BRENDA - Enzyme Database

A family 8 glycoside hydrolase from Bacillus halodurans C-125 (BH2105) is a reducing end xylose-releasing exo-oligoxylanase

Honda, Y.; Kitaoka, M.; J. Biol. Chem. 279, 55097-55103 (2004) View publication on PubMed

Data extracted from this reference:

Cloned(Commentary)
EC Number
Cloned (Commentary)
Organism
3.2.1.156
expression in Escherichia coli
Alkalihalobacillus halodurans
Engineering
EC Number
Protein Variants
Commentary
Organism
3.2.1.156
D128A
specific activity is 290fold lower than that of the wild-type enzyme
Alkalihalobacillus halodurans
3.2.1.156
D263A
specific activity is 4421fold lower than that of the wild-type enzyme
Alkalihalobacillus halodurans
3.2.1.156
D70A
specific activity is 1545fold lower than that of the wild-type enzyme
Alkalihalobacillus halodurans
KM Value [mM]
EC Number
KM Value [mM]
KM Value Maximum [mM]
Substrate
Commentary
Organism
Structure
3.2.1.156
0.0024
-
beta-D-xylopyranosyl-(1-4)-beta-D-xylopyranosyl-(1-4)-beta-D-xylopyranose
-
Alkalihalobacillus halodurans
3.2.1.156
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
-
Alkalihalobacillus halodurans
3.2.1.156
0.005
-
beta-D-xylopyranosyl-(1-4)-beta-D-xylopyranosyl-(1-4)-beta-D-xylopyranosyl-(1-4)-beta-D-xylopyranose
-
Alkalihalobacillus halodurans
3.2.1.156
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
-
Alkalihalobacillus halodurans
Localization
EC Number
Localization
Commentary
Organism
GeneOntology No.
Textmining
3.2.1.156
intracellular
-
Alkalihalobacillus halodurans
5622
-
Natural Substrates/ Products (Substrates)
EC Number
Natural Substrates
Organism
Commentary (Nat. Sub.)
Natural Products
Commentary (Nat. Pro.)
Organism (Nat. Pro.)
Reversibility
ID
3.2.1.156
additional information
Alkalihalobacillus 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
?
-
-
?
3.2.1.156
additional information
Alkalihalobacillus 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
?
-
-
?
Organism
EC Number
Organism
UniProt
Commentary
Textmining
3.2.1.156
Alkalihalobacillus halodurans
-
C-125
-
3.2.1.156
Alkalihalobacillus halodurans C-125
-
C-125
-
Purification (Commentary)
EC Number
Purification (Commentary)
Organism
3.2.1.156
-
Alkalihalobacillus halodurans
Substrates and Products (Substrate)
EC Number
Substrates
Commentary Substrates
Literature (Substrates)
Organism
Products
Commentary (Products)
Literature (Products)
Organism (Products)
Reversibility
Substrate Product ID
3.2.1.156
beta-D-glucopyranosyl-(1-4)-beta-D-xylopyranosyl-(1-4)-beta-D-xylopyranose + H2O
1.1% of the activity with beta-D-xylopyranosyl-(1-4)-beta-D-xylopyranosyl-(1-4)-beta-D-xylopyranose
659431
Alkalihalobacillus halodurans
?
-
-
-
?
3.2.1.156
beta-D-glucopyranosyl-(1-4)-beta-D-xylopyranosyl-(1-4)-beta-D-xylopyranose + H2O
1.1% of the activity with beta-D-xylopyranosyl-(1-4)-beta-D-xylopyranosyl-(1-4)-beta-D-xylopyranose
659431
Alkalihalobacillus halodurans C-125
?
-
-
-
?
3.2.1.156
beta-D-xylopyranosyl-(1-4)-beta-D-xylopyranosyl-(1-4)-beta-D-deoxyxylopyranose + H2O
3.2% of the activity with beta-D-xylopyranosyl-(1-4)-beta-D-xylopyranosyl-(1-4)-beta-D-xylopyranose
659431
Alkalihalobacillus halodurans
?
-
-
-
?
3.2.1.156
beta-D-xylopyranosyl-(1-4)-beta-D-xylopyranosyl-(1-4)-beta-D-deoxyxylopyranose + H2O
3.2% of the activity with beta-D-xylopyranosyl-(1-4)-beta-D-xylopyranosyl-(1-4)-beta-D-xylopyranose
659431
Alkalihalobacillus halodurans C-125
?
-
-
-
?
3.2.1.156
beta-D-xylopyranosyl-(1-4)-beta-D-xylopyranosyl-(1-4)-beta-D-glucopyranose + H2O
0.5% of the activity with beta-D-xylopyranosyl-(1-4)-beta-D-xylopyranosyl-(1-4)-beta-D-xylopyranose
659431
Alkalihalobacillus halodurans
?
-
-
-
?
3.2.1.156
beta-D-xylopyranosyl-(1-4)-beta-D-xylopyranosyl-(1-4)-beta-D-glucopyranose + H2O
0.5% of the activity with beta-D-xylopyranosyl-(1-4)-beta-D-xylopyranosyl-(1-4)-beta-D-xylopyranose
659431
Alkalihalobacillus halodurans C-125
?
-
-
-
?
3.2.1.156
beta-D-xylopyranosyl-(1-4)-beta-D-xylopyranosyl-(1-4)-beta-D-xylopyranose + H2O
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
659431
Alkalihalobacillus halodurans
beta-D-xylopyranosyl-(1-4)-alpha-D-xylopyranose
-
-
-
?
3.2.1.156
beta-D-xylopyranosyl-(1-4)-beta-D-xylopyranosyl-(1-4)-beta-D-xylopyranose + H2O
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
659431
Alkalihalobacillus halodurans C-125
beta-D-xylopyranosyl-(1-4)-alpha-D-xylopyranose
-
-
-
?
3.2.1.156
beta-D-xylopyranosyl-(1-4)-beta-D-xylopyranosyl-(1-4)-beta-D-xylopyranosyl-(1-4)-beta-D-xylopyranose + H2O
-
659431
Alkalihalobacillus halodurans
?
-
-
-
?
3.2.1.156
beta-D-xylopyranosyl-(1-4)-beta-D-xylopyranosyl-(1-4)-beta-D-xylopyranosyl-(1-4)-beta-D-xylopyranosyl-(1-4)-beta-D-xylopyranose + H2O
-
659431
Alkalihalobacillus halodurans
?
-
-
-
?
3.2.1.156
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
-
659431
Alkalihalobacillus halodurans
?
-
-
-
?
3.2.1.156
additional information
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
659431
Alkalihalobacillus halodurans
?
-
-
-
?
3.2.1.156
additional information
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
659431
Alkalihalobacillus halodurans C-125
?
-
-
-
?
Synonyms
EC Number
Synonyms
Commentary
Organism
3.2.1.156
reducing end xylose-releasing exo-oligoxylanase
-
Alkalihalobacillus halodurans
3.2.1.156
Rex
-
Alkalihalobacillus halodurans
Temperature Optimum [°C]
EC Number
Temperature Optimum [°C]
Temperature Optimum Maximum [°C]
Commentary
Organism
3.2.1.156
50
-
-
Alkalihalobacillus halodurans
Temperature Range [°C]
EC Number
Temperature Minimum [°C]
Temperature Maximum [°C]
Commentary
Organism
3.2.1.156
35
55
about 50% of maximal activity at 35°C and at 55°C
Alkalihalobacillus halodurans
Temperature Stability [°C]
EC Number
Temperature Stability Minimum [°C]
Temperature Stability Maximum [°C]
Commentary
Organism
3.2.1.156
40
-
pH 7.1, 30 min, stable at temperatures up to
Alkalihalobacillus halodurans
Turnover Number [1/s]
EC Number
Turnover Number Minimum [1/s]
Turnover Number Maximum [1/s]
Substrate
Commentary
Organism
Structure
3.2.1.156
73
-
beta-D-xylopyranosyl-(1-4)-beta-D-xylopyranosyl-(1-4)-beta-D-xylopyranosyl-(1-4)-beta-D-xylopyranosyl-(1-4)-beta-D-xylopyranose
-
Alkalihalobacillus halodurans
3.2.1.156
162
-
beta-D-xylopyranosyl-(1-4)-beta-D-xylopyranosyl-(1-4)-beta-D-xylopyranosyl-(1-4)-beta-D-xylopyranose
-
Alkalihalobacillus halodurans
3.2.1.156
163
-
beta-D-xylopyranosyl-(1-4)-beta-D-xylopyranosyl-(1-4)-beta-D-xylopyranose
-
Alkalihalobacillus halodurans
3.2.1.156
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
-
Alkalihalobacillus halodurans
pH Optimum
EC Number
pH Optimum Minimum
pH Optimum Maximum
Commentary
Organism
3.2.1.156
6.2
7.3
-
Alkalihalobacillus halodurans
pH Range
EC Number
pH Minimum
pH Maximum
Commentary
Organism
3.2.1.156
5.3
8.2
pH 5.3: about 60% of maximal activity, pH 8.2: about 50% of maximal activity
Alkalihalobacillus halodurans
pH Stability
EC Number
pH Stability
pH Stability Maximum
Commentary
Organism
3.2.1.156
5
9.8
30°C, 30 min, stable
Alkalihalobacillus halodurans
Cloned(Commentary) (protein specific)
EC Number
Commentary
Organism
3.2.1.156
expression in Escherichia coli
Alkalihalobacillus halodurans
Engineering (protein specific)
EC Number
Protein Variants
Commentary
Organism
3.2.1.156
D128A
specific activity is 290fold lower than that of the wild-type enzyme
Alkalihalobacillus halodurans
3.2.1.156
D263A
specific activity is 4421fold lower than that of the wild-type enzyme
Alkalihalobacillus halodurans
3.2.1.156
D70A
specific activity is 1545fold lower than that of the wild-type enzyme
Alkalihalobacillus halodurans
KM Value [mM] (protein specific)
EC Number
KM Value [mM]
KM Value Maximum [mM]
Substrate
Commentary
Organism
Structure
3.2.1.156
0.0024
-
beta-D-xylopyranosyl-(1-4)-beta-D-xylopyranosyl-(1-4)-beta-D-xylopyranose
-
Alkalihalobacillus halodurans
3.2.1.156
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
-
Alkalihalobacillus halodurans
3.2.1.156
0.005
-
beta-D-xylopyranosyl-(1-4)-beta-D-xylopyranosyl-(1-4)-beta-D-xylopyranosyl-(1-4)-beta-D-xylopyranose
-
Alkalihalobacillus halodurans
3.2.1.156
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
-
Alkalihalobacillus halodurans
Localization (protein specific)
EC Number
Localization
Commentary
Organism
GeneOntology No.
Textmining
3.2.1.156
intracellular
-
Alkalihalobacillus halodurans
5622
-
Natural Substrates/ Products (Substrates) (protein specific)
EC Number
Natural Substrates
Organism
Commentary (Nat. Sub.)
Natural Products
Commentary (Nat. Pro.)
Organism (Nat. Pro.)
Reversibility
ID
3.2.1.156
additional information
Alkalihalobacillus 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
?
-
-
?
3.2.1.156
additional information
Alkalihalobacillus 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
?
-
-
?
Purification (Commentary) (protein specific)
EC Number
Commentary
Organism
3.2.1.156
-
Alkalihalobacillus halodurans
Substrates and Products (Substrate) (protein specific)
EC Number
Substrates
Commentary Substrates
Literature (Substrates)
Organism
Products
Commentary (Products)
Literature (Products)
Organism (Products)
Reversibility
ID
3.2.1.156
beta-D-glucopyranosyl-(1-4)-beta-D-xylopyranosyl-(1-4)-beta-D-xylopyranose + H2O
1.1% of the activity with beta-D-xylopyranosyl-(1-4)-beta-D-xylopyranosyl-(1-4)-beta-D-xylopyranose
659431
Alkalihalobacillus halodurans
?
-
-
-
?
3.2.1.156
beta-D-glucopyranosyl-(1-4)-beta-D-xylopyranosyl-(1-4)-beta-D-xylopyranose + H2O
1.1% of the activity with beta-D-xylopyranosyl-(1-4)-beta-D-xylopyranosyl-(1-4)-beta-D-xylopyranose
659431
Alkalihalobacillus halodurans C-125
?
-
-
-
?
3.2.1.156
beta-D-xylopyranosyl-(1-4)-beta-D-xylopyranosyl-(1-4)-beta-D-deoxyxylopyranose + H2O
3.2% of the activity with beta-D-xylopyranosyl-(1-4)-beta-D-xylopyranosyl-(1-4)-beta-D-xylopyranose
659431
Alkalihalobacillus halodurans
?
-
-
-
?
3.2.1.156
beta-D-xylopyranosyl-(1-4)-beta-D-xylopyranosyl-(1-4)-beta-D-deoxyxylopyranose + H2O
3.2% of the activity with beta-D-xylopyranosyl-(1-4)-beta-D-xylopyranosyl-(1-4)-beta-D-xylopyranose
659431
Alkalihalobacillus halodurans C-125
?
-
-
-
?
3.2.1.156
beta-D-xylopyranosyl-(1-4)-beta-D-xylopyranosyl-(1-4)-beta-D-glucopyranose + H2O
0.5% of the activity with beta-D-xylopyranosyl-(1-4)-beta-D-xylopyranosyl-(1-4)-beta-D-xylopyranose
659431
Alkalihalobacillus halodurans
?
-
-
-
?
3.2.1.156
beta-D-xylopyranosyl-(1-4)-beta-D-xylopyranosyl-(1-4)-beta-D-glucopyranose + H2O
0.5% of the activity with beta-D-xylopyranosyl-(1-4)-beta-D-xylopyranosyl-(1-4)-beta-D-xylopyranose
659431
Alkalihalobacillus halodurans C-125
?
-
-
-
?
3.2.1.156
beta-D-xylopyranosyl-(1-4)-beta-D-xylopyranosyl-(1-4)-beta-D-xylopyranose + H2O
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
659431
Alkalihalobacillus halodurans
beta-D-xylopyranosyl-(1-4)-alpha-D-xylopyranose
-
-
-
?
3.2.1.156
beta-D-xylopyranosyl-(1-4)-beta-D-xylopyranosyl-(1-4)-beta-D-xylopyranose + H2O
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
659431
Alkalihalobacillus halodurans C-125
beta-D-xylopyranosyl-(1-4)-alpha-D-xylopyranose
-
-
-
?
3.2.1.156
beta-D-xylopyranosyl-(1-4)-beta-D-xylopyranosyl-(1-4)-beta-D-xylopyranosyl-(1-4)-beta-D-xylopyranose + H2O
-
659431
Alkalihalobacillus halodurans
?
-
-
-
?
3.2.1.156
beta-D-xylopyranosyl-(1-4)-beta-D-xylopyranosyl-(1-4)-beta-D-xylopyranosyl-(1-4)-beta-D-xylopyranosyl-(1-4)-beta-D-xylopyranose + H2O
-
659431
Alkalihalobacillus halodurans
?
-
-
-
?
3.2.1.156
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
-
659431
Alkalihalobacillus halodurans
?
-
-
-
?
3.2.1.156
additional information
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
659431
Alkalihalobacillus halodurans
?
-
-
-
?
3.2.1.156
additional information
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
659431
Alkalihalobacillus halodurans C-125
?
-
-
-
?
Temperature Optimum [°C] (protein specific)
EC Number
Temperature Optimum [°C]
Temperature Optimum Maximum [°C]
Commentary
Organism
3.2.1.156
50
-
-
Alkalihalobacillus halodurans
Temperature Range [°C] (protein specific)
EC Number
Temperature Minimum [°C]
Temperature Maximum [°C]
Commentary
Organism
3.2.1.156
35
55
about 50% of maximal activity at 35°C and at 55°C
Alkalihalobacillus halodurans
Temperature Stability [°C] (protein specific)
EC Number
Temperature Stability Minimum [°C]
Temperature Stability Maximum [°C]
Commentary
Organism
3.2.1.156
40
-
pH 7.1, 30 min, stable at temperatures up to
Alkalihalobacillus halodurans
Turnover Number [1/s] (protein specific)
EC Number
Turnover Number Minimum [1/s]
Turnover Number Maximum [1/s]
Substrate
Commentary
Organism
Structure
3.2.1.156
73
-
beta-D-xylopyranosyl-(1-4)-beta-D-xylopyranosyl-(1-4)-beta-D-xylopyranosyl-(1-4)-beta-D-xylopyranosyl-(1-4)-beta-D-xylopyranose
-
Alkalihalobacillus halodurans
3.2.1.156
162
-
beta-D-xylopyranosyl-(1-4)-beta-D-xylopyranosyl-(1-4)-beta-D-xylopyranosyl-(1-4)-beta-D-xylopyranose
-
Alkalihalobacillus halodurans
3.2.1.156
163
-
beta-D-xylopyranosyl-(1-4)-beta-D-xylopyranosyl-(1-4)-beta-D-xylopyranose
-
Alkalihalobacillus halodurans
3.2.1.156
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
-
Alkalihalobacillus halodurans
pH Optimum (protein specific)
EC Number
pH Optimum Minimum
pH Optimum Maximum
Commentary
Organism
3.2.1.156
6.2
7.3
-
Alkalihalobacillus halodurans
pH Range (protein specific)
EC Number
pH Minimum
pH Maximum
Commentary
Organism
3.2.1.156
5.3
8.2
pH 5.3: about 60% of maximal activity, pH 8.2: about 50% of maximal activity
Alkalihalobacillus halodurans
pH Stability (protein specific)
EC Number
pH Stability
pH Stability Maximum
Commentary
Organism
3.2.1.156
5
9.8
30°C, 30 min, stable
Alkalihalobacillus halodurans