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Information on EC 3.2.1.2 - beta-amylase and Organism(s) Hordeum vulgare and UniProt Accession P16098
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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
-
beta-limit
-
starch-degrading
- amyloglucosidase
- polymyxa
- maltotriose
- maltopentaose
-
granule-bound
- alpha-cyclodextrin
-
extrachloroplastic
- industry
-
sporamin
- molecular biology
- brewing
The taxonomic range for the selected organisms is: Hordeum vulgare
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, glycogenase, bam-8, 
more
topSYNONYM 
ORGANISM
UNIPROT
COMMENTARY 
LITERATURE
(1-4)-alpha-D-glucan maltohydrolase
-
-
-
-
1,4-alpha-D-glucan maltohydrolase
-
-
-
-
amylase, beta-
-
-
-
-
beta amylase
-
-
-
-
Bmy1
glycogenase
-
-
-
-
saccharogen amylase
-
-
-
-
saccharogenamylase
-
-
-
-
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
catalytic mechanism
-
PATHWAY SOURCE
PATHWAYS
-
-, -
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
-
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
p-nitrophenylmaltopentaoside + H2O
?
catalyzes the release of maltose
-
-
?
starch + H2O
?
from potato, catalyzes the release of maltose from the non-reducing ends of starch, three-dimensional structure of Sd2L
-
-
?
p-nitrophenylmaltopentaoside + H2O
?
-
catalyzes the release of maltose
-
-
?
starch + H2O
?
-
catalyzes the release of maltose from soluble starch, three-dimensional structures of Sd2L and V233A mutant of Sd1
-
-
?
starch + H2O
maltose + ?
-
soluble starch, depolymerization, reaction scheme
-
-
?
additional information
?
-
-
germination markedly increases the beta-amylase
-
-
?
additional information
?
-
-
beta-amylase is an exo-enzyme that specifically binds to a double (1-4-alpha-D-glucopyranosyl-1-4-alpha-D-glucopyranosyl-) unit from the non-reducing ends of polymaltosidic polysaccharides, and sequentially cleaves glucose disaccharidic units until it encounters any structural variation, producing maltose as sole hydrolysis product
-
-
?
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
additional information
?
-
-
germination markedly increases the beta-amylase
-
-
?
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
beta-amylase-inhibitor
-
several strains of Streptomyces produce a beta-amylase inhibitor when grown on a medium containing starch and deoxynojirimycin
-
Ag+
-
1 mM, almost complete inhibition of mutant enzyme M185L/S295A/I297V/S350P/S351P/Q352D/A376S
Cd2+
-
1 mM, almost complete inhibition of barley enzyme and recombinant enzyme, less inhibitory towards mutant enzyme M185L/S295A/I297V/S350P/S351P/Q352D/A376S
Cu2+
-
1 mM, almost complete inhibition of mutant enzyme M185L/S295A/I297V/S350P/S351P/Q352D/A376S
Hg2+
-
1 mM, almost complete inhibition of mutant enzyme M185L/S295A/I297V/S350P/S351P/Q352D/A376S
PCMB
-
0.1 mM, complete inhibition of mutant enzyme M185L/S295A/I297V/S350P/S351P/Q352D/A376S
Zn2+
-
1 mM, almost complete inhibition of barley enzyme and recombinant enzyme, less inhibitory towards mutant enzyme M185L/S295A/I297V/S350P/S351P/Q352D/A376S
ACTIVATING COMPOUND
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
polyethylene glycol 1000
-
1500 Da PEG, increases the enzyme activity by 60% at 0.02% w/v
polyethylene glycol 1500
-
1500 Da PEG, increases the enzyme activity by 77% at 0.02% w/v
-
polyethylene glycol 2000
-
1500 Da PEG, increases the enzyme activity by 58% at 0.02% w/v
polyethylene glycol 400
-
1500 Da PEG, increases the enzyme activity by 7% at 0.02% w/v
-
polyethylene glycol 4600
-
1500 Da PEG, increases the enzyme activity by 74% at 0.02% w/v
polyethylene glycol 600
-
1500 Da PEG, increases the enzyme activity by 19% at 0.02% w/v
polyethylene glycol 8000
-
1500 Da PEG, increases the enzyme activity by 68% at 0.02% w/v
polyvinyl alcohol
-
10 kDa: increases the enzyme activity by 36% at 0.02% w/v, 50 kDa: increases the enzyme activity by 21% at 0.02% w/v
KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
0.491
amylose
-
DP = 17, mutant enzyme M185L/S295A/I297V/S350P/S351P/Q352D/A376S
0.0083
starch
-
pH 5, 40°C, soluble starch, wild-type Sd2H and V233A/L347S double mutant of Sd2L
additional information
additional information
beta-amylase from germinated barley has a higher substrate binding affinity for starch than enzyme from mature grain, removal of the four C-terminal glycine-rich repeats enhances the substrate binding affinity, kinetic parameters for several deletion mutants
-
additional information
additional information
-
beta-amylase from germinated barley has a higher substrate binding affinity for starch than enzyme from mature grain, removal of the four C-terminal glycine-rich repeats enhances the substrate binding affinity, kinetic parameters for several deletion mutants
-
additional information
additional information
-
the 3 allelic forms of beta-amylase Sd1, Sd2H and Sd2L exhibit different kinetic properties, an R115C mutation is responsible for this difference
-
additional information
additional information
-
kinetics, isothermal titration microcalorimetric method
-
TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
308
starch
-
pH 5, 40°C, soluble starch, wild-type Sd2H and V233A/L347S double mutant of Sd2L
additional information
additional information
kinetic parameters for several deletion mutants
-
additional information
additional information
-
kinetic parameters for several deletion mutants
-
Ki VALUE [mM]
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
additional information
-
catalytic activity of the enzyme at different pressure/temperature conditions, up to 700 mPa, 20-70°C, overview
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
55
TEMPERATURE RANGE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
20 - 70
-
at different pressure/temperature conditions, up to 700 mPa, overview
pI VALUE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
4.8 - 6
-
isoelectric focusing analysis of isozyme pI of different cultivars, overview
ORGANISM
COMMENTARY
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
SOURCE
additional information
-
BMY is stored in seeds bound to starchy endosperm possibly through S-S bridges, during germination the enzyme is released by proteolytic cleavage resulting in a smaller enzyme form
-
BMY is stored in seeds bound to starchy endosperm possibly through S-S bridges, during germination the enzyme is released by proteolytic cleavage resulting in a smaller enzyme form
additional information
-
differentiation of beta-amylase phenotypes in cultivated barley from worldwide collections, geographical distribution, overview
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_HORVU
535
0
59647
Swiss-Prot
Secretory Pathway (Reliability: 5)
PDB
SCOP
CATH
UNIPROT
ORGANISM
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
56000
59144
-
x * 59144, mutant enzyme M185L/S295A/I297V/S350P/S351P/Q352D/A376S, calculation from amino acid sequence
56000
-
x * 56000, mutant enzyme M185L/S295A/I297V/S350P/S351P/Q352D/A376S, SDS-PAGE
SUBUNIT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
?
-
x * 59144, mutant enzyme M185L/S295A/I297V/S350P/S351P/Q352D/A376S, calculation from amino acid sequence
?
-
x * 56000, mutant enzyme M185L/S295A/I297V/S350P/S351P/Q352D/A376S, SDS-PAGE
POSTTRANSLATIONAL MODIFICATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
proteolytic modification
beta-amylase undergoes proteolytic cleavage of the C-terminal region after germination, removal of the four C-terminal glycine-rich repeats enhances the thermostability and substrate binding affinity
proteolytic modification
-
BMY is stored in seeds bound to starchy endosperm possibly through S-S bridges, during germination the enzyme is released by proteolytic cleavage resulting in a smaller enzyme form, the uncleaved enzyme form shows reduced activity
CRYSTALLIZATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
PROTEIN VARIANTS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
L347S
-
Sd2L mutant, mutation increases the thermostability index T50 by 2.1°C by slowing thermal unfolding of enzyme during heating
M185L/S295A/I297V/S350P/S351P/Q352D/A376S
-
the mutant enzyme acquires enhanced thermostability, but its function as beta-amylase is unchanged. The mutant is stable at pH-values up to 12.5, while the original recombinant enzyme is unstable at pH-values above pH 9.5
R115C
-
Sd2L mutant, mutation is responsible for the difference in the kinetic properties of the allelic forms
V233A
-
Sd2L and Sd1 mutant, mutation increases the thermostability index T50 of Sd2L by 1.9°C, mutation causes an acceleration of the refolding after heating
V233A/L347S
-
Sd2L double mutation resulting in exactly the same sequence as Sd2H beta-amylase, mutation increases the thermostability index T50 of Sd2L by 4°C
additional information
additional information
generation of different specific deletions at the C-terminal tail and complete deletion of the four C-terminal glycine-rich repeats, complete deletion enhances the thermostability, but the incomplete not, both enhance the substrate binding affinity
additional information
-
generation of different specific deletions at the C-terminal tail and complete deletion of the four C-terminal glycine-rich repeats, complete deletion enhances the thermostability, but the incomplete not, both enhance the substrate binding affinity
additional information
-
Sd1 and Sd2L beta-amylase with a 46 amino acid deletion in the C-terminal tail
pH STABILITY
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
12.5
-
mutant enzyme M185L/S295A/I297V/S350P/S351P/Q352D/A376S is stable up to
208638
TEMPERATURE STABILITY
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
57
57.5
-
30 min, analysis of isozyme thermostability of different cultivars, overview
60
-
pH 4.8, half-life: 291 min for the first decay segment, 1790 min for the second decay segment
69
-
30 min, mutant enzyme M185L/S295A/I297V/S350P/S351P/Q352D/A376S, 50% inactivation
70
-
pH 4.8, half-life: 14.4 min for the first decay segment, 37.9 min for the second decay segment
additional information
additional information
-
the 3 allelic forms of beta-amylase Sd1, Sd2H and Sd2L exhibit different thermostability, due to two amino acid substitutions, V233A and L347S, which increase the thermostability index T50 of Sd2L by 1.9°C and 2.1°C, respectively
additional information
-
the recombinant isozyme Bmy2 from cultivar Morex shows a slightly higher thermostability compared to the recombinant enzyme from cultivar Steptoe, T50 values, residues D238, M337, and Q362 are involved in the Morex Bmy2 thermostability, overview
additional information
-
thermal inactivation kinetics of the enzyme at different pressure/temperature conditions, mechanism, overview
PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
native beta-amylase from both mature grain and germinated barley of Sd1 and Sd2L barley varieties, recombinant beta-amylase
CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
Sd1 and Sd2L, from developing grain, expression in Escherichia coli M15
expression in Escherichia coli, the recombinant enzyme lacks 4 amino acids at positions 2-5 (Glu-Val-Asn-Val) when compared with barley beta-amylase
-
expression of a sevenfold mutant beta-amylase, M185L/S295A/I297V/S350P/S351P/Q352D/A376S
-
isozyme Bmy2 from cultivars Morex and Steptoe, DNA and amino acid sequence determination and analysis, expression in Escherichia coli
-
two of the 3 allelic forms of beta-amylase Sd1 and Sd2L are cloned and sequenced
-
EXPRESSION
ORGANISM
UNIPROT
LITERATURE
the beta-amylase activity is negatively correlated with abscisic acid concentration, exogenous application of H2O2 and ascorbic acid decreases beta-amylase activity in the abscisic acid-sensitive barley mutant TL43
-
the beta-amylase activity is positively correlated with H2O2 concentration, exogenous application of H2O2 and ascorbic acid increases beta-amylase activity in barley variety Triumph
-
APPLICATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
brewing
-
beta-amylase allelic forms have different thermostability and kinetic properties, which critically influence their malting quality, production of barley varieties with better malting quality by genetic engineering
nutrition
-
the enzyme is important in maltose production, and in fermentation processes of food and alcoholic beverages
REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
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
-
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
-
Hon, C.C.; Reilly, P.J.
Properties of beta-amylase immobilized to alkylamine porous silica
Biotechnol. Bioeng.
21
505-512
1979
Hordeum vulgare, Triticum aestivum
Visuri, K.; Nummi, M.
Purification and characterisation of crystalline beta-amylase from barley
Eur. J. Biochem.
28
555-565
1972
Hordeum vulgare
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
Yoshigi, N.; Okada, Y.; Sahara, H.; Koshino, S.
Expression in Escherichia coli of cDNA encoding barley beta-amylase and properties of recombinant beta-amylase
Biosci. Biotechnol. Biochem.
58
1080-1086
1994
Hordeum vulgare
Mikami, B.; Yoon, H.J.; Yosjigi, N.
The crystal structure of the sevenfold mutant of barley beta-amylase with increased thermostability at 2.5 A resolution
J. Mol. Biol.
285
1235-1243
1999
Hordeum vulgare
Ma, Y.F.; Eglinton, J.K.; Evans, D.E.; Logue, S.J.; Langridge, P.
Removal of the four C-terminal glycine-rich repeats enhances the thermostability and substrate binding affinity of barley beta-amylase
Biochemistry
39
13350-13355
2000
Hordeum vulgare (P16098), Hordeum vulgare
Ma, Y.F.; Evans, D.E.; Logue, S.J.; Langridge, P.
Mutations of barley beta-amylase that improve substrate-binding affinity and thermostability
Mol. Genet. Genomics
266
345-352
2001
Hordeum vulgare
Heinz, V.; Buckow, R.; Knorr, D.
Catalytic activity of beta-amylase from barley in different pressure/temperature domains
Biotechnol. Prog.
21
1632-1638
2005
Hordeum vulgare
Zhang, W.; Kaneko, T.; Ishii, M.; Takeda, K.
Differentiation of beta-amylase phenotypes in cultivated barley
Crop Sci.
44
1608-1614
2004
Hordeum vulgare
-
Clark, S.E.; Hayes, P.M.; Henson, C.A.
Characterization of barley tissue-ubiquitous beta-amylase2 and effects of the single nucleotide polymorphisms on the enzymes thermostability
Crop Sci.
45
1868-1876
2005
Hordeum vulgare
-
Yoon, S.; Robyt, J.F.
Activation and stabilization of 10 starch-degrading enzymes by Triton X-100, polyethylene glycols, and polyvinyl alcohols
Enzyme Microb. Technol.
37
556-562
2005
Hordeum vulgare
-
Dahot, M.U.; Saboury, A.A.; Moosavi-Movahedi, A.A.
Inhibition of beta-amylase activity by calcium, magnesium and zinc ions determined by spectrophotometry and isothermal titration calorimetry
J. Enzyme Inhib. Med. Chem.
19
157-160
2004
Hordeum vulgare
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
-
Chiapparino, E.; Donini, P.; Reeves, J.; Tuberosa, R.; OSullivan, D.M.
Distribution of ?-amylase I haplotypes among European cultivated barleys
Mol. Breed.
18
341-354
2006
Hordeum vulgare (Q9AVJ8), Hordeum vulgare (Q9FUK6)
Hickman, B.E.; Janaswamy, S.; Yao, Y.
Properties of starch subjected to partial gelatinization and beta-amylolysis
J. Agric. Food Chem.
57
666-674
2009
Hordeum vulgare
Monnet, D.; Joly, C.; Dole, P.; Bliard, C.
Enhanced mechanical properties of partially beta-amylase trimmed starch for material applications
Carbohydr. Polym.
80
747-752
2010
Hordeum vulgare
-
Mukerjea, R.; Robyt, J.F.
Isolation, structure, and characterization of the putative soluble amyloses from potato, wheat, and rice starches
Carbohydr. Res.
345
449-451
2010
Hordeum vulgare
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