BRENDA - Enzyme Database
show all sequences of 3.2.1.162

Purification and characterization of a thermostable delta-carrageenase from a hot spring bacterium, Bacillus sp

Li, J.; Hu, Q.; Seswita-Zilda, D.; Biotechnol. Lett. 36, 1669-1674 (2014)

Data extracted from this reference:

Inhibitors
Inhibitors
Commentary
Organism
Structure
Cd2+
-
Bacillus sp. (in: Bacteria)
Cu2+
-
Bacillus sp. (in: Bacteria)
EDTA
-
Bacillus sp. (in: Bacteria)
Fe2+
-
Bacillus sp. (in: Bacteria)
Mg2+
-
Bacillus sp. (in: Bacteria)
Mn2+
-
Bacillus sp. (in: Bacteria)
Sr2+
-
Bacillus sp. (in: Bacteria)
Localization
Localization
Commentary
Organism
GeneOntology No.
Textmining
extracellular
-
Bacillus sp. (in: Bacteria)
-
-
Metals/Ions
Metals/Ions
Commentary
Organism
Structure
Ca2+
activates
Bacillus sp. (in: Bacteria)
Co2+
activates
Bacillus sp. (in: Bacteria)
K+
activates
Bacillus sp. (in: Bacteria)
Na+
activates
Bacillus sp. (in: Bacteria)
Molecular Weight [Da]
Molecular Weight [Da]
Molecular Weight Maximum [Da]
Commentary
Organism
37000
-
x * 37000, SDS-PAGE
Bacillus sp. (in: Bacteria)
Natural Substrates/ Products (Substrates)
Natural Substrates
Organism
Commentary (Nat. Sub.)
Natural Products
Commentary (Nat. Pro.)
Organism (Nat. Pro.)
Reversibility
delta-carrageenan + H2O
Bacillus sp. (in: Bacteria)
Cga-L50 is an endo-type delta-carrageenase that hydrolyzes beta-1,4-linkages of kappa-carrageenan, yielding neo-delta-carrabiose as the main product
neo-delta-carrabiose + ?
-
-
?
delta-carrageenan + H2O
Bacillus sp. (in: Bacteria) Lc50-1
Cga-L50 is an endo-type delta-carrageenase that hydrolyzes beta-1,4-linkages of kappa-carrageenan, yielding neo-delta-carrabiose as the main product
neo-delta-carrabiose + ?
-
-
?
Organism
Organism
Primary Accession No. (UniProt)
Commentary
Textmining
Bacillus sp. (in: Bacteria)
-
a thermophilic strain isolated from a hot spring in Indonesia
-
Bacillus sp. (in: Bacteria) Lc50-1
-
a thermophilic strain isolated from a hot spring in Indonesia
-
Purification (Commentary)
Commentary
Organism
native enzyme 37.8fold from culture supernatant, by ammonium sulfate fractionation, anion exchange chromatography, and gel filtration
Bacillus sp. (in: Bacteria)
Specific Activity [micromol/min/mg]
Specific Activity Minimum [µmol/min/mg]
Specific Activity Maximum [µmol/min/mg]
Commentary
Organism
105.9
-
purified native enzyme, pH 7.5, 75°C
Bacillus sp. (in: Bacteria)
Substrates and Products (Substrate)
Substrates
Commentary Substrates
Literature (Substrates)
Organism
Products
Commentary (Products)
Literature (Products)
Organism (Products)
Reversibility
delta-carrageenan + H2O
Cga-L50 is an endo-type delta-carrageenase that hydrolyzes beta-1,4-linkages of kappa-carrageenan, yielding neo-delta-carrabiose as the main product
731525
Bacillus sp. (in: Bacteria)
neo-delta-carrabiose + ?
-
-
-
?
delta-carrageenan + H2O
Cga-L50 is an endo-type delta-carrageenase that hydrolyzes beta-1,4-linkages of kappa-carrageenan, yielding neo-delta-carrabiose as the main product
731525
Bacillus sp. (in: Bacteria) Lc50-1
neo-delta-carrabiose + ?
-
-
-
?
Subunits
Subunits
Commentary
Organism
?
x * 37000, SDS-PAGE
Bacillus sp. (in: Bacteria)
Temperature Optimum [°C]
Temperature Optimum [°C]
Temperature Optimum Maximum [°C]
Commentary
Organism
75
-
-
Bacillus sp. (in: Bacteria)
Temperature Stability [°C]
Temperature Stability Minimum [°C]
Temperature Stability Maximum [°C]
Commentary
Organism
85
-
purified native enzyme, 10 min, over 50% activity remaining
Bacillus sp. (in: Bacteria)
pH Optimum
pH Optimum Minimum
pH Optimum Maximum
Commentary
Organism
8
-
-
Bacillus sp. (in: Bacteria)
pH Stability
pH Stability
pH Stability Maximum
Commentary
Organism
6
9
purified native enzyme, stable at
Bacillus sp. (in: Bacteria)
Inhibitors (protein specific)
Inhibitors
Commentary
Organism
Structure
Cd2+
-
Bacillus sp. (in: Bacteria)
Cu2+
-
Bacillus sp. (in: Bacteria)
EDTA
-
Bacillus sp. (in: Bacteria)
Fe2+
-
Bacillus sp. (in: Bacteria)
Mg2+
-
Bacillus sp. (in: Bacteria)
Mn2+
-
Bacillus sp. (in: Bacteria)
Sr2+
-
Bacillus sp. (in: Bacteria)
Localization (protein specific)
Localization
Commentary
Organism
GeneOntology No.
Textmining
extracellular
-
Bacillus sp. (in: Bacteria)
-
-
Metals/Ions (protein specific)
Metals/Ions
Commentary
Organism
Structure
Ca2+
activates
Bacillus sp. (in: Bacteria)
Co2+
activates
Bacillus sp. (in: Bacteria)
K+
activates
Bacillus sp. (in: Bacteria)
Na+
activates
Bacillus sp. (in: Bacteria)
Molecular Weight [Da] (protein specific)
Molecular Weight [Da]
Molecular Weight Maximum [Da]
Commentary
Organism
37000
-
x * 37000, SDS-PAGE
Bacillus sp. (in: Bacteria)
Natural Substrates/ Products (Substrates) (protein specific)
Natural Substrates
Organism
Commentary (Nat. Sub.)
Natural Products
Commentary (Nat. Pro.)
Organism (Nat. Pro.)
Reversibility
delta-carrageenan + H2O
Bacillus sp. (in: Bacteria)
Cga-L50 is an endo-type delta-carrageenase that hydrolyzes beta-1,4-linkages of kappa-carrageenan, yielding neo-delta-carrabiose as the main product
neo-delta-carrabiose + ?
-
-
?
delta-carrageenan + H2O
Bacillus sp. (in: Bacteria) Lc50-1
Cga-L50 is an endo-type delta-carrageenase that hydrolyzes beta-1,4-linkages of kappa-carrageenan, yielding neo-delta-carrabiose as the main product
neo-delta-carrabiose + ?
-
-
?
Purification (Commentary) (protein specific)
Commentary
Organism
native enzyme 37.8fold from culture supernatant, by ammonium sulfate fractionation, anion exchange chromatography, and gel filtration
Bacillus sp. (in: Bacteria)
Specific Activity [micromol/min/mg] (protein specific)
Specific Activity Minimum [µmol/min/mg]
Specific Activity Maximum [µmol/min/mg]
Commentary
Organism
105.9
-
purified native enzyme, pH 7.5, 75°C
Bacillus sp. (in: Bacteria)
Substrates and Products (Substrate) (protein specific)
Substrates
Commentary Substrates
Literature (Substrates)
Organism
Products
Commentary (Products)
Literature (Products)
Organism (Products)
Reversibility
delta-carrageenan + H2O
Cga-L50 is an endo-type delta-carrageenase that hydrolyzes beta-1,4-linkages of kappa-carrageenan, yielding neo-delta-carrabiose as the main product
731525
Bacillus sp. (in: Bacteria)
neo-delta-carrabiose + ?
-
-
-
?
delta-carrageenan + H2O
Cga-L50 is an endo-type delta-carrageenase that hydrolyzes beta-1,4-linkages of kappa-carrageenan, yielding neo-delta-carrabiose as the main product
731525
Bacillus sp. (in: Bacteria) Lc50-1
neo-delta-carrabiose + ?
-
-
-
?
Subunits (protein specific)
Subunits
Commentary
Organism
?
x * 37000, SDS-PAGE
Bacillus sp. (in: Bacteria)
Temperature Optimum [°C] (protein specific)
Temperature Optimum [°C]
Temperature Optimum Maximum [°C]
Commentary
Organism
75
-
-
Bacillus sp. (in: Bacteria)
Temperature Stability [°C] (protein specific)
Temperature Stability Minimum [°C]
Temperature Stability Maximum [°C]
Commentary
Organism
85
-
purified native enzyme, 10 min, over 50% activity remaining
Bacillus sp. (in: Bacteria)
pH Optimum (protein specific)
pH Optimum Minimum
pH Optimum Maximum
Commentary
Organism
8
-
-
Bacillus sp. (in: Bacteria)
pH Stability (protein specific)
pH Stability
pH Stability Maximum
Commentary
Organism
6
9
purified native enzyme, stable at
Bacillus sp. (in: Bacteria)
Other publictions for EC 3.2.1.162
No.
1st author
Pub Med
title
organims
journal
volume
pages
year
Activating Compound
Application
Cloned(Commentary)
Crystallization (Commentary)
Engineering
General Stability
Inhibitors
KM Value [mM]
Localization
Metals/Ions
Molecular Weight [Da]
Natural Substrates/ Products (Substrates)
Organic Solvent Stability
Organism
Oxidation Stability
Posttranslational Modification
Purification (Commentary)
Reaction
Renatured (Commentary)
Source Tissue
Specific Activity [micromol/min/mg]
Storage Stability
Substrates and Products (Substrate)
Subunits
Temperature Optimum [°C]
Temperature Range [°C]
Temperature Stability [°C]
Turnover Number [1/s]
pH Optimum
pH Range
pH Stability
Cofactor
Ki Value [mM]
pI Value
IC50 Value
Activating Compound (protein specific)
Application (protein specific)
Cloned(Commentary) (protein specific)
Cofactor (protein specific)
Crystallization (Commentary) (protein specific)
Engineering (protein specific)
General Stability (protein specific)
IC50 Value (protein specific)
Inhibitors (protein specific)
Ki Value [mM] (protein specific)
KM Value [mM] (protein specific)
Localization (protein specific)
Metals/Ions (protein specific)
Molecular Weight [Da] (protein specific)
Natural Substrates/ Products (Substrates) (protein specific)
Organic Solvent Stability (protein specific)
Oxidation Stability (protein specific)
Posttranslational Modification (protein specific)
Purification (Commentary) (protein specific)
Renatured (Commentary) (protein specific)
Source Tissue (protein specific)
Specific Activity [micromol/min/mg] (protein specific)
Storage Stability (protein specific)
Substrates and Products (Substrate) (protein specific)
Subunits (protein specific)
Temperature Optimum [°C] (protein specific)
Temperature Range [°C] (protein specific)
Temperature Stability [°C] (protein specific)
Turnover Number [1/s] (protein specific)
pH Optimum (protein specific)
pH Range (protein specific)
pH Stability (protein specific)
pI Value (protein specific)
Expression
General Information
General Information (protein specific)
Expression (protein specific)
KCat/KM [mM/s]
KCat/KM [mM/s] (protein specific)
731525
Li
Purification and characterizat ...
Bacillus sp. (in: Bacteria), Bacillus sp. (in: Bacteria) Lc50-1
Biotechnol. Lett.
36
1669-1674
2014
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7
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1
4
1
2
-
5
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1
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1
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2
1
1
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1
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1
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1
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7
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1
4
1
2
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1
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1
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2
1
1
-
1
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1
-
1
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732212
Kang
Efficient enzymatic degradatio ...
Pseudoalteromonas carrageenovora
J. Biotechnol.
192 Pt A
108-113
2014
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1
1
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1
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1
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1
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1
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1
1
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1
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1
1
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1
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1
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1
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1
1
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1
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667539
Guibet
Degradation of lambda-carragee ...
Pseudoalteromonas carrageenovora, Pseudoalteromonas carrageenovora ATCC 43555
Biochem. J.
404
105-114
2007
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-
1
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1
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3
2
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4
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1
1
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1
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7
1
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2
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1
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2
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2
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1
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7
1
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668168
Guibet
Complete assignment of 1H and ...
Pseudoalteromonas carrageenovora
Carbohydr. Res.
341
1859-1869
2006
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3
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1
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669161
Ohta
A novel enzyme, lambda-carrage ...
Pseudoalteromonas sp., Pseudoalteromonas sp. CL19
J. Biochem.
140
475-481
2006
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1
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1
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5
1
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1
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1
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1
1
1
2
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1
1
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1
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1
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5
1
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1
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1
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2
1
1
1
2
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1
1
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668129
Johnston
Enzymic hydrolysis of the pota ...
Pseudomonas carrageenovora
Can. J. Microbiol.
19
779-788
1973
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