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Information on EC 3.2.1.1 - alpha-amylase and Organism(s) Bacillus licheniformis and UniProt Accession P06278

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IUBMB Comments
Acts on starch, glycogen and related polysaccharides and oligosaccharides in a random manner; reducing groups are liberated in the alpha-configuration. The term "alpha" 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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Bacillus licheniformis
UNIPROT: P06278
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Word Map
The taxonomic range for the selected organisms is: Bacillus licheniformis
The enzyme appears in selected viruses and cellular organisms
Synonyms
alpha-amylase, diastase, alpha amylase, pancreatic alpha-amylase, crustacean cardioactive peptide, maltogenic amylase, taka-amylase a, human salivary alpha-amylase, bacillus licheniformis alpha-amylase, alpha-amylase 2, more
SYNONYM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
Bacillus licheniformis alpha-amylase
-
1,4-alpha-D-glucan glucanohydrolase
-
-
-
-
alpha-1,4-glucan-4-glucanohydrolase
-
-
Alpha-amylase carcinoid
-
-
-
-
alpha-amylase PA
-
-
Amy c6
-
-
-
-
AMY1
-
-
-
-
Amylase THC 250
-
-
-
-
amylase, alpha-
-
-
-
-
Amylopsin
-
-
-
-
Bactosol TK
-
-
-
-
Buclamase
-
-
-
-
Clarase
-
-
-
-
Clone 103
-
-
-
-
Clone 168
-
-
-
-
Clone PHV19
-
-
-
-
Clones GRAMY56 and 963
-
-
-
-
diastase
-
-
-
-
endoamylase
-
-
-
-
Fortizyme
-
-
-
-
G 995
-
-
-
-
glycogenase
-
-
-
-
High pI alpha-amylase
-
-
-
-
Isozyme 1B
-
-
-
-
Kleistase L 1
-
-
-
-
liquozyme
-
commercial preparation, free and immobilzed enzyme, covalently bound to calcium alginate matrix
Low pI alpha-amylase
-
-
-
-
Maxamyl
-
-
-
-
Maxilase
-
-
-
-
Meiotic expression upregulated protein 30
-
-
-
-
Pancreatic alpha-amylase
-
-
-
-
Pivozin
-
-
-
-
Ptyalin
-
-
-
-
Spitase CP 1
-
-
-
-
TAA
-
-
-
-
Taka-amylase A
-
-
-
-
Takatherm
-
-
-
-
Thermamyl
-
-
-
-
Thermolase
-
-
-
-
thermostable alpha-amylase
-
free and immobilzed enzyme, covalently bound to calcium alginate matrix
REACTION
REACTION DIAGRAM
COMMENTARY hide
ORGANISM
UNIPROT
LITERATURE
Endohydrolysis of (1->4)-alpha-D-glucosidic linkages in polysaccharides containing three or more (1->4)-alpha-linked D-glucose units
show the reaction diagram
reaction mechanism and kinetic mechanism
-
REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
O-glycosyl bond hydrolysis
-
-
SYSTEMATIC NAME
IUBMB Comments
4-alpha-D-glucan glucanohydrolase
Acts on starch, glycogen and related polysaccharides and oligosaccharides in a random manner; reducing groups are liberated in the alpha-configuration. The term "alpha" 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 hide
9000-90-2
-
SUBSTRATE
PRODUCT                       
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
4,6-ethylidene-[G7]-p-nitrophenyl-[G1]-alpha-D-maltoheptaoside + H2O
p-nitrophenol + 4,6-ethyliden-[G7]-alpha-D-maltoheptaoside
show the reaction diagram
-
-
-
?
starch + H2O
?
show the reaction diagram
starch + H2O
maltooligosaccharides
show the reaction diagram
-
-
-
?
amylose + H2O
?
show the reaction diagram
-
with potato amylose as substrate, the enzyme displays an intermediate degree of multiple attack (the number of bonds broken during the lifetime of an enzyme-substrate complex minus one). The level of multiple attack increases when temperature is raised
-
-
?
amylose + H2O
malto-oligosaccharides
show the reaction diagram
glycogen + H2O
?
show the reaction diagram
-
-
-
-
?
p-nitrophenyl-alpha-D-maltopentaoside + H2O
?
show the reaction diagram
-
-
-
-
?
potato starch + H2O
?
show the reaction diagram
-
-
-
-
?
raw starch + H2O
maltose + maltotriose
show the reaction diagram
hydrolyzed raw starch isolated from a jack fruit seed cotyledons, recombinant enzyme can hydrolyze raw jackfruit seed starch up to 52% after 6 h treatment at 30°C
-
-
?
soluble starch + H2O
?
show the reaction diagram
-
alpha-amylase PA
-
-
?
soluble starch + H2O
maltose + maltotriose
show the reaction diagram
-
-
-
?
starch + H2O
?
show the reaction diagram
starch + H2O
D-glucooligomer
show the reaction diagram
-
-
-
-
?
starch + H2O
fragments of starch
show the reaction diagram
-
-
-
-
?
starch + H2O
malto-oligosaccharides
show the reaction diagram
amylopectin + H2O
additional information
-
NATURAL SUBSTRATE
NATURAL PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
starch + H2O
?
show the reaction diagram
-
-
-
?
starch + H2O
maltooligosaccharides
show the reaction diagram
-
-
-
?
amylose + H2O
malto-oligosaccharides
show the reaction diagram
-
soluble substrate
-
-
?
glycogen + H2O
?
show the reaction diagram
-
-
-
-
?
starch + H2O
fragments of starch
show the reaction diagram
-
-
-
-
?
starch + H2O
malto-oligosaccharides
show the reaction diagram
-
-
-
-
?
METALS and IONS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
CaCl2
-
the reusability of the immobilized enzymes are similar in starch hydrolysis reaction medium containing either 5 mM or 0.25 mM CaCl2
F-
-
stimulates
MoO42-
-
10-100 mM, stimulates
Na+
-
stimulates
PO43-
-
100 mM, stimulates
S2O32-
-
stimulates
SO32-
-
stimulates
SO42-
-
stimulates
WO42-
-
stimulates
additional information
-
the enzyme shows Ca2+-independency, no effect by Ca2+ at 1-5 mM. Poor effects by 1-5 mM of Na+, K+, and Mg2+
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
Tris
starch-hydrolyzing activity in presence of Tris of different concentrations, pH 7.4, 37°C
2-mercaptoethanol
-
37.6% inhibition at 1 mM, 43.7% at 5 mM
4-bromophenacyl bromide
-
ascorbate
-
28.4% inhibition at 5 mM, 34.9% at 10 mM
Ba2+
-
5.3% inhibition at 1 mM, 11.1% at 5 mM
Dimethyl formamide
-
38.2% inhibition at 1 mM, 72.0% at 5 mM
dodecyltrimethylammonium bromide
-
2.5 mM, approx. 20% inhibition at 60°C
DTNB
-
55.2% inhibition at 5 mM
DTT
-
61.9% inhibition at 1 mM, 84.8% at 5 mM
Fe3+
-
complete inhibition at 1-5 mM
H2O2
-
82.3% inhibition at 0.5%, 43.7% at 5 mM
iodoacetate
-
around 100 mM
lauryl sulfobetaine
-
2.5 mM, approx. 20% inhibition at 60°C
Pb2+
-
74.5% inhibition at 1 mM, complete inhibition at 5 mM
PMSF
-
36.5% inhibition at 1mM, 53.7% at 5 mM
SDS
-
14.9% inhibition at 2%
Sodium citrate
-
23.1% inhibition at 5 mM
Sodium dodecyl sulfate
-
2.5 mM, approx. 20% inhibition at 60°C
Triton X-100
-
12.4% inhibition at 10%
Tween 20
-
8.9% inhibition at 20%, 9.2% activation at 10%
Tween 80
-
8.3% inhibition at 20%
additional information
-
no effect by 5-10 mM of urea and glycerol, poor effects by 0.5-1% sodium tetraborate
-
ACTIVATING COMPOUND
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
polyethylene glycol 1000
-
1500 Da PEG, increases the enzyme activity by 36% at 0.02% w/v
polyethylene glycol 1500
-
1500 Da PEG, increases the enzyme activity by 43% at 0.02% w/v
-
polyethylene glycol 2000
-
1500 Da PEG, increases the enzyme activity by 44% at 0.02% w/v
polyethylene glycol 400
-
1500 Da PEG, increases the enzyme activity by 19% at 0.02% w/v
-
polyethylene glycol 4600
-
1500 Da PEG, increases the enzyme activity by 44% at 0.02% w/v
polyethylene glycol 600
-
1500 Da PEG, increases the enzyme activity by 24% at 0.02% w/v
polyethylene glycol 8000
-
1500 Da PEG, increases the enzyme activity by 40% at 0.02% w/v
polyvinyl alcohol
-
10 kDa: increases the enzyme activity by 31% at 0.02% w/v, 50 kDa: increases the enzyme activity by 35% at 0.02% w/v
Triton X-100
-
increases the enzyme activity by 35% at 0.02% w/v
Tween 20
-
8.9% inhibition at 20%, 9.2% activation at 10%
KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.01 - 0.281
4,6-ethylidene-[G7]-p-nitrophenyl-[G1]-alpha-D-maltoheptaoside
additional information
starch
TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
7.86 - 266
4,6-ethylidene-[G7]-p-nitrophenyl-[G1]-alpha-D-maltoheptaoside
additional information
starch
Ki VALUE [mM]
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
13
Tris
determined with Lineweaver-Burk plot, competitive inhibition, pH 7.4, 37°C, docking simulations show that Tris binds deep inside the active site of the enzyme
SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
1343
purified recombinant enzyme, pH 5.0, 60°C
2902.26
-
purified enzyme, pH 5.0, 100°C, substrate starch
additional information
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
10
recombinant extracellular enzyme Blamy-I
5 - 7
-
in presence of 0.5% starch and 4 mM CaCl2
6.4 - 7.6
-
broad
pH RANGE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
5.5 - 9.5
4000 U/ml at pH 5.5, above 4000 U/ml at pH 10.0, pH-optimum: 10000 U/ml
3 - 10
-
activity range, mutant I157S/W193R enzyme
4 - 10
4 - 8
-
free enzyme, pH 4: ca. 5% relative activity, pH 8.0: ca. 12% relative activity, pH-optimum: 5.5
4.5 - 8
-
first and second use of immobilzed enzyme, first use: pH 4.5 ca. with 4% relative activity, pH 8.0 with ca. 25% relative activity, second use: pH 4.5 with ca. 22% relative activity, pH 8.0 with ca. 11% relative activity, pH-optimum: 6.0
5 - 10
-
pH 5.0: about 85% of maximal activity, pH 10.0: about 20% of maximal activity
5.1 - 8.2
-
pH-range where 50% or more of the maximal activity is maintained, alpha-amylase PA
TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
25
assay at, determination of catalytic properties on the substrates
70 - 90
-
at pH 7.0
80
recombinant extracellular enzyme Blamy-I
additional information
TEMPERATURE RANGE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
25 - 100
approx. 20% of maximal activity at 25°C, approx. 90% of maximal activity at 90°C
20 - 150
-
20% of maximal activity at 20°C, 30% at 50°C, 65% at 60°C, 75% at 80°C and 150°C, 90% at 90°C and 110-130°C, profile overview
34 - 48
-
34°C: about 35% of maximal activity, 48°C: about 40% of maximal activity
40 - 100
-
40°C: about 50% of maximal activity, 100°C: about 60% of maximal activity
50
-
ca. 40% of the activity at 95°C is attained
pI VALUE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
6.05
sequence calculation
ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
SOURCE
additional information
isolation of amylolytic strains, determination of optimal growth parameters, overview. Bacillus licheniformis grows best at 60°C, pH 7.0-8.0
Manually annotated by BRENDA team
LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY hide
GeneOntology No.
LITERATURE
SOURCE
GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
physiological function
-
alpha-amylases catalyze the hydrolysis of internal alpha-D-(1,4)-glucosidic linkages in starch, glycogen, and related oligo- and polysaccharides to produce maltodextrins, maltooligosaccharides, and glucose
additional information
UNIPROT
ENTRY NAME
ORGANISM
NO. OF AA
NO. OF TRANSM. HELICES
MOLECULAR WEIGHT[Da]
SOURCE
SEQUENCE
LOCALIZATION PREDICTION?
AMY_BACLI
512
1
58549
Swiss-Prot
-
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
22500
-
gel filtration
28000
-
x * 28000, SDS-PAGE
55000
58000
62650
-
x * 62650, SDS-PAGE
SUBUNIT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
monomer
additional information
PROTEIN VARIANTS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
A209V
more thermostable than wild type enzyme
H133Y
more thermostable than wild type enzyme
L134R
amyl, from recombinant Bacillus subtilis, when the pH is reduced from 6.5 to 4.5, compared with wild-type, Km increases but turnover number decreases, the mutants show an inverse trend, which results in catalytic efficiency (kcat/Km) increased. When the pH is 6.5, the kcat/Km is about 1.5times that of the mutants L134R, S320A, and L134R/S320A. In contrast, the kcat/Km of L134R and S320A are about 8.6- and 7.6times higher than that of the wild-type at pH 4.5. No significant difference on the kcat/Km of the mutants L134R, S320A, and L134R/S320A is shown when the pH is 5.5 and 6.5, respectively
L134R/S320A
amyd, from recombinant Bacillus subtilis, when the pH is reduced from 6.5 to 4.5, compared with wild-type, Km increases but turnover number decreases, the mutants show an inverse trend, which results in catalytic efficiency (kcat/Km) increased. The highest kcat/Km with pH 4.5 approximately 14times that of the wild-type is observed in the double mutant. No significant difference on the kcat/Km of the mutants L134R, S320A, and L134R/S320A is shown when the pH is 5.5 and 6.5, respectively
M15T/H133Y/N188S
at pH 83°C, pH 5.0, 5 mM CaCl2, 4fold longer half-life than wild-type enzyme
M15T/H133Y/N188S/A209V
at pH 83°C, pH 5.0, 5 mM CaCl2, 23fold longer half-life than wild-type enzyme
M15T/N188S
at pH 83°C, pH 5.0, 5 mM CaCl2, 1.5fold longer half-life than wild-type enzyme
M15T/N188S/A209V
at pH 83°C, pH 5.0, 5 mM CaCl2, 4.5fold longer half-life than wild-type enzyme
S320A
amy2, from recombinant Bacillus subtilis, when the pH is reduced from 6.5 to 4.5, compared with wild-type, Km increases but turnover number decreases, the mutants show an inverse trend, which results in catalytic efficiency (kcat/Km) increased. When the pH is 6.5, the kcat/Km is about 1.5times that of the mutants L134R, S320A, and L134R/S320A. In contrast, the kcat/Km of L134R and S320A are about 8.6- and 7.6times higher than that of the wild-type at pH 4.5. No significant difference on the kcat/Km of the mutants L134R, S320A, and L134R/S320A is shown when the pH is 5.5 and 6.5, respectively
I157S/W193R
-
random mutagenesis, the mutant shows an altered pH profile compared to the wild-type enzyme
N172R/H156Y/A181T
-
the mutations increase the thermostability of alpha-amylase by 5fold
additional information
pH STABILITY
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
10
30 min, whole cells, 95% amylase activity is remaining
750079
4.5
the mutant L134R/S320A shows a stronger activity in acidic conditions, In contrast, the wild-type is sensitive to acidic pH. The double mutant is more effective in increasing enzyme stability against acidic pH than L134R and S320A
690586
5
30 min, whole cells, 90% amylase activity is remaining
750079
6 - 9
30 min, whole cells, the amylase activity is completely stable
750079
3
-
30°C, 18 h, 50% loss of activity
393404
4
-
30°C, 18 h, 34% loss of activity
393404
4 - 10
-
purified native enzyme, highly stable at
750781
4 - 9
stable at
750825
5.5
-
90°C, 1 h, 50% loss of activity, alpha-amylase PA
680540
5.5 - 10
-
stable
393378
6
-
30°C, 18 h, 15% loss of activity
393404
6 - 11
-
25°C, 24 h, stable
393406
6 - 12
recombinant enzyme, stable at
750980
7 - 10
-
stable
393412
7 - 9
-
30°C, 18 h, stable
393404
TEMPERATURE STABILITY
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
100
around 60% of the enzyme activity is still detectable in wild-type and mutant enzymes after incubating in a boiling bath for 60 min
70
30 min, whole cells, the amylase activity is completely stable
80
30 min, whole cells, 90% amylase activity is remaining
90
approx. 25% loss of activity after 150 min, approx. 60% loss of activity after 400 min
110
-
1 h, 50-60% loss of activity
20 - 70
-
purified native enzyme, 10 min, completely stable at
41
-
T50-value at pH 4.5, without CaCl2, alpha-amylase PA
60 - 70
recombinant enzyme, stable up to in absence of Ca2+
63
-
T50-value at pH 4.5, 5 mM CaCl2, alpha-amylase PA
71
-
T50-value at pH 6.0, without CaCl2, alpha-amylase PA
78
-
half-life of the mosaic hybrid enzymes ALA76-151, ALA17-151: 5 min
84
-
T50-value at pH 6.0, 5 mM CaCl2, alpha-amylase PA
85
-
60 min, with the exception of the enzyme from strain NCIB 9668, more than 98% of the activity is retained
91
-
1 h, stable
additional information
GENERAL STABILITY
ORGANISM
UNIPROT
LITERATURE
unfolding kinetics, unfolding induced by guanidine hydrochloride
Ca2+ and Na+ stabilize at higher reaction temperatures
-
stabilization by Ca2+, alpha-amylase PA
-
tryptolytic digestion of the enzyme produces two fragments, TF18K and TF38K, and no further fragments can be seen after 6 h incubation. Presence of antiTF18K leads to significant stabilization of the enzyme.
-
ORGANIC SOLVENT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
2-propanol
-
loss of 83% activity at 10% 2-propanol after 30 min at room temperature
Acetone
-
loss of 15% activity at 20% acetone after 30 min at room temperature
Butanol
-
loss of 89% activity at 10% butanol after 30 min at room temperature
octane
-
strong protection against thermal inactivation
toluene
-
strong protection against thermal inactivation
additional information
-
the enzyme activity is poorly affected by 10-20% of methanol, ethanol, chloroform, isoamylalcohol, and hexane after 30 min at room temperature
PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
solubilized recombinant enzyme 138fold from Escherichia coli by cation exchange chromatography
wild-type, and recombinant mutants L134R, S320A, and L134R/S320A
native extracellular enzyme 8.34fold by ammonium sulfate fractionation, gel filtration, and anion exchange chromatography
-
recombinant extracellular enzyme 14.2fold from Escherichia coli strain BL21 (DE3) by hydrophobic interaction chromatography and gel filtration to homogeneity
strain NCIB 6364
-
CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
expressed in Bacillus subitilis WB600
high level expression of thermostable Bacillus licheniformis alpha-amylase in Escherichia coli strain BL21-CodonPlus(DE3)-RIL mainly in inclusion bodies, subcloning in Escherichia coli strain DH5alpha
DNA and amino acid sequence determination and analysis, sequence comparisons
-
expression of wild-type and mutant enzymes in Escherichia coli strain BL21(DE3)
-
gene amyA, sequence comparisons, recombinant overexpression in Escherichia coli strain BL21 (DE3) using the native signal peptide, method optimization leading to 8fold increased production of extracellular enzyme. The amylase activity in culture supernatant of Escherichia coli cells from non-optimized conditions is 51.2 U/ml, from optimized conditions 409.5 U/ml
RENATURED/Commentary
ORGANISM
UNIPROT
LITERATURE
solubilization of recombinant enzyme from inclusion bodies after expression in Escherichia coli without the use of denaturing agents, extraction by resuspending in 50 mmol/l sodium acetate, pH 5.0, containing 20% v/v glycerol followed by stirring at 40°C for 3-4 h, and subsequent centrifugation
APPLICATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
synthesis
industrial-scale starch liquefaction
biofuel production
the recombinant enzyme can be utilized for bioethanol production from jackfruit seed starch
industry
-
the high cumulative activity and seven successive reuses obtained at liquefaction temperature render the covalently bound thermostable enzyme to calcium alginate matrix, a promising candidate for use in industrial starch hydrolysis process
synthesis
REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Dobreva, E.; Ivanova, V.
Characterisierung der Strkehydrolysate nach Einwirkung einer thermostabilen alpha-Amylase
Acta Biotechnol.
9
549-554
1989
Bacillus licheniformis, Bacillus licheniformis 44MB82
-
Manually annotated by BRENDA team
Bajpai, P.; Bajpai, P.K.
High-temperature alkaline alpha-amylase from Bacillus licheniformis TCRDC-B13
Biotechnol. Bioeng.
33
72-78
1989
Bacillus licheniformis, Bacillus licheniformis TCRDC-B13
Manually annotated by BRENDA team
Krishnan, T.; Chandra, A.K.
Purification and characterization of alpha-amylase from Bacillus licheniformis CUMC305
Appl. Environ. Microbiol.
46
430-437
1983
Bacillus licheniformis, Bacillus licheniformis CUMC305
Manually annotated by BRENDA team
Kindle, K.L.
Characterization and production of thermostable alpha-amylase
Appl. Biochem. Biotechnol.
8
153-170
1983
Acinetobacter sp., Alicyclobacillus acidocaldarius, Aspergillus niger, Geobacillus stearothermophilus, Bacillus amyloliquefaciens, Weizmannia coagulans, Priestia megaterium, Bacillus subtilis, Bacillus licheniformis, Bacillus sp. (in: Bacteria), Thermochaetoides thermophila, Humicola brevis, Trichocladium griseum, Humicola insolens, Thermomyces lanuginosus, Humicola stellata, Malbranchea pulchella, Micromonospora vulgaris, Rhizomucor miehei, Rhizomucor pusillus, Thermothelomyces myriococcoides, Rhizopus microsporus, Mycothermus thermophilus, Thermomyces dupontii, Thermoactinomyces vulgaris, Thermoascus aurantiacus, Thermoascus crustaceus, Thermomonospora curvata, Thermomonospora viridis, Thermomonospora vulgaris, Bacillus licheniformis CUMC305, Weizmannia coagulans CUMC512, Bacillus sp. (in: Bacteria) 11-15
-
Manually annotated by BRENDA team
Morgan, F.J.; Priest, F.G.
Characterization of a thermostable alpha-amylase from Bacillus licheniformis NCIB 6343
J. Appl. Bacteriol.
50
107-114
1981
Bacillus licheniformis, Bacillus licheniformis NCIB 8549, Bacillus licheniformis NCIB 8061, Bacillus licheniformis NCIB 6346, Bacillus licheniformis NCTC 8233, Bacillus licheniformis NCIB 8874, Bacillus licheniformis NCIB 6816, Bacillus licheniformis NCIB 8537, Bacillus licheniformis NCIB 9668, Bacillus licheniformis NCIB 7224
-
Manually annotated by BRENDA team
Medda, S.; Chandra, A.K.
New strains of Bacillus licheniformis and Bacillus coagulans producing thermostable alpha-amylase active at alkaline pH
J. Appl. Bacteriol.
48
47-58
1980
Weizmannia coagulans, Bacillus licheniformis, Bacillus licheniformis CUMC305, Weizmannia coagulans CUMC512
Manually annotated by BRENDA team
Ingle, M.B.; Erikson, R.J.
Bacterial alpha-amylases
Adv. Appl. Microbiol.
24
257-278
1978
Alicyclobacillus acidocaldarius, Geobacillus stearothermophilus, Weizmannia coagulans, Bacillus licheniformis, Bacillus sp. (in: Bacteria), Clostridium acetobutylicum, Thermomonospora curvata, Alicyclobacillus acidocaldarius 104-1A, Bacillus sp. (in: Bacteria) A-40-2, Alicyclobacillus acidocaldarius Agnano 101
Manually annotated by BRENDA team
Svensson, B.
Protein engineering in the alpha-amylase family: catalytic mechanism, substrate specificity and stability
Plant Mol. Biol.
25
141-157
1994
Aspergillus oryzae, Geobacillus stearothermophilus, Bacillus amyloliquefaciens, Bacillus subtilis, Bacillus licheniformis, Drosophila melanogaster, Escherichia coli, Saccharomycopsis fibuligera, Homo sapiens, Hordeum vulgare, Mus musculus, Oryza sp., Vigna radiata, Streptomyces hygroscopicus, Sus scrofa, Triticum aestivum, Xanthomonas campestris
Manually annotated by BRENDA team
Conrad, B.; Hoang, V.; Polley, A.; Hofemeister, J.
Hybrid Bacillus amyloliquefaciens X Bacillus licheniformis alpha-amylases. Construction, properties and sequence determinants
Eur. J. Biochem.
230
481-490
1995
Bacillus amyloliquefaciens, Bacillus licheniformis
Manually annotated by BRENDA team
Dercova, K.; Augustin, J.; Krajcova, D.
Cell growth and alpha-amylase production characteristics of Bacillus subtilis
Folia Microbiol. (Praha)
37
17-23
1991
Geobacillus stearothermophilus, Bacillus subtilis, Bacillus licheniformis, Bacillus licheniformis CCM 2145, Geobacillus stearothermophilus CCM 2183, Bacillus subtilis DP 1
Manually annotated by BRENDA team
Shaw, A.; Bott, R.; Day, A.G.
Protein engineering of alpha-amylase for low pH performance
Curr. Opin. Biotechnol.
10
349-352
1999
Bacillus licheniformis (P06278), Bacillus licheniformis
Manually annotated by BRENDA team
Khajeh, K.; Nemat-Gorgani, M.
Comparative studies on a mesophilic and a thermophilic alpha-amylase
Appl. Biochem. Biotechnol.
90
47-55
2001
Bacillus amyloliquefaciens, Bacillus licheniformis
Manually annotated by BRENDA team
Fitter, J.; Herrmann, R.; Dencher, N.A.; Blume, A.; Hauss, T.
Activity and stability of a thermostable alpha-amylase compared to its mesophilic homologue: mechanisms of thermal adaptation
Biochemistry
40
10723-10731
2001
Bacillus amyloliquefaciens, Bacillus licheniformis (P06278)
Manually annotated by BRENDA team
Kainuma, K.
Applied glycoscience-past, present and future
Foods Food Ingredients J. Jpn.
178
4-10
1998
Bacillus licheniformis
-
Manually annotated by BRENDA team
Fitter, J.; Haber-Pohlmeier, S.
Structural stability and unfolding properties of thermostable bacterial alpha-amylases: a comparative study of homologous enzymes
Biochemistry
43
9589-9599
2004
Bacillus amyloliquefaciens, Bacillus licheniformis (P06278)
Manually annotated by BRENDA team
Bravo Rodriguez, V.; Jurado Alameda, E.; Martinez Gallegos, J.F.; Reyes Requena, A.; Garcia Lopez, A.I.
Enzymatic hydrolysis of soluble starch with an alpha-amylase from Bacillus licheniformis
Biotechnol. Prog.
22
718-722
2006
Bacillus licheniformis
Manually annotated by BRENDA team
Mitsuiki, S.; Mukae, K.; Sakai, M.; Goto, M.; Hayashida, S.; Furukawa, K.
Comparative characterization of raw starch hydrolyzing a-amylases from various Bacillus strains
Enzyme Microb. Technol.
37
410-416
2005
Bacillus cereus, Bacillus subtilis, Bacillus licheniformis
-
Manually annotated by BRENDA team
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
Aspergillus oryzae, Bacillus amyloliquefaciens, Bacillus licheniformis, Homo sapiens, Sus scrofa
-
Manually annotated by BRENDA team
Duy, C.; Fitter, J.
Thermostability of irreversible unfolding alpha-amylases analyzed by unfolding kinetics
J. Biol. Chem.
280
37360-37365
2005
Aspergillus oryzae, Bacillus amyloliquefaciens, Bacillus subtilis, Bacillus licheniformis, Sus scrofa
Manually annotated by BRENDA team
Ul-Haq, I.; Ashraf, H.; Ali, S.; Qadeer, M.A.
Kinetic characterization of extracellular alpha-amylase from a derepressed mutant of Bacillus licheniformis
Appl. Biochem. Biotechnol.
141
251-264
2007
Bacillus licheniformis, Bacillus licheniformis NA-14
Manually annotated by BRENDA team
Bijttebier, A.; Goesaert, H.; Delcour, J.A.
Temperature impacts the multiple attack action of amylases
Biomacromolecules
8
765-772
2007
Aspergillus oryzae, Geobacillus stearothermophilus, Bacillus amyloliquefaciens, Bacillus subtilis, Bacillus licheniformis, Sus scrofa, Thermoactinomyces vulgaris
Manually annotated by BRENDA team
Ghasemi, A.; Khajeh, K.; Ranjbar, B.
Stabilization of Bacillus licheniformis alpha-amylase by specific antibody which recognizes the N-terminal fragment of the enzyme
Int. J. Biol. Macromol.
41
162-167
2007
Bacillus licheniformis
Manually annotated by BRENDA team
Lee, S.; Oneda, H.; Minoda, M.; Tanaka, A.; Inouye, K.
Comparison of starch hydrolysis activity and thermal stability of two Bacillus licheniformis alpha-amylases and insights into engineering alpha-amylase variants active under acidic conditions
J. Biochem.
139
997-1005
2006
Bacillus licheniformis, Bacillus licheniformis IFO12196
Manually annotated by BRENDA team
Liu, Y.H.; Lu, F.P.; Li, Y.; Wang, J.L.; Gao, C.
Acid stabilization of Bacillus licheniformis alpha amylase through introduction of mutations
Appl. Microbiol. Biotechnol.
80
795-803
2008
Bacillus licheniformis (P06278), Bacillus licheniformis, Bacillus licheniformis CICC 10181 (P06278)
Manually annotated by BRENDA team
Tee, B.L.; Kaletunc, G.
Immobilization of a thermostable alpha-amylase by covalent binding to an alginate matrix increases high temperature usability
Biotechnol. Prog.
25
436-445
2009
Bacillus licheniformis
Manually annotated by BRENDA team
Ghalanbor, Z.; Ghaemi, N.; Marashi, S.A.; Amanlou, M.; Habibi-Rezaei, M.; Khajeh, K.; Ranjbar, B.
Binding of Tris to Bacillus licheniformis alpha-amylase can affect its starch hydrolysis activity
Protein Pept. Lett.
15
212-214
2008
Bacillus licheniformis (P06278), Bacillus licheniformis
Manually annotated by BRENDA team
Prakash, O.; Jaiswal, N.
alpha-Amylase: an ideal representative of thermostable enzymes
Appl. Biochem. Biotechnol.
160
2401-2414
2010
Alicyclobacillus acidocaldarius, Geobacillus stearothermophilus, Bacillus amyloliquefaciens, Anoxybacillus flavithermus, Bacillus subtilis, Lederbergia lentus, Bacillus licheniformis, Chloroflexus aurantiacus, Thermothelomyces heterothallicus, Desulfurococcus mucosus, Dictyoglomus thermophilum, Thermomyces lanuginosus, Lactiplantibacillus plantarum, Lipomyces kononenkoae, Pyrococcus furiosus, Pyrococcus woesei, Pyrodictium abyssi, Rhizopus sp., Rhodothermus marinus, Mycothermus thermophilus, Staphylothermus marinus, Thermoactinomyces vulgaris, Thermococcus fumicolans, Thermococcus hydrothermalis, Thermococcus litoralis, Thermococcus profundus, Thermotoga maritima, Thermus filiformis, Lactobacillus amylovorus, Halothermothrix orenii, Thermococcus aggregans, Thermococcus celer, Thermococcus guaymasensis
Manually annotated by BRENDA team
Rashid, N.; Ahmed, N.; Saleem Haider, M.; Haque, I.
Effective solubilization and single-step purification of Bacillus licheniformis alpha-amylase from insoluble aggregates
Folia Microbiol. (Praha)
55
133-136
2010
Bacillus licheniformis (P06278), Bacillus licheniformis, Bacillus licheniformis ATCC 27811 (P06278)
Manually annotated by BRENDA team
Priyadharshini, R.; Manoharan, S.; Hemalatha, D.; Gunasekaran, P.
Repeated random mutagenesis of alpha-amylase from Bacillus licheniformis for improved pH performance
J. Microbiol. Biotechnol.
20
1696-1701
2010
Bacillus licheniformis, Bacillus licheniformis MTCC 6598
Manually annotated by BRENDA team
Gashtasbi, F.; Ahmadian, G.; Noghabi, K.A.
New insights into the effectiveness of alpha-amylase enzyme presentation on the Bacillus subtilis spore surface by adsorption and covalent immobilization
Enzyme Microb. Technol.
64-65
17-23
2014
Bacillus licheniformis
Manually annotated by BRENDA team
Awasthi, M.K.; Wong, J.W.C.; Kumar, S.; Awasthi, S.K.; Wang, Q.; Wang, M.; Ren, X.; Zhao, J.; Chen, H.; Zhang, Z.
Biodegradation of food waste using microbial cultures producing thermostable alpha-amylase and cellulase under different pH and temperature
Biores. Technol.
248
160-170
2018
Bacillus cereus, Brevibacillus sp., Brevibacillus borstelensis, Bacillus licheniformis (P06278)
Manually annotated by BRENDA team
Wu, X.; Wang, Y.; Tong, B.; Chen, X.; Chen, J.
Purification and biochemical characterization of a thermostable and acid-stable alpha-amylase from Bacillus licheniformis B4-423
Int. J. Biol. Macromol.
109
329-337
2018
Bacillus licheniformis, Bacillus licheniformis B4-423
Manually annotated by BRENDA team
Homaei, A.; Ghanbarzadeh, M.; Monsef, F.
Biochemical features and kinetic properties of alpha-amylases from marine organisms
Int. J. Biol. Macromol.
83
306-314
2016
Aureobasidium pullulans, Bacillus cereus, Anoxybacillus flavithermus, Bacillus subtilis, Thermomonospora curvata, Thermus sp., Vibrio sp., Eisenia fetida, Saccharopolyspora sp. A9, Wangia sp. C52, Pseudomonas sp. K6-28-040, Anoxybacillus beppuensis, Nocardiopsis sp. B2, Zunongwangia profunda, Rossellomorea aquimaris, Bacillus sp. ALSHL3, Streptomyces sp. D1, Bacillus sp. GM8901, Bacillus sp. TS-23, Bacillus sp. I-3, Bacillus sp. TSCVKK, Bacillus sp. WN 11, Bacillus sp. A-3-15, Chromohalobacter sp. TVSP 101, Bacillus sp. marini, Marinobacter sp. EMB8, Halobacillus sp. amylus, Chryseobacterium taeanense (A0A1G8DI07), Sutcliffiella cohnii (A0A223KY92), Nesterenkonia sp. (A0A2U8ZSD8), Bacillus licheniformis (A1YR25), Bacillus sp. YX-1 (A9YDD9), Parageobacillus caldoxylosilyticus (C0LZ63), Bacillus sp. Ferdowsicous (P86331), Bacillus sp. KSM-K38 (Q93I48), Streptomyces coelicolor A3 (Q9L035), Aureobasidium pullulans N13d, Bacillus subtilis AX20, Chryseobacterium taeanense TKU001 (A0A1G8DI07), Bacillus subtilis DM-03, Anoxybacillus beppuensis TSSC-1, Sutcliffiella cohnii US147 (A0A223KY92), Rossellomorea aquimaris VITP4, Halobacillus sp. amylus HM454199, Parageobacillus caldoxylosilyticus TK4 (C0LZ63), Nesterenkonia sp. F (A0A2U8ZSD8), Streptomyces coelicolor A3 A3(2) (Q9L035), Bacillus licheniformis NH1 (A1YR25), Streptomyces coelicolor A3 M145 (Q9L035), Streptomyces coelicolor A3 ATCC BAA-471 (Q9L035)
Manually annotated by BRENDA team
Roy, J.K.; Manhar, A.K.; Nath, D.; Mandal, M.; Mukherjee, A.K.
Cloning and extracellular expression of a raw starch digesting alpha-amylase (Blamy-I) and its application in bioethanol production from a non-conventional source of starch
J. Basic Microbiol.
55
1287-1298
2015
Bacillus licheniformis (I3P686), Bacillus licheniformis, Bacillus licheniformis AS08E (I3P686)
Manually annotated by BRENDA team