BRENDA - Enzyme Database
show all sequences of 3.2.1.145

Molecular cloning and expression in Pichia pastoris of a Irpex lacteus exo-/beta-1,3-galactanase gene

Kotake, T.; Kitazawa, K.; Takata, R.; Okabe, K.; Ichingse, H.; Kaneko, S.; Tsumuraya, Y.; Biosci. Biotechnol. Biochem. 73, 2303-2309 (2009)

Data extracted from this reference:

Cloned(Commentary)
Cloned (Commentary)
Organism
DNA and amino acid sequence determination and analysis, expression of the gene encoding the enzyme fused to a yeast secretion signal sequence under control of the alcohol oxidase promoter in Pichia pastoris
Irpex lacteus
Molecular Weight [Da]
Molecular Weight [Da]
Molecular Weight Maximum [Da]
Commentary
Organism
45520
-
x * 45520, mature enzyme, sequence calculation
Irpex lacteus
Organism
Organism
UniProt
Commentary
Textmining
Irpex lacteus
-
-
-
Irpex lacteus NBRC 5367
-
-
-
Purification (Commentary)
Purification (Commentary)
Organism
recombinant enzyme 0.7fold from Pichia pastoris cell culture medium by cation exchange chromatography and gel filtration
Irpex lacteus
Specific Activity [micromol/min/mg]
Specific Activity Minimum [µmol/min/mg]
Specific Activity Maximum [µmol/min/mg]
Commentary
Organism
47.6
-
purified recombinant enzyme
Irpex lacteus
Substrates and Products (Substrate)
Substrates
Commentary Substrates
Literature (Substrates)
Organism
Products
Commentary (Products)
Literature (Products)
Organism (Products)
Reversibility
Substrate Product ID
beta-1,3-galactan + H2O
best substrate, mode of action, overview
707784
Irpex lacteus
?
-
-
-
?
beta-1,3-galactan + H2O
best substrate, mode of action, overview
707784
Irpex lacteus NBRC 5367
?
-
-
-
?
additional information
substrate specificity, the recombinant enzyme specifically hydrolyses beta-1,3-galactooligosacchrides, as an exo-beta-1,3-galactanase, with high activity for arabinogalactan-proteins from radish, hydrolyzing beta-1,3-galactan main chains, as well as beta-1,3-galactan. Products are beta-1,6-galactobiose, beta-1,6-galactotriose, alpha-arabinofuranosyl-1,3-galactosyl-beta-1,6-galatose with galactose from beta-1,3-galactans attached with and without beta-1,6-galatosyl branchesprepared from acacia gum, overview
707784
Irpex lacteus
?
-
-
-
-
additional information
substrate specificity, the recombinant enzyme specifically hydrolyses beta-1,3-galactooligosacchrides, as an exo-beta-1,3-galactanase, with high activity for arabinogalactan-proteins from radish, hydrolyzing beta-1,3-galactan main chains, as well as beta-1,3-galactan. Products are beta-1,6-galactobiose, beta-1,6-galactotriose, alpha-arabinofuranosyl-1,3-galactosyl-beta-1,6-galatose with galactose from beta-1,3-galactans attached with and without beta-1,6-galatosyl branchesprepared from acacia gum, overview
707784
Irpex lacteus NBRC 5367
?
-
-
-
-
Subunits
Subunits
Commentary
Organism
?
x * 45520, mature enzyme, sequence calculation
Irpex lacteus
Synonyms
Synonyms
Commentary
Organism
exo-/beta-1,3-galactanase
-
Irpex lacteus
Il1,3Gal
-
Irpex lacteus
Temperature Optimum [°C]
Temperature Optimum [°C]
Temperature Optimum Maximum [°C]
Commentary
Organism
40
-
recombinant enzyme
Irpex lacteus
Temperature Range [°C]
Temperature Minimum [°C]
Temperature Maximum [°C]
Commentary
Organism
10
55
activity range, temperature profile, recombinant enzyme, overview
Irpex lacteus
pH Optimum
pH Optimum Minimum
pH Optimum Maximum
Commentary
Organism
4.5
-
recombinant enzyme
Irpex lacteus
pH Range
pH Minimum
pH Maximum
Commentary
Organism
3
6.5
activity range, pH profile, recombinant enzyme, overview
Irpex lacteus
Cloned(Commentary) (protein specific)
Commentary
Organism
DNA and amino acid sequence determination and analysis, expression of the gene encoding the enzyme fused to a yeast secretion signal sequence under control of the alcohol oxidase promoter in Pichia pastoris
Irpex lacteus
Molecular Weight [Da] (protein specific)
Molecular Weight [Da]
Molecular Weight Maximum [Da]
Commentary
Organism
45520
-
x * 45520, mature enzyme, sequence calculation
Irpex lacteus
Purification (Commentary) (protein specific)
Commentary
Organism
recombinant enzyme 0.7fold from Pichia pastoris cell culture medium by cation exchange chromatography and gel filtration
Irpex lacteus
Specific Activity [micromol/min/mg] (protein specific)
Specific Activity Minimum [µmol/min/mg]
Specific Activity Maximum [µmol/min/mg]
Commentary
Organism
47.6
-
purified recombinant enzyme
Irpex lacteus
Substrates and Products (Substrate) (protein specific)
Substrates
Commentary Substrates
Literature (Substrates)
Organism
Products
Commentary (Products)
Literature (Products)
Organism (Products)
Reversibility
ID
beta-1,3-galactan + H2O
best substrate, mode of action, overview
707784
Irpex lacteus
?
-
-
-
?
beta-1,3-galactan + H2O
best substrate, mode of action, overview
707784
Irpex lacteus NBRC 5367
?
-
-
-
?
additional information
substrate specificity, the recombinant enzyme specifically hydrolyses beta-1,3-galactooligosacchrides, as an exo-beta-1,3-galactanase, with high activity for arabinogalactan-proteins from radish, hydrolyzing beta-1,3-galactan main chains, as well as beta-1,3-galactan. Products are beta-1,6-galactobiose, beta-1,6-galactotriose, alpha-arabinofuranosyl-1,3-galactosyl-beta-1,6-galatose with galactose from beta-1,3-galactans attached with and without beta-1,6-galatosyl branchesprepared from acacia gum, overview
707784
Irpex lacteus
?
-
-
-
-
additional information
substrate specificity, the recombinant enzyme specifically hydrolyses beta-1,3-galactooligosacchrides, as an exo-beta-1,3-galactanase, with high activity for arabinogalactan-proteins from radish, hydrolyzing beta-1,3-galactan main chains, as well as beta-1,3-galactan. Products are beta-1,6-galactobiose, beta-1,6-galactotriose, alpha-arabinofuranosyl-1,3-galactosyl-beta-1,6-galatose with galactose from beta-1,3-galactans attached with and without beta-1,6-galatosyl branchesprepared from acacia gum, overview
707784
Irpex lacteus NBRC 5367
?
-
-
-
-
Subunits (protein specific)
Subunits
Commentary
Organism
?
x * 45520, mature enzyme, sequence calculation
Irpex lacteus
Temperature Optimum [°C] (protein specific)
Temperature Optimum [°C]
Temperature Optimum Maximum [°C]
Commentary
Organism
40
-
recombinant enzyme
Irpex lacteus
Temperature Range [°C] (protein specific)
Temperature Minimum [°C]
Temperature Maximum [°C]
Commentary
Organism
10
55
activity range, temperature profile, recombinant enzyme, overview
Irpex lacteus
pH Optimum (protein specific)
pH Optimum Minimum
pH Optimum Maximum
Commentary
Organism
4.5
-
recombinant enzyme
Irpex lacteus
pH Range (protein specific)
pH Minimum
pH Maximum
Commentary
Organism
3
6.5
activity range, pH profile, recombinant enzyme, overview
Irpex lacteus
Other publictions for EC
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
Synonyms
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)
752571
Fujita
Degradative enzymes for type ...
Bifidobacterium longum subsp. Longum
Appl. Microbiol. Biotechnol.
103
1299-1310
2019
-
-
1
-
-
-
-
-
-
-
-
-
-
3
-
-
1
-
-
-
-
-
6
1
6
1
-
-
-
1
-
-
-
-
-
-
-
-
1
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
1
-
-
-
-
6
1
1
-
-
-
1
-
-
-
-
3
3
-
-
-
752397
Godoy
Crystal structure of a putati ...
Bifidobacterium bifidum, Bifidobacterium bifidum NCIMB 41171, Bifidobacterium bifidum S17
Acta Crystallogr. Sect. F
72
288-293
2016
-
-
1
1
-
-
-
-
-
-
1
-
-
5
-
-
1
-
-
-
-
-
3
2
2
-
-
-
-
-
-
-
-
-
-
-
-
-
1
-
1
-
-
-
-
-
-
-
-
1
-
-
-
-
1
-
-
-
-
3
2
-
-
-
-
-
-
-
-
-
1
1
-
-
-
731184
Fujita
Bifidobacterium longum subsp. ...
Bifidobacterium longum, Bifidobacterium longum JCM 1217
Appl. Environ. Microbiol.
80
4577-4584
2014
-
-
1
-
1
-
-
1
-
-
1
-
-
6
-
-
-
-
-
-
9
-
14
-
2
1
-
-
-
1
-
-
-
-
-
-
-
-
1
-
-
1
-
-
-
-
1
-
-
1
-
-
-
-
-
-
-
9
-
14
-
1
-
-
-
1
-
-
-
1
2
2
1
-
-
731202
Okawa
Identification of an exo-beta- ...
Fusarium oxysporum 12S, Fusarium oxysporum
Appl. Microbiol. Biotechnol.
97
9685-9694
2013
-
-
1
-
-
-
-
-
-
-
-
-
-
5
-
-
1
-
-
-
1
-
12
1
2
1
-
-
-
1
-
-
-
-
-
-
-
-
1
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
1
-
-
1
-
12
1
1
-
-
-
1
-
-
-
-
1
1
-
-
-
731581
Ling
An exo-beta-(1->3)-D-galactana ...
Streptomyces sp. 19(2012), Streptomyces sp.
Carbohydr. Res.
352
70-81
2012
-
1
1
-
-
-
-
-
-
-
3
4
-
6
-
-
1
-
-
-
1
-
12
1
4
1
-
-
-
2
-
-
-
-
1
-
-
2
2
-
-
-
-
-
-
-
-
-
-
3
4
-
-
-
2
-
-
2
-
12
2
2
-
-
-
2
-
-
2
-
1
2
-
-
-
732396
Jiang
Crystal structure of 1,3Gal43A ...
Hungateiclostridium thermocellum
J. Struct. Biol.
180
447-457
2012
-
-
1
1
2
-
-
-
-
-
2
-
-
4
-
-
1
-
-
-
-
-
1
2
3
1
-
-
-
1
-
-
-
-
-
-
-
-
1
-
1
2
-
-
-
-
-
-
-
2
-
-
-
-
1
-
-
-
-
1
2
1
-
-
-
1
-
-
-
-
2
2
-
-
-
713904
Sakamoto
Characterization of an exo-bet ...
Sphingomonas sp., Sphingomonas sp. 24T
Appl. Microbiol. Biotechnol.
90
1701-1710
2011
1
-
-
-
-
-
-
-
-
-
1
-
-
3
-
-
1
-
-
1
2
-
12
1
2
1
-
1
-
1
-
1
-
-
-
-
1
-
-
-
-
-
-
-
-
-
-
-
-
1
-
-
-
-
1
-
1
2
-
12
1
1
-
1
-
1
-
1
-
-
-
-
-
-
-
703061
Ling
Preparation of a new chromogen ...
Irpex lacteus
Carbohydr. Res.
344
1941-1946
2009
-
-
-
-
-
-
-
-
-
-
-
-
-
1
-
-
-
-
-
1
1
-
1
-
2
1
-
-
-
1
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
1
1
-
1
-
1
-
-
-
1
-
-
-
-
-
-
-
-
-
706965
Ishida
Crystallization of selenomethi ...
Phanerochaete chrysosporium
Acta Crystallogr. Sect. F
65
1274-1276
2009
-
-
1
1
-
-
-
-
-
-
-
-
-
2
-
-
1
-
-
-
-
-
-
1
3
-
-
-
-
-
-
-
-
-
-
-
-
-
1
-
1
-
-
-
-
-
-
-
-
-
-
-
-
-
1
-
-
-
-
-
1
-
-
-
-
-
-
-
-
-
-
-
-
-
-
707784
Kotake
Molecular cloning and expressi ...
Irpex lacteus, Irpex lacteus NBRC 5367
Biosci. Biotechnol. Biochem.
73
2303-2309
2009
-
-
1
-
-
-
-
-
-
-
1
-
-
2
-
-
1
-
-
-
1
-
4
1
2
1
1
-
-
1
1
-
-
-
-
-
-
-
1
-
-
-
-
-
-
-
-
-
-
1
-
-
-
-
1
-
-
1
-
4
1
1
1
-
-
1
1
-
-
-
-
-
-
-
-
677662
Ichinose
Characterization of an exo-bet ...
Hungateiclostridium thermocellum
Appl. Environ. Microbiol.
72
3515-3523
2006
-
-
1
-
-
-
-
-
-
-
1
-
-
4
-
-
1
-
-
-
1
-
5
-
2
2
-
-
-
1
1
-
-
-
-
-
-
-
1
-
-
-
-
-
-
-
-
-
-
1
-
-
-
-
1
-
-
1
-
5
-
2
-
-
-
1
1
-
-
-
-
-
-
-
-
678786
Ichinose
Characterization of an exo-bet ...
Streptomyces avermitilis, Streptomyces avermitilis NBRC 14893
Biosci. Biotechnol. Biochem.
70
2745-2750
2006
-
-
1
-
-
-
-
-
-
-
1
-
-
4
-
1
1
-
-
-
1
-
10
-
2
1
-
-
-
1
-
-
-
-
-
-
-
-
1
-
-
-
-
-
-
-
-
-
-
1
-
-
-
1
1
-
-
1
-
10
-
1
-
-
-
1
-
-
-
-
-
-
-
-
-
666634
Kotake
Molecular cloning of a b-galac ...
Raphanus sativus
Plant Physiol.
138
1563-1576
2005
-
-
1
-
-
-
4
3
-
-
2
-
-
4
-
-
1
-
-
-
1
-
10
1
1
1
-
1
3
1
1
-
-
-
-
-
-
-
1
-
-
-
-
-
4
-
3
-
-
2
-
-
-
-
1
-
-
1
-
10
1
1
-
1
3
1
1
-
-
-
-
-
-
-
-
171335
Tsumuraya
Purification of an exo-beta-(1 ...
Irpex lacteus
J. Biol. Chem.
265
7207-7215
1990
-
-
-
-
-
-
-
2
-
-
2
1
-
1
-
-
1
-
-
-
1
-
4
1
-
-
1
1
-
1
-
1
-
-
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-
-
-
-
-
-
-
-
-
2
-
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2
1
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1
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1
-
4
1
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1
1
-
1
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1
-
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-
-
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