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PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
by using a single-step HisTrap purification performed on a Atka fast protein liquid chromatograph. Protein yield: 140 mg recombinant enzyme per liter cell culture
Ni-NTA affinity column chromatography, HisTrap HP column chromatography, Q Sepharose column chromatography, and SP Sepharose column chromatography
recombinant His-tagged wild-type and mutant enzymes from Escherichia coli strain BL-21 Codon-Plus(DE3) RIL by metal affinity chromatography
-
recombinant His6-tagged wild-type and mutant enzymes from Escherichia coli strain BL21 Star (DE3) by nickel affinity chromatography to homogeneity
Ni-NTA affinity column chromatography, HisTrap HP column chromatography, Q Sepharose column chromatography, and SP Sepharose column chromatography
-
Ni-NTA affinity column chromatography, HisTrap HP column chromatography, Q Sepharose column chromatography, and SP Sepharose column chromatography
-
Ni-NTA affinity column chromatography, HisTrap HP column chromatography, Q Sepharose column chromatography, and SP Sepharose column chromatography
Halalkalibacterium halodurans
-
Ni-NTA affinity column chromatography, HisTrap HP column chromatography, Q Sepharose column chromatography, and SP Sepharose column chromatography
-
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CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
expressed as a His-tagged fusion protein in Escherichia coli
expressed in Escherichia coli BL21(DE3)pLysS cells
expression of wild-type and mutant enzymes in Escherichia coli strain BL21
Halalkalibacterium halodurans
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)
gene rex8A, the gene is located downstream of a GH3 gene (xyl3A), DNA and amino acid sequence determination and analysis, genetic organization, phylogenetic analysis, recombinant expression of His-tagged wild-type and mutant enzymes in Escherichia coli strain BL-21 Codon-Plus(DE3) RIL
-
expressed as a His-tagged fusion protein in Escherichia coli
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APPLICATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
biotechnology
Halalkalibacterium halodurans
-
a novel method for producing a glycosynthase from an inverting glycoside hydrolase by mutating a residue that holds the nucleophilic water molecule (Y198) with the general base residue while keeping the general base residue intact
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REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Honda, Y.; Fushinobu, S.; Hidaka, M.; Wakagi, T.; Shoun, H.; Kitaoka, M.
Crystallization and preliminary X-ray analysis of reducing-end xylose-releasing exo-oligoxylanase from Bacillus halodurans C-125
Acta Crystallogr. Sect. F
61
291-292
2005
Halalkalibacterium halodurans, Halalkalibacterium halodurans C-125
brenda
Honda, Y.; Kitaoka, M.
A family 8 glycoside hydrolase from Bacillus halodurans C-125 (BH2105) is a reducing end xylose-releasing exo-oligoxylanase
J. Biol. Chem.
279
55097-55103
2004
Halalkalibacterium halodurans, Halalkalibacterium halodurans C-125
brenda
Fushinobu, S.; Hidaka, M.; Honda, Y.; Wakagi, T.; Shoun, H.; Kitaoka, M.
Structural basis for the specificity of the reducing end xylose-releasing exo-oligoxylanase from Bacillus halodurans C-125
J. Biol. Chem.
280
17180-17186
2005
Halalkalibacterium halodurans, Halalkalibacterium halodurans C-125
brenda
Honda, Y.; Kitaoka, M.
The first glycosynthase derived from an inverting glycoside hydrolase
J. Biol. Chem.
281
1426-1431
2006
Halalkalibacterium halodurans
brenda
Lagaert, S.; Van Campenhout, S.; Pollet, A.; Bourgois, T.M.; Delcour, J.A.; Courtin, C.M.; Volckaert, G.
Recombinant expression and characterization of a reducing-end xylose-releasing exo-oligoxylanase from Bifidobacterium adolescentis
Appl. Environ. Microbiol.
73
5374-5377
2007
Bifidobacterium adolescentis (A1A048), Bifidobacterium adolescentis
brenda
Honda, Y.; Fushinobu, S.; Hidaka, M.; Wakagi, T.; Shoun, H.; Taniguchi, H.; Kitaoka, M.
Alternative strategy for converting an inverting glycoside hydrolase into a glycosynthase
Glycobiology
18
325-330
2008
Halalkalibacterium halodurans
brenda
Hidaka, M.; Fushinobu, S.; Honda, Y.; Wakagi, T.; Shoun, H.; Kitaoka, M.
Structural explanation for the acquisition of glycosynthase activity
J. Biochem.
147
237-244
2010
Halalkalibacterium halodurans (Q9KB30)
brenda
Motomitsu, K.; Yuji, H.; Shinya, F.; Masafumi, H.; Takane, K.; Kenji, Y.
Conversion of inverting glycoside hydrolases into catalysts for synthesizing glycosides employing a glycosynthase strategy
Trends Glycosci. Glycotechnol.
21
23-39
2009
Halalkalibacterium halodurans
-
brenda
Pollet, A.; Schoepe, J.; Dornez, E.; Strelkov, S.; Delcour, J.; Courtin, C.
Functional analysis of glycoside hydrolase family 8 xylanases shows narrow but distinct substrate specificities and biotechnological potential
Appl. Microbiol. Biotechnol.
87
2125-2135
2010
Halalkalibacterium halodurans, uncultured bacterium, Bifidobacterium adolescentis, Pseudoalteromonas haloplanktis
brenda
Lagaert, S.; Pollet, A.; Delcour, J.A.; Lavigne, R.; Courtin, C.M.; Volckaert, G.
Characterization of two beta-xylosidases from Bifidobacterium adolescentis and their contribution to the hydrolysis of prebiotic xylooligosaccharides
Appl. Microbiol. Biotechnol.
92
1179-1185
2011
Bifidobacterium adolescentis (A1A048), Bifidobacterium adolescentis
brenda
Hong, P.Y.; Iakiviak, M.; Dodd, D.; Zhang, M.; Mackie, R.I.; Cann, I.
Two new xylanases with different substrate specificities from the human gut bacterium Bacteroides intestinalis DSM 17393
Appl. Environ. Microbiol.
80
2084-2093
2014
Bacteroides intestinalis, Bacteroides intestinalis DSM 17393
brenda
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
Appl. Environ. Microbiol.
82
5116-5124
2016
Paenibacillus barcinonensis (A0A0S2UQQ5), Paenibacillus barcinonensis, Paenibacillus barcinonensis CECT 7022 (A0A0S2UQQ5), Paenibacillus barcinonensis BP-23 (A0A0S2UQQ5), Paenibacillus barcinonensis DSM 15478 (A0A0S2UQQ5), Paenibacillus barcinonensis DSM 15478
brenda
Malgas, S.; Pletschke, B.I.
The effect of an oligosaccharide reducing-end xylanase, BhRex8A, on the synergistic degradation of xylan backbones by an optimised xylanolytic enzyme cocktail
Enzyme Microb. Technol.
122
74-81
2019
Bifidobacterium adolescentis (A1A048), Bifidobacterium adolescentis, Halalkalibacterium halodurans (Q9KB30), Bifidobacterium adolescentis ATCC 15703 (A1A048), Halalkalibacterium halodurans DSM 181973 (Q9KB30), Bifidobacterium adolescentis NCTC 11814 (A1A048), Bifidobacterium adolescentis E194a (A1A048), Bifidobacterium adolescentis DSM 20083 (A1A048)
brenda
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Release 2023.1 (January 2023)
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