3.2.1.156: oligosaccharide reducing-end xylanase

This is an abbreviated version!
For detailed information about oligosaccharide reducing-end xylanase, go to the full flat file.

Reaction

Synonyms

BaRex8A, BhRex8A, DFQ00_11062, GH8 xylanase, More, oligosaccharide reducing-end xylanase, PhXyl, reducing end xylose-releasing exo-oligoxylanase, reducing-end xylose-releasing exo-oligoxylanase, reducing-end xylose-releasing exooligoxylanase, Rex, Rex8A, RexA, rXyn8, XYLA

ECTree

     3 Hydrolases

         3.2 Glycosylases

             3.2.1 Glycosidases, i.e. enzymes that hydrolyse O- and S-glycosyl compounds

                3.2.1.156 oligosaccharide reducing-end xylanase

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Results	in table
108	AA Sequence
1	Application
2	CAS Registry Number
10	Cloned(Commentary)
3	Crystallization (Commentary)
21	General Information
1	General Stability
13	kcat/KM [mM/s]
9	KM Value [mM]
6	Localization
1	Molecular Weight [Da]
11	Natural Substrates/ Products (Substrates)
47	Organism
24	PDB ID
8	pH Optimum
3	pH Range
1	pH Stability
1	pI Value
39	Protein Variants
9	Purification (Commentary)
5	Reaction
2	Reaction Type
29	Reference
7	Source Tissue
131	Substrates and Products (Substrate)
13	Subunits
65	Synonyms
1	Systematic Name
8	Temperature Optimum [°C]
1	Temperature Range [°C]
2	Temperature Stability [°C]
13	Turnover Number [1/s]

Engineering

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Engineering on EC 3.2.1.156 - oligosaccharide reducing-end xylanase

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PROTEIN VARIANTS

ORGANISM

UNIPROT

COMMENTARY

LITERATURE

D148A

Bacteroides intestinalis

-

site-directed mutagenesis, inactive mutant

731182

D286A

Bacteroides intestinalis

-

site-directed mutagenesis, inactive mutant

731182

E90A

Bacteroides intestinalis

-

site-directed mutagenesis, inactive mutant

731182

D148A

Bacteroides intestinalis DSM 17393

-

site-directed mutagenesis, inactive mutant

-

D286A

Bacteroides intestinalis DSM 17393

-

site-directed mutagenesis, inactive mutant

-

E90A

Bacteroides intestinalis DSM 17393

-

site-directed mutagenesis, inactive mutant

-

D128A

Halalkalibacterium halodurans

-

specific activity is 290fold lower than that of the wild-type enzyme

659431

D263A

2 entries

D263C

3 entries

D263G

2 entries

D263L

Halalkalibacterium halodurans

-

conversion of glycosynthase from converting enzyme, synthesis of some xylotriose from xylobiose + HF + xylose

665712

D263N

3 entries

D263P

Halalkalibacterium halodurans

-

very little glycosynthase or converting activity

665712

D263S

2 entries

D263T

Halalkalibacterium halodurans

-

conversion of glycosynthase from converting enzyme, synthesis of some xylotriose from xylobiose + HF + xylose

665712

D263V

Halalkalibacterium halodurans

-

conversion of glycosynthase from converting enzyme, synthesis of some xylotriose from xylobiose + HF + xylose

665712

D263X

Halalkalibacterium halodurans

-

construction of a D263 mutant library by saturation mutagenesis

710649

D70A

Halalkalibacterium halodurans

-

specific activity is 1545fold lower than that of the wild-type enzyme

659431

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

659467

Y198F

3 entries

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)

680048

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

4 entries

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

710649

D263A

Halalkalibacterium halodurans

-

specific activity is 4421fold lower than that of the wild-type enzyme

659431

D263A

Halalkalibacterium halodurans

-

conversion of glycosynthase from converting enzyme, synthesis of some xylotriose from xylobiose + HF + xylose

665712

D263C

Halalkalibacterium halodurans

-

conversion of glycosynthase from converting enzyme, synthesis of xylotriose from xylobiose + HF + xylose, highest glycosynthase activity of mutants tested

665712

D263C

Halalkalibacterium halodurans

Q9KB30

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

708955

D263C

Halalkalibacterium halodurans

-

saturation mutagenesis, the mutant accumulates high amounts of xylotriose, but reduced F- releasing activity compared to the wild-type enzyme

710649

D263G

Halalkalibacterium halodurans

-

conversion of glycosynthase from converting enzyme, synthesis of some xylotriose from xylobiose + HF + xylose

665712

D263G

Halalkalibacterium halodurans

Q9KB30

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

708955

D263N

Halalkalibacterium halodurans

-

conversion of glycosynthase from converting enzyme, synthesis of xylotriose from xylobiose + HF + xylose, second highest glycosynthase activity of mutants tested

665712

D263N

Halalkalibacterium halodurans

-

mutations at D263 results in decreased F- releasing activity

680048

D263N

Halalkalibacterium halodurans

Q9KB30

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

708955

D263S

Halalkalibacterium halodurans

-

very little glycosynthase or converting activity

665712

D263S

Halalkalibacterium halodurans

Q9KB30

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

708955

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)

680048

Y198F

Halalkalibacterium halodurans

Q9KB30

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

708955

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

710649

E70A

Paenibacillus barcinonensis

A0A0S2UQQ5

site-directed mutagenesis

752545

E70A

Paenibacillus barcinonensis BP-23

-

site-directed mutagenesis

-

E70A

Paenibacillus barcinonensis CECT 7022

-

site-directed mutagenesis

-

E70A

Paenibacillus barcinonensis DSM 15478

-

site-directed mutagenesis

-