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Information on EC 3.2.1.2 - beta-amylase and Organism(s) Glycine max and UniProt Accession P10538
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3.2.1.2 beta-amylaseIUBMB Comments
Acts on starch, glycogen and related polysaccharides and oligosaccharides producing beta-maltose by an inversion. The term 'beta'' relates to the initial anomeric configuration of the free sugar group released and not to the configuration of the linkage hydrolysed.
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Word Map
- 3.2.1.2
- starch
- alpha-amylase
- maltose
- barley
- potato
- soybean
-
sweet
- amylopectin
-
amylolytic
- glucoamylase
- endosperm
- hordeum
- amylases
- pullulanase
-
debranching
- dextrin
- nutrition
- maltotetraose
- thermosulfurogenes
- isoamylase
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beta-limit
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starch-degrading
- amyloglucosidase
- polymyxa
- maltotriose
- maltopentaose
-
granule-bound
- alpha-cyclodextrin
-
extrachloroplastic
- industry
-
sporamin
- molecular biology
- brewing
The taxonomic range for the selected organisms is: Glycine max
The expected taxonomic range for this enzyme is: Eukaryota, Bacteria, Archaea
The expected taxonomic range for this enzyme is: Eukaryota, Bacteria, Archaea
Reaction Schemes
Synonyms
beta-amylase, arath, spoii, tr-bamy, beta amylase, ct-bmy, bam-2, beta-amylase 1, bam-8, glycogenase, 
more
topSYNONYM 
ORGANISM
UNIPROT
COMMENTARY 
LITERATURE
SBA
(1-4)-alpha-D-glucan maltohydrolase
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-
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1,4-alpha-D-glucan maltohydrolase
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amylase, beta-
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-
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beta amylase
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-
-
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glycogenase
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-
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saccharogen amylase
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saccharogenamylase
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-
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REACTION
REACTION DIAGRAM
COMMENTARY
ORGANISM
UNIPROT
LITERATURE
Hydrolysis of (1->4)-alpha-D-glucosidic linkages in polysaccharides so as to remove successive maltose units from the non-reducing ends of the chains
Hydrolysis of (1->4)-alpha-D-glucosidic linkages in polysaccharides so as to remove successive maltose units from the non-reducing ends of the chains
roles of Glu186 and Glu380 as general acid and general base catalyst in the catalytic reaction, reaction mechanism involving residue T342
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Hydrolysis of (1->4)-alpha-D-glucosidic linkages in polysaccharides so as to remove successive maltose units from the non-reducing ends of the chains
active site structure, carbohydrate binding subsites, role of a conformational change of the inner loop in the catalytic mechanism, T342 is involved, overview
Hydrolysis of (1->4)-alpha-D-glucosidic linkages in polysaccharides so as to remove successive maltose units from the non-reducing ends of the chains
roles of Glu186 and Glu380 as general acid and general base catalyst in the catalytic reaction, substrate binding and reaction mechanism
PATHWAY SOURCE
PATHWAYS
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-, -
SYSTEMATIC NAME
IUBMB Comments
4-alpha-D-glucan maltohydrolase
Acts on starch, glycogen and related polysaccharides and oligosaccharides producing beta-maltose by an inversion. The term 'beta'' relates to the initial anomeric configuration of the free sugar group released and not to the configuration of the linkage hydrolysed.
CAS REGISTRY NUMBER
COMMENTARY
9000-91-3
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SUBSTRATE
PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate)
(Substrate)
LITERATURE
(Substrate)
(Substrate)
COMMENTARY
(Product)
(Product)
LITERATURE
(Product)
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
amylopectin + H2O
?
from potato, active site structure, Glu-186 and Glu-380 play important roles as general acid and base catalyst
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-
?
maltoheptaose + H2O
maltose + D-glucose + ?
the exo-type enzyme can catalyze the successive liberation of beta-maltose from the nonreducing ends of alpha-1,4-linked glucopyranosyl polymers. A phenomenon called multiple or repetitive attack is observed where the enzyme releases several maltose molecules in a single enzyme-substrate complex. The multiple attack action needs the force of enzyme sliding on the substrate. In addition, it is important for the multiple attack that the enzyme and substrate have the characteristics of a stable productive substrate-enzyme complex through a hydrogen bond between the nonreducing end of the substrate and the carboxyl residue of the enzyme
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-
?
maltopentaose + H2O
2 maltose + D-glucose
substrate/product binding structure, sugar subsite conformations, overview
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-
?
starch + H2O
?
active site structure, Glu-186 and Glu-380 play important roles as general acid and base catalyst, catalyzes the liberation of beta-anomeric maltose from the non-reducing ends
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?
starch + H2O
?
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beta-amylase hydrolyzes alpha-1,4-linkage, raw starch granules from potato, wheat, rice and corn, with the granules from rice being the best substrate, no efficient hydrolysis of raw starch granules, very slow enzymic attack
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?
additional information
?
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soybean trypsin inhibitor and beta-amylase induce rat alveolar macrophages to release nitrogen oxides
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-
?
NATURAL SUBSTRATE
NATURAL PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate)
(Substrate)
LITERATURE
(Substrate)
(Substrate)
COMMENTARY
(Product)
(Product)
LITERATURE
(Product)
(Product)
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
beta-amylase-inhibitor
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several strains of Streptomyces produce a beta-amylase inhibitor when grown on a medium containing starch and deoxynojirimycin
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KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
additional information
additional information
kinetic parameters for wild-type and mutant SBA
-
additional information
additional information
-
kinetic parameters for wild-type and mutant SBA
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additional information
additional information
-
Km: 2.25 mg/ml for amylopectin for isoenzyme 2, Km: 1.65 mg/ml for amylopectin, isoenzyme 6
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TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
additional information
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
5.4
5.4
hydrolysis of potato amylopectin, at 37°C, the reduced pKa-value of Glu-380 is stabilized by the hydrogen bond network and is responsible for the lower pH-optimum of soybean beta-amylase compared with that of Bacillus cereus, pH 6.7
pH RANGE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
3 - 8
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pH 3.0: about 35% of maximal activity, pH 8.0: about 70% of maximal activity
TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
37
TEMPERATURE RANGE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
45
-
at 45°C beta-amylase is 60% less active in hydrolysis of corn starch granules than enzyme from Bacillus cereus
ORGANISM
COMMENTARY
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
SOURCE
LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY
GeneOntology No.
LITERATURE
SOURCE
UNIPROT
ENTRY NAME
ORGANISM
NO. OF AA
NO. OF TRANSM. HELICES
MOLECULAR WEIGHT[Da]
SOURCE
SEQUENCE
LOCALIZATION PREDICTION
The reliability class of the localization prediction ranges from 1 (very reliable) to 5 (not reliable).
The reliability class of the localization prediction ranges from 1 (very reliable) to 5 (not reliable). AMYB_SOYBN
496
0
56143
Swiss-Prot
Secretory Pathway (Reliability: 3)
PDB
SCOP
CATH
UNIPROT
ORGANISM
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
57000
SUBUNIT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
additional information
additional information
structure analysis, intramolecular hydrogen bond interactions
additional information
-
structure analysis, intramolecular hydrogen bond interactions
POSTTRANSLATIONAL MODIFICATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
CRYSTALLIZATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
purified recombinant mutant enzymes, mutant enzyme E186Q in complex with substrate maltopentaose, and mutant enzyme E380Q in complex with product maltose, hanging drop vapour diffusion method, 20 mg/ml protein in 45-50% w/v ammonium sulfate, 0.1 M sodium acetate, pH 5.4, 1 mM EDTA, and 18 mM 2-methyl-2,4-pentanediol, equilibration against 1 ml mother liquor, 4°C, soaking of crystals in 30 mM ligand solution, cryoprotection of crystals with 30% v/v glycerol in crystallization solution, X-ray diffraction structure determination and analysis at 1.6 and 1.9 A resolution, respectively, active site structure modelling
purified recombinant T342 mutant enzymes, hanging drop vapour diffusion method, 0.005 ml of 10 mg/ml protein solution is mixed with 0.005 ml of reservoir solution containing 40-50% w/v ammonium sulfate, 1 mM EDTA, 18 mM 2-methyl-2,4-pentanediol, and 0.1 M sodium acetate, pH 5.4, equilibration against 1 ml of reservoir solution, 4°C, gradual soaking of crystals in 0.1 M sodium acetate, pH 6.1, 50% w/v ammonium sulfate, 1 mM EDTA, 20 mM DTT, 0.3 M maltose, and 30% v/v glycerol, X-ray diffraction structure determination and analysis at 1.12-1.6 A resolution, active site structure modelling
wild-type, M51T, E178Y and N340T mutant SBA, complexed with maltose, hanging-drop vapor diffusion method, X-ray analysis
high-resolution crystal structure for catalytic active enzyme and for the enzyme complexes with either beta-maltose or maltal
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PROTEIN VARIANTS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
D53A
mutant enzyme shows 13% of the wild-type activity towards maltoheptaose
E178Y
kinetic data, 43% of specific activity of wild-type SBA, the pH-optimum of mutant enzyme is shifted to pH 6, the hydrogen bond between Glu-380 and Asn-340 is completely disrupted, mutant SBA structure
E186Q
site-directed mutagenesis, mutation of catalytic residue, the mutant shows 16000fold decreased activity compared to the wild-type enzyme
E380Q
site-directed mutagenesis, mutation of catalytic residue, the mutant shows 37000fold decreased activity compared to the wild-type enzyme
M51T
kinetic data, 11% of specific activity of wild-type SBA, the pH-optimum of mutant enzyme is shifted to pH 6.5, the hydrogen bonds between Glu-380 and Asn-340 and between Glu-380 and Lys-295 are completely disrupted, mutant SBA structure
N340T
kinetic data, 32% of specific activity of wild-type SBA, the pH-optimum of mutant enzyme is shifted to pH 6.6, the hydrogen bond between Glu-380 and Asn-340 is completely disrupted, mutant SBA structure
T342A
site-directed mutagenesis, structural analysis of mutant active site conformation
T342S
site-directed mutagenesis, structural analysis of mutant active site conformation
T342V
site-directed mutagenesis, structural analysis of mutant active site conformation
W55R
mutant enzyme shows 20% of the wild-type activity towards maltoheptaose
pH STABILITY
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
TEMPERATURE STABILITY
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
60
-
pH 5.4, 90 min, 38% loss of activity of isoenzyme 2, 55% loss of activity of isoenzyme 6
GENERAL STABILITY
ORGANISM
UNIPROT
LITERATURE
guanidine hydrochloride, 6 M, complete disorganization of the secondary structure
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SDS, effective in disturbing the tertiary structure, no effect on secondary structure
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PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
recombinant wild-type and mutant enzymes from Escherichia coli strain JM105
CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
expression of wild-type and mutant enzymes in Escherichia coli strain JM105
expression of wild-type and mutants in Escherichia coli strains JM109 and JM105
REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Wang, Y.; Arahira, M.; Fukazawa, C.
An Isoelectric Separation of Soybean ?-Amylase Isoforms and Their Enzymic Characteristics.
Biosci. Biotechnol. Biochem.
63
726-730
1999
Glycine max
French, D.
beta-Amylases
The Enzymes, 2nd Ed (Boyer, P. D. , Lardy, H. , Myrbck, K. , eds. )
4
345-368
1960
Glycine max, Hordeum vulgare, Ipomoea batatas, Secale cereale, Triticum aestivum
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Ren, H.; Madison, J.T.; Thompson, J.F.
Identification of an ethanol-soluble protein as beta-amylase and its purification from soybean seeds
Phytochemistry
33
535-539
1993
Glycine max
Arai, M.; Sumida, M.; Nakatani, S.; Murao, S.
A novel beta-amylase inhibitor
Agric. Biol. Chem.
47
183-185
1983
Niallia circulans, Priestia megaterium, Glycine max, Hordeum vulgare, Ipomoea batatas
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Mikami, B.; Aibara, S.; Morita, Y.
Distribution and properties of soybean beta-amylase isoenzymes
Agric. Biol. Chem.
46
943-953
1982
Glycine max
-
Mori, E.; Mikami, B.; Morita, Y.; Jirgensons, B.
Circular dichroism and the conformational properties of soybean beta-amylase
Arch. Biochem. Biophys.
211
382-389
1981
Glycine max
Morita, Y.; Yagi, F.; Aibara, S.; Yamashita, H.
Chemical composition and properties of soybean beta-amylase
J. Biochem.
79
591-603
1976
Glycine max
Mikami, B.; Degano, M.; Hehre, E.J.; Sacchettini, J.C.
Crystal structures of soybean beta-amylase reacted with beta-maltose and maltal: active site components and their apparent roles in catalysis
Biochemistry
33
7779-7787
1994
Glycine max
Yoshigi, N.; Okada, Y.; Maeba, H.; Sahara, H.; Tamaki, T.
Construction of a plasmid used for the expression of a sevenfold-mutant barley beta-amylase with increased thermostability in Escherichia coli and properties of the sevenfold-mutant beta-amylase
J. Biochem.
118
562-567
1995
Glycine max, Hordeum vulgare
Jorens, P.G.; van Overveld, F.J.; Bult, H.; Vermeire, P.A.; Herman, A.G.
Soybean trypsin inhibitor and beta-amylase induce alveolar macrophages to release nitrogen oxides
Biochem. Pharmacol.
44
387-390
1992
Glycine max
Hirata, A.; Adachi, M.; Sekine, A.; Kang, Y.N.; Utsumi, S.; Mikami, B.
Structural and enzymatic analysis of soybean beta-amylase mutants with increased pH optimum
J. Biol. Chem.
279
7287-7295
2004
Glycine max (P10538), Glycine max
Sarikaya, E.; Higasa, T.; Adachi, M.; Mikami, B.
Comparison of degradation abilities of alpha- and beta-amylases on raw starch granules
Process Biochem.
35
711-715
2000
Bacillus cereus, Glycine max
-
Kang, Y.N.; Tanabe, A.; Adachi, M.; Utsumi, S.; Mikami, B.
Structural analysis of threonine 342 mutants of soybean beta-amylase: role of a conformational change of the inner loop in the catalytic mechanism
Biochemistry
44
5106-5116
2005
Glycine max (P10538), Glycine max
Kang, Y.N.; Adachi, M.; Utsumi, S.; Mikami, B.
The roles of Glu186 and Glu380 in the catalytic reaction of soybean beta-amylase
J. Mol. Biol.
339
1129-1140
2004
Glycine max (P10538), Glycine max
Kaplan, F.; Sung, D.Y.; Guy, C.L.
Roles of beta-amylase and starch breakdown during temperature stress
Physiol. Plant.
126
120-128
2006
Arabidopsis thaliana, Glycine max, Hordeum vulgare, Solanum tuberosum
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