BRENDA - Enzyme Database
show all sequences of 3.2.1.68

Studies on the inhibition and molecular properties of crystalline Pseudomonas isoamylase

Kitagawa, H.; Amemura, A.; Harada, T.; Agric. Biol. Chem. 39, 989-994 (1975)
No PubMed abstract available

Data extracted from this reference:

Crystallization (Commentary)
Crystallization
Organism
-
Pseudomonas amyloderamosa
Inhibitors
Inhibitors
Commentary
Organism
Structure
2,4-dinitrofluorobenzene
-
Pseudomonas amyloderamosa
2-Hydroxy-5-nitrobenzyl bromide
-
Pseudomonas amyloderamosa
Ag2+
-
Pseudomonas amyloderamosa
amylose
-
Pseudomonas amyloderamosa
cellobiose
10 mM, 0.4% amylose, relative activity 88%
Pseudomonas amyloderamosa
corn amylose
-
Pseudomonas amyloderamosa
Cu2+
relative activity 78%
Pseudomonas amyloderamosa
cyclomaltoheptaose
10 mM, 0.4% amylose, relative activity 93%
Pseudomonas amyloderamosa
D-glucono-delta-lactone
relative activity 87%
Pseudomonas amyloderamosa
D-glucose
10 mM, 0.4% amylose, relative activity 95%
Pseudomonas amyloderamosa
guanidine hydrochloride
3 M, activity completely lost
Pseudomonas amyloderamosa
Hg2+
-
Pseudomonas amyloderamosa
Iodine
relative activity 93%
Pseudomonas amyloderamosa
iodoacetate
-
Pseudomonas amyloderamosa
isomaltose
10 mM, 0.4% amylose, relative activity 82%
Pseudomonas amyloderamosa
maltose
10 mM, inhibition slightly, with 0.4% amylose relative activity 90%
Pseudomonas amyloderamosa
maltotetraose
10 mM, 0.4% amylose, relative activity 50%
Pseudomonas amyloderamosa
maltotriose
10 mM, 0.4% amylose, relative activity 53%
Pseudomonas amyloderamosa
N-bromosuccinimide
-
Pseudomonas amyloderamosa
oligosaccharides with alpha-1,4-glucosidic linkages
-
Pseudomonas amyloderamosa
Phenylmercuriacetate
-
Pseudomonas amyloderamosa
SDS
0,1%, activity completely lost
Pseudomonas amyloderamosa
Succinic anhydride
relative activity 94%
Pseudomonas amyloderamosa
Urea
20% activity retained
Pseudomonas amyloderamosa
xylose
10 mM, 0.4% amylose, relative activity 97%
Pseudomonas amyloderamosa
Molecular Weight [Da]
Molecular Weight [Da]
Molecular Weight Maximum [Da]
Commentary
Organism
46000
-
2 * 46000, sedimentation equilibrium
Pseudomonas amyloderamosa
50000
-
2 subunits, not linked covalently
Pseudomonas amyloderamosa
94000
-
native enzyme, centrifugation analysis; sedimentation equilibrium
Pseudomonas amyloderamosa
Natural Substrates/ Products (Substrates)
Natural Substrates
Organism
Commentary (Nat. Sub.)
Natural Products
Commentary (Nat. Pro.)
Organism (Nat. Pro.)
Reversibility
starch + H2O
Pseudomonas amyloderamosa
-
?
-
-
?
Organism
Organism
Primary Accession No. (UniProt)
Commentary
Textmining
Pseudomonas amyloderamosa
-
-
-
Substrates and Products (Substrate)
Substrates
Commentary Substrates
Literature (Substrates)
Organism
Products
Commentary (Products)
Literature (Products)
Organism (Products)
Reversibility
amylopectin + H2O
or the beta-limit dextrins, cleaves the branching points completely in vitro
136804
Pseudomonas amyloderamosa
maltose + maltooligosaccharides
-
136804
Pseudomonas amyloderamosa
?
glycogen + H2O
cleaves the branching points completely in vitro
136804
Pseudomonas amyloderamosa
maltose + maltooligosaccharides
-
136804
Pseudomonas amyloderamosa
?
glycogen + H2O
or the beta-limit dextrins
136804
Pseudomonas amyloderamosa
maltose + maltooligosaccharides
-
136804
Pseudomonas amyloderamosa
?
starch + H2O
-
136804
Pseudomonas amyloderamosa
?
-
-
-
?
Subunits
Subunits
Commentary
Organism
dimer
2 * 46000, sedimentation equilibrium; 2 * 50000, not linked covalently
Pseudomonas amyloderamosa
Crystallization (Commentary) (protein specific)
Crystallization
Organism
-
Pseudomonas amyloderamosa
Inhibitors (protein specific)
Inhibitors
Commentary
Organism
Structure
2,4-dinitrofluorobenzene
-
Pseudomonas amyloderamosa
2-Hydroxy-5-nitrobenzyl bromide
-
Pseudomonas amyloderamosa
Ag2+
-
Pseudomonas amyloderamosa
amylose
-
Pseudomonas amyloderamosa
cellobiose
10 mM, 0.4% amylose, relative activity 88%
Pseudomonas amyloderamosa
corn amylose
-
Pseudomonas amyloderamosa
Cu2+
relative activity 78%
Pseudomonas amyloderamosa
cyclomaltoheptaose
10 mM, 0.4% amylose, relative activity 93%
Pseudomonas amyloderamosa
D-glucono-delta-lactone
relative activity 87%
Pseudomonas amyloderamosa
D-glucose
10 mM, 0.4% amylose, relative activity 95%
Pseudomonas amyloderamosa
guanidine hydrochloride
3 M, activity completely lost
Pseudomonas amyloderamosa
Hg2+
-
Pseudomonas amyloderamosa
Iodine
relative activity 93%
Pseudomonas amyloderamosa
iodoacetate
-
Pseudomonas amyloderamosa
isomaltose
10 mM, 0.4% amylose, relative activity 82%
Pseudomonas amyloderamosa
maltose
10 mM, inhibition slightly, with 0.4% amylose relative activity 90%
Pseudomonas amyloderamosa
maltotetraose
10 mM, 0.4% amylose, relative activity 50%
Pseudomonas amyloderamosa
maltotriose
10 mM, 0.4% amylose, relative activity 53%
Pseudomonas amyloderamosa
N-bromosuccinimide
-
Pseudomonas amyloderamosa
oligosaccharides with alpha-1,4-glucosidic linkages
-
Pseudomonas amyloderamosa
Phenylmercuriacetate
-
Pseudomonas amyloderamosa
SDS
0,1%, activity completely lost
Pseudomonas amyloderamosa
Succinic anhydride
relative activity 94%
Pseudomonas amyloderamosa
Urea
20% activity retained
Pseudomonas amyloderamosa
xylose
10 mM, 0.4% amylose, relative activity 97%
Pseudomonas amyloderamosa
Molecular Weight [Da] (protein specific)
Molecular Weight [Da]
Molecular Weight Maximum [Da]
Commentary
Organism
46000
-
2 * 46000, sedimentation equilibrium
Pseudomonas amyloderamosa
50000
-
2 subunits, not linked covalently
Pseudomonas amyloderamosa
94000
-
native enzyme, centrifugation analysis; sedimentation equilibrium
Pseudomonas amyloderamosa
Natural Substrates/ Products (Substrates) (protein specific)
Natural Substrates
Organism
Commentary (Nat. Sub.)
Natural Products
Commentary (Nat. Pro.)
Organism (Nat. Pro.)
Reversibility
starch + H2O
Pseudomonas amyloderamosa
-
?
-
-
?
Substrates and Products (Substrate) (protein specific)
Substrates
Commentary Substrates
Literature (Substrates)
Organism
Products
Commentary (Products)
Literature (Products)
Organism (Products)
Reversibility
amylopectin + H2O
or the beta-limit dextrins, cleaves the branching points completely in vitro
136804
Pseudomonas amyloderamosa
maltose + maltooligosaccharides
-
136804
Pseudomonas amyloderamosa
?
glycogen + H2O
cleaves the branching points completely in vitro
136804
Pseudomonas amyloderamosa
maltose + maltooligosaccharides
-
136804
Pseudomonas amyloderamosa
?
glycogen + H2O
or the beta-limit dextrins
136804
Pseudomonas amyloderamosa
maltose + maltooligosaccharides
-
136804
Pseudomonas amyloderamosa
?
starch + H2O
-
136804
Pseudomonas amyloderamosa
?
-
-
-
?
Subunits (protein specific)
Subunits
Commentary
Organism
dimer
2 * 46000, sedimentation equilibrium; 2 * 50000, not linked covalently
Pseudomonas amyloderamosa
Other publictions for EC 3.2.1.68
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)
752159
Shufen
-
Editing of rice isoamylase ge ...
Oryza sativa Japonica Group
Rice Sci.
26
77-87
2019
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1
1
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750238
Li
Investigation of debranching ...
Bacillus lentus
Carbohydr. Res.
446-447
93-100
2017
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1
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1
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1
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1
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8
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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8
1
1
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1
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749623
Ran
Enhanced production of recomb ...
Thermobifida fusca
Appl. Biochem. Biotechnol.
180
464-476
2016
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1
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3
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4
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1
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4
1
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750830
Hu
The optimization of isoamylas ...
Pseudomonas sp.
Int. J. Biol. Macromol.
86
105-111
2016
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2
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1
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1
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1
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751254
Li
Engineering of isoamylase imp ...
Bacillus lentus, Bacillus lentus JNU3
J. Ind. Microbiol. Biotechnol.
43
3-12
2016
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1
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9
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4
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1
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1
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2
1
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1
10
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1
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1
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9
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1
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1
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2
1
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1
10
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1
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751833
Nabemoto
-
Molecular characterization of ...
Ipomoea batatas
Plant Biotechnol.
33
351-359
2016
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1
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1
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1
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751948
Kobayashi
Comparison of chain-length pr ...
Cyanothece sp. ATCC 51142, Escherichia coli, Oryza sativa, Pseudomonas amyloderamosa, Synechococcus elongatus, Synechococcus elongatus PCC7942
PLoS ONE
11
e0157020
2016
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5
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15
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5
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1
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19
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5
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5
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1
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19
-
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731578
Xu
Cycloamylose production from a ...
Pseudomonas sp.
Carbohydr. Polym.
102
66-73
2014
-
1
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3
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1
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732146
Sim
Crystal structure of the Chlam ...
Chlamydomonas reinhardtii, Chlamydomonas reinhardtii 330
J. Biol. Chem.
289
22991-23003
2014
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1
1
1
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6
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1
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10
1
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2
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4
8
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732490
Park
Molecular characterization of ...
Amaranthus hybridus subsp. cruentus
Mol. Biol. Rep.
41
7857-7864
2014
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1
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1
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7
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732278
Li
Purification, characterization ...
Bacillus sp. (in: Bacteria), Bacillus sp. (in: Bacteria) CICIM 304
J. Ind. Microbiol. Biotechnol.
40
437-446
2013
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1
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9
1
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4
2
2
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4
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12
1
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2
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12
1
1
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2
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1
1
1
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2
2
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732581
Lin
Function of isoamylase-type st ...
Zea mays
New Phytol.
200
1009-1021
2013
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1
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1
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1
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2
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4
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2
2
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2
3
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732655
Facon
Distinct functional properties ...
Arabidopsis thaliana, Arabidopsis thaliana Col-0, Zea mays
Plant Physiol.
163
1363-1375
2013
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2
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1
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2
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2
9
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6
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2
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9
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6
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10
2
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3
5
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732750
Sundberg
The heteromultimeric debranchi ...
Arabidopsis thaliana
PLoS ONE
8
e75223
2013
-
1
1
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1
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4
1
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5
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1
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1
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1
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1
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3
3
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713710
Ray
-
Microbial isoamylases: An over ...
Myroides odoratus, Pseudomonas amyloderamosa, Pseudomonas amyloderamosa SB-15
Am. J. Food Technol.
6
1-18
2011
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4
2
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1
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3
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2
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15
2
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2
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15
2
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716495
Yun
Rice debranching enzyme isoamy ...
Oryza sativa
Plant Cell Physiol.
52
1068-1082
2011
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1
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2
2
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716622
Utsumi
Functional diversity of isoamy ...
Oryza sativa
Plant Physiol.
156
61-77
2011
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1
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1
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5
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1
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1
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1
1
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707760
Wang
Deactivation of isoamylase and ...
Pseudomonas amyloderamosa, Pseudomonas amyloderamosa WU7211-2
Bioprocess Biosyst. Eng.
33
1007-1015
2010
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1
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2
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1
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1
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716600
Kubo
Functions of heteromeric and h ...
Zea mays
Plant Physiol.
153
956-969
2010
-
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1
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Biochemical characterization o ...
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Cloning and nucleotide sequenc ...
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Fujita
Purification, characterization ...
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Three-dimensional structure of ...
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Ito
Alkaline detergent enzymes fro ...
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Extremophiles
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Rahman
Characterization of SU1 isoamy ...
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An isoamylase with neutral pH ...
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Clave
Amylase, lipase, pancreatic is ...
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1
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4
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136810
Lin
-
Improved elution of isoamylase ...
Pseudomonas amyloderamosa, Pseudomonas amyloderamosa WU-5315
Lett. Appl. Microbiol.
19
383-385
1994
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1
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1
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136809
Ara
-
Purification and characterizat ...
Bacillus sp. (in: Bacteria), Pseudomonas amyloderamosa, Pseudomonas amyloderamosa SMP1
J. Gen. Microbiol.
139
781-786
1993
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3
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4
1
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1
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4
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1
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1
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10
2
1
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1
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1
1
1
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3
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4
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1
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1
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1
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1
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10
2
1
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1
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1
1
1
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136807
Fujita
-
Characterization of an isoamyl ...
Pseudomonas amyloderamosa, Pseudomonas amyloderamosa MI-414
Agric. Biol. Chem.
54
2315-2321
1990
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2
1
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2
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1
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1
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1
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1
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2
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136799
Amemura
Cloning and nucleotide sequenc ...
Pseudomonas amyloderamosa
J. Biol. Chem.
263
9271-9275
1988
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2
1
1
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1
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2
1
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5
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7
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1
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1
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7
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136800
Ishizaki
-
Debranching enzymes of potato ...
Solanum tuberosum
Agric. Biol. Chem.
47
771-779
1983
1
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1
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4
1
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1
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1
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4
1
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1
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1
1
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10
1
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1
2
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1
1
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136801
Spencer-Martins
Extracellular isoamylase produ ...
Lipomyces kononenkoae
Appl. Environ. Microbiol.
44
1253-1257
1982
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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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4
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1
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1
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9
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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
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1
1
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1
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1
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9
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1
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1
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136802
Amemura
Molecular weight of the undegr ...
Pseudomonas amyloderamosa
Biochim. Biophys. Acta
611
390-393
1980
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1
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6
1
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2
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4
2
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1
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6
1
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4
2
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136803
Kato
-
Affinity chromatography of Pse ...
Pseudomonas amyloderamosa
Agric. Biol. Chem.
41
2077-2080
1977
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2
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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
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1
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1
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4
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1
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2
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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
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1
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4
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1
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136804
Kitagawa
-
Studies on the inhibition and ...
Pseudomonas amyloderamosa
Agric. Biol. Chem.
39
989-994
1975
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1
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25
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3
1
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1
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4
1
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1
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25
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3
1
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4
1
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136805
Lee
-
Glycogen and starch debranchin ...
Cytophaga sp., Pseudomonas amyloderamosa
The Enzymes, 3rd Ed. (Boyer, P. D. , ed. )
5
191-234
1972
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2
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2
1
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2
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8
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2
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2
1
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8
-
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136806
Yokobayashi
Purification and properties of ...
Pseudomonas amyloderamosa
Biochim. Biophys. Acta
212
458-469
1970
-
-
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5
-
1
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2
1
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2
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1
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1
1
6
-
1
1
3
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1
2
1
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5
-
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1
-
2
1
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1
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1
1
6
-
1
1
3
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1
2
1
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-