Any feedback?
Information on EC 3.2.1.1 - alpha-amylase and Organism(s) Bacillus amyloliquefaciens and UniProt Accession P00692
for references in articles please use BRENDA:EC3.2.1.1Please wait a moment until all data is loaded. This message will disappear when all data is loaded.
EC Tree
3.2.1.1 alpha-amylaseIUBMB 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.
Specify your search results
Word Map
- 3.2.1.1
- cortisol
- wheat
- aspergillus
- maltose
- pancreas
- glycogen
- oryzae
- granule
- lipase
- alpha-glucosidase
-
acid-schiff
- flour
- glucoamylase
-
amylolytic
- amylose
- aleurone
- grain
-
sympathetic
-
social
- parotid
- cereal
- acarbose
- amyloliquefaciens
-
psychological
-
anxiety
- amylopectin
- beta-amylase
- stearothermophilus
- honey
-
gibberellic
- endosperm
- phaseolus
-
psychosocial
-
bread
-
hypothalamic-pituitary-adrenal
-
alcian
-
bake
- cyclodextrins
- dextrin
- amyloglucosidase
-
pas-positive
-
transglycosylation
-
baking
- pullulanase
-
debranching
-
dough
- isoamylase
- awakening
-
eclosion
- pullulan
- brewing
- nutrition
- synthesis
- biotechnology
- pharmacology
- analysis
- medicine
- industry
- food industry
- energy production
- biofuel production
- detergent
- agriculture
The taxonomic range for the selected organisms is: Bacillus amyloliquefaciens
The enzyme appears in selected viruses and cellular organisms
The enzyme appears in selected viruses and cellular organisms
Reaction Schemes
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
topSYNONYM 
ORGANISM
UNIPROT
COMMENTARY 
LITERATURE
1,4-alpha-D-glucan glucanohydrolase
-
-
-
-
Alpha-amylase carcinoid
-
-
-
-
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
-
-
-
-
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
-
-
-
-
PATHWAY SOURCE
PATHWAYS
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
9000-90-2
-
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
2 starch + H2O
2 malto-oligosaccharides + maltose
-
hydrolysis of soluble starch, and degradation of raw starch granules of different source, overview
-
-
?
corn starch + H2O
?
-
62% relative enzyme activity compared to reaction with soluble starch as substrate, pH 5.0, 50°C
-
-
?
potato starch + H2O
?
-
95% relative enzyme activity compared to reaction with soluble starch as substrate, pH 5.0, 50°C
-
-
?
rice starch + H2O
?
-
43% relative enzyme activity compared to reaction with soluble starch as substrate, pH 5.0, 50°C
-
-
?
starch + H2O
?
-
soluble starch as substrate, pH 5.0, 50°C, 100% relative enzyme activity
the liberated reducing sugars (glucose equivalents) are estimated by the dinitrosalicylic acid method
-
?
wheat starch + H2O
?
-
56.5% relative enzyme activity compared to reaction with soluble starch as substrate, pH 5.0, 50°C
-
-
?
amylose + H2O
?
-
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
?
-
120% relative enzyme activity compared to reaction with soluble starch as substrate, pH 5.0, 50°C
-
-
?
amylose + H2O
malto-oligosaccharides
-
soluble substrate, hydrolysis of alpha-1,4-linkages
-
-
?
maltopentaose + H2O
malto-oligomers + maltose
-
preferred substrate
-
-
?
p-nitrophenyl-alpha-D-maltopentaoside + H2O
?
-
poor substrate
-
-
?
p-nitrophenyl-alpha-D-maltopentaoside + H2O
?
-
good substrate
-
-
?
amylopectin + H2O
additional information
-
-
-
predominant initial products are: maltose, maltotriose, maltohexaose and maltoheptaose
?
amylose + H2O
additional information
-
-
-
predominant initial products are: maltose, maltotriose, maltohexaose and maltoheptaose
?
glycogen + H2O
additional information
-
-
-
immediate products are maltohexaose and maltoheptaose
?
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
METALS and IONS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
Ca2+
the Ca2+-binding residue Asp233 affects significantly the alpha-amylase specific activity
Ca2+
Cu2+
-
enhances the enzyme activity with 5 mM Cu2+, 120% relative activity, and with 10 mM 87% relative activity, pH 5.0, 50°C
additional information
Ca2+
-
increases the thermostability of the enzyme, four Ca2+ ions per enzyme molecule
Ca2+
-
enhances the enzyme activity with 5 mM Ca2+, 120% relative activity, and with 10 mM 96% relative activity, pH 5.0, 50°C
additional information
-
the enzyme is poorly affected by Ca2+, Mg2+, Li+, Cu2+, Ba2+, and Mn2+
additional information
-
BH072 alpha-amylase is a Ca2+-independent enzyme
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
dodecyltrimethylammonium bromide
-
2.5 mM, approx. 40% inhibition at 60°C
K+
-
inhibits enzyme activity, 60 and 42% relative activity with 5 and 10 mM K+, pH 5.0, 50°C
Mg2+
-
shows no significant effect with 5 mM Mg2+, 92% relative activity, lead to inhibition with 10 mM, 48% relative activity, pH 5.0, 50°C
Mn2+
-
inhibits enzyme activity, 50 and 21% relative activity with 5 and 10 mM Mn2+, pH 5.0, 50°C
SDS
-
retains 30 and 12% relative activity after inhibition with 5 and 10 mM SDS, respectively, pH 5.0, 50°C
Urea
-
retains 58 and 16% relative activity after inhibition with 5 and 10 mM urea, respectively, pH 5.0, 50°C
additional information
-
no or poor inhibition by Ba2+, K+, Ca2+, Mn2+, and Co2+ at 5-50 mM and by SDS, PMSF, Triton X-100, and Tween 20 at 1-5%
-
EDTA
-
80% of the enzyme activity is lost when the enzyme is incubated with 10 mM EDTA, indicating the enzyme is a metalloenzyme, pH 5.0, 50°C
Zn2+
-
shows no significant effect with 5 mM Zn2+, 90% relative activity, lead to inhibition with 10 mM, 56% relative activity
ACTIVATING COMPOUND
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
polyethylene glycol 1000
-
1500 Da PEG, increases the enzyme activity by 24% at 0.02% w/v
polyethylene glycol 1500
-
1500 Da PEG, increases the enzyme activity by 23% at 0.02% w/v
-
polyethylene glycol 2000
-
1500 Da PEG, increases the enzyme activity by 19% at 0.02% w/v
polyethylene glycol 400
-
1500 Da PEG, increases the enzyme activity by 5% at 0.02% w/v
-
polyethylene glycol 4600
-
1500 Da PEG, increases the enzyme activity by 19% at 0.02% w/v
polyethylene glycol 600
-
1500 Da PEG, increases the enzyme activity by 16% at 0.02% w/v
polyethylene glycol 8000
-
1500 Da PEG, increases the enzyme activity by 19% at 0.02% w/v
polyvinyl alcohol
-
10 kDa: increases the enzyme activity by 28% 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
additional information
amylose
-
Km: 2.34 mg and Vmax: 3.047 mg/min
additional information
additional information
-
thermodynamics and kinetics
-
additional information
additional information
-
0.24 mg/ml for soluble starch, variant enzyme M77
-
additional information
additional information
-
0.34 mg/ml for soluble starch, wild-type enzyme
-
additional information
additional information
-
0.63 mg/ml for soluble starch, variant enzyme 21B
-
additional information
additional information
-
0.8 mg/ml for soluble starch, variant enzyme M111
-
additional information
additional information
-
Km of BH072 alpha-amylase is 4.27 mg/ml
-
TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
additional information
additional information
-
503 per s for soluble starch, variant enzyme M77
-
additional information
additional information
-
586 per s for soluble starch, wild-type enzyme
-
additional information
additional information
-
656 per s for soluble starch, variant enzyme M111
-
additional information
additional information
-
722 per s for soluble starch, variant enzyme 21B
-
SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
additional information
-
activities with soluble starch of wild-type native enzyme, and recombinant wild-type enzyme from different expressing Escherichia coli strains, overview
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
pH RANGE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
4 - 10
-
pH 4.0, 5.0, 6.0, 7.0, 8.0, 9.0, and 10.0 with relative activities of 62, 100, 82, 78, 65, 35, and 20%, respectively
TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
50 - 75
in presence of 5 mM Ca2+, the optimum temperature of AmyQ is between 50 and 75°C
40
45
50 - 60
60
65
45
-
enzymes from strain SB, T and F show 2 optima: at 45°C and at 60°C
50 - 60
-
optimal temperature in presence of 5 mM Ca2+, variant enzyme 21B
50 - 60
-
optimal temperature in presence of 5 mM Ca2+, variant enzyme M111
60
-
enzymes from strain SB, T and F show 2 optima: at 45°C and at 60°C
60
-
optimal temperature in absence of Ca2+ and presence of 5 mM Ca2+, variant enzyme M77
60
-
optimal temperature in absence of Ca2+ and presence of 5 mM Ca2+, wild-type enzyme
65
-
enzymes from strain SB, T and F show 2 optima: at 45°C and at 60°C. Enzmyes from strain N and P show a single optimum at 65°C
TEMPERATURE RANGE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
25 - 85
-
approx. 60% of maximal activity at 25°C, approx. 30% of maximal activity at 85°C
30 - 90
-
55% of maximal activity at 30°C, 80% at 80°C, and 30% at 90°C, profile overview
40 - 80
-
40, 50, 60, 70, and 80°C with relative activities of 78, 100, 80, 40, and 18%, respectively
ORGANISM
COMMENTARY
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
SOURCE
LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY
GeneOntology No.
LITERATURE
SOURCE
GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
additional information
-
N-terminal amino acid sequencing using mass spectrometry for analysis and homology modelling of the catalytic domain, 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). PDB
SCOP
CATH
UNIPROT
ORGANISM
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
58000
SUBUNIT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
additional information
additional information
-
loosly packed enzyme interior, secondary enzyme structure does not protect against aqueous environment, overview
additional information
-
three-dimensional structure analysis of intact and unfolded enzyme
CRYSTALLIZATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
hanging drop vapor diffusion method, using 24% (w/v) PEG 3350 and 3.5 mM CaCl2 in 10 mM Tris buffer pH 7.5
PROTEIN VARIANTS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
D231N
the specific activity for the mutant enzyme D233N is decreased by 6.3% compared to the wild type. There are no significant changes in the Km value, thermostability, optimum temperature, and optimum pH
D233N
the specific activity for the mutant enzyme D233N is decreased by 84.8% compared to the wild type. D233N exhibits 56% increase in Km and 85.1% decrease in kcat, thermostability at 60°C, optimum temperature and optimum pH for D233N ae reduced to about 10°C and 3-4 units, respectively
D438G
the specific activity for the mutant enzyme D233N is decreased by 3.5% compared to the wild type. There are no significant changes in the Km value, thermostability, optimum temperature, and optimum pH
I34H
-
mutation to corresponding residue of Bacillus licheniformis, complete loss of catalytic activity
P407H
-
mutation to corresponding residue of Bacillus licheniformis, leads to increase in thermostability without significant changes in kinetic parameters. Mutant displays a more rigid structure than wild-type
Q67H
-
mutation to corresponding residue of Bacillus licheniformis, leads to increase in thermostability without significant changes in kinetic parameters. Flexibility of mutant is increased compared to wild-type
V289D
-
the mutation results in complete loss of the alpha-amylase activity
V289E
-
the mutation results in complete loss of the alpha-amylase activity
V289F
-
the mutant shows 48.9% activity compared to the wild type enzyme
V289G
-
the mutant shows 14.5% activity compared to the wild type enzyme
V289I
-
the mutant shows 20% more hydrolytic activity than the wild type enzyme
V289L
-
the mutant shows 36.4% activity compared to the wild type enzyme
V289P
-
the mutant shows 2.2% activity compared to the wild type enzyme
V289R
-
the mutation results in complete loss of the alpha-amylase activity
V289S
-
the mutant shows 5% activity compared to the wild type enzyme
V289Y
-
the mutant shows 9.2% activity compared to the wild type enzyme, the mutant has acquired a transglycosylation activity, which results in the change of product profile of the reaction, giving a longer oligosaccharide
additional information
-
hybrid Bacillus amyloliquefaciens X Bacillus licheniformis alpha-amylase, expression in Escherichia coli and Bacillus subtilis. The letters A and L in the hybrid names stand for the Bacillus amyloliquefaciens and the Bacillus licheniformis portion, respectively, and the numbers for the amino acid residues at the cross-over sites of the hybrid enzymes: Al76, Al108, AL112, AL142, AL147, AL149, AL151, LAL19-153, AL163, AL174
pH STABILITY
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
TEMPERATURE STABILITY
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
35
-
1 h, enzyme from strain P loses 6% of its activity, enzyme from strain SB loses 9% of its activity, enzyme from strain N loses 12% of its activity, enzyme from strain T loses 15% of its activity, enzyme from strain F is stable
60
70
75
-
wild-type, half-life 125 min, mutant Q67H, 145 min, and mutant P407H, 185 min
78
-
half-life of the mosaic hybrid enzymes ALA76-151, ALA17-151: 5 min
80
90
95
-
approx. 50% loss of activity after 2 min, complete loss of activity after 20 min
additional information
60
-
in the absence of CaCl2, the enzyme is stable up to 25 min retaining 65% of the activity. In the presence of 5 mM CaCl2 90% of the activity retained after 25 min incubation at 60°C
70
-
wild-type, 75% of initial activity after 80 min, mutant Q67H after 185 min, and mutant P407H 125 min of incubation, respectively
80
-
96% loss of activity in the absence of additive, 93%, 80%, 86% and 91% loss of activity in the presence of 20% trehalose, sorbitol, mannitol and glycerol, respectively
80
-
approx. 50% loss of activity after 60 min, complete loss of activity after 100 min
90
-
30 min, 10-20% loss of activity of the hybrid enzymes AL76, AL108, and AL112, 35-50% loss of activity of the hybrid enzymes AL142, AL147, AL149, AL151, LAL19-163, AL163, and AL174. About 90% of activity after 30 min of the hybrid enzymes AL231, AL256 and AL263
90
-
half-life of hybrid enzymes: about 50 min for LA431, AL17, Al34
90
-
no loss of activity in the presence of 50% toluene or n-octane
additional information
-
analysis of thermostability of irreversibly unfolding alpha-amylases, unfolding kinetics, Ca2+ increases the thermostability of the enzyme
additional information
-
thermal unfolding kinetics and thermal stability, overview
GENERAL STABILITY
ORGANISM
UNIPROT
LITERATURE
unfolding kinetics, unfolding induced by guanidine hydrochloride
-
ORGANIC SOLVENT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
DEAE-Sepharose column chromatography and G-50 gel filtration
native enzyme from strain BH072 21.23fold by ammonium sulfate fractionation, dialysis, anion exchange chromatography, and gel filtration
-
native enzyme to homogeneity from strain NCIM 2829 culture filtrate
-
native extracellular enzyme from culture medium by adsorption chromatography, the enzyme is sensitive to proteolytic degradation during purification and requires PMSF addition for protection
-
CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
expression in Escherichia coli strains JM109, HB101, HMS174(DE3), and BL21(DE3)
-
REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
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
-
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
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
Welker, N.E.; Campbell, L.L.
Crystallization and properties of alpha-amylase from five strains of Bacillus amyloliquefaciens
Biochemistry
6
3681-3689
1967
Bacillus amyloliquefaciens
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
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)
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)
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
-
De, M.; Das, K.P.; Chakrabartty, P.K.
Purification and characterization of alpha-amylase from Bacillus amyloliquefaciens NCIM 2829
Indian J. Biochem. Biophys.
42
287-294
2005
Bacillus amyloliquefaciens, Bacillus amyloliquefaciens NCIM 2829
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
Demirkan, E.S.; Mikami, B.; Adachi, M.; Higasa, T.; Utsumi, S.
alpha-Amylase from B. amyloliquefaciens: purification, characterization, raw starch degradation and expression in E. coli
Process Biochem.
40
2629-2636
2005
Bacillus amyloliquefaciens
-
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
Lee, S.; Mouri, Y.; Minoda, M.; Oneda, H.; Inouye, K.
Comparison of the wild-type alpha-amylase and its variant enzymes in Bacillus amyloliquefaciens in activity and thermal stability, and insights into engineering the thermal stability of Bacillus alpha-amylase
J. Biochem.
139
1007-1015
2006
Bacillus amyloliquefaciens
Gangadharan, D.; Nampoothiri, K.M.; Sivaramakrishnan, S.; Pandey, A.
Biochemical characterization of raw-starch-digesting alpha amylase purified from Bacillus amyloliquefaciens
Appl. Biochem. Biotechnol.
158
653-662
2009
Bacillus amyloliquefaciens
Alikhajeh, J.; Khajeh, K.; Ranjbar, B.; Naderi-Manesh, H.; Lin, Y.H.; Liu, E.; Guan, H.H.; Hsieh, Y.C.; Chuankhayan, P.; Huang, Y.C.; Jeyaraman, J.; Liu, M.Y.; Chen, C.J.
Structure of Bacillus amyloliquefaciens alpha-amylase at high resolution: implications for thermal stability
Acta Crystallogr. Sect. F
66
121-129
2010
Bacillus amyloliquefaciens (P00692), Bacillus amyloliquefaciens
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
Liu, Y.; Shen, W.; Shi, G.Y.; Wang, Z.X.
Role of the calcium-binding residues Asp231, Asp233, and Asp438 in alpha-amylase of Bacillus amyloliquefaciens as revealed by mutational analysis
Curr. Microbiol.
60
162-166
2010
Bacillus amyloliquefaciens (P00692), Bacillus amyloliquefaciens, Bacillus amyloliquefaciens CICIM B2125 (P00692)
Priyadharshini, R.; Hemalatha, D.; Gunasekaran, P.
Role of Val289 residue in the alpha-amylase of Bacillus amyloliquefaciens MTCC 610: An analysis by site directed mutagenesis
J. Microbiol. Biotechnol.
20
563-568
2010
Bacillus amyloliquefaciens, Bacillus amyloliquefaciens MTCC 610
Haghani, K.; Khajeh, K.; Naderi-Manesh, H.; Ranjbar, B.
Investigation on the effects of three X->histidine replacements on thermostability of alpha-amylase from Bacillus amyloliquefaciens
J. Microbiol. Biotechnol.
22
592-599
2012
Bacillus amyloliquefaciens, Bacillus amyloliquefaciens ATCC 23350
Du, R.; Song, Q.; Zhang, Q.; Zhao, F.; Kim, R.C.; Zhou, Z.; Han, Y.
Purification and characterization of novel thermostable and Ca-independent alpha-amylase produced by Bacillus amyloliquefaciens BH072
Int. J. Biol. Macromol.
115
1151-1156
2018
Bacillus amyloliquefaciens, Bacillus amyloliquefaciens BH072
EXTERNAL LINKS (specific for EC-Number 3.2.1.1)
Transporter Classification Database (TCDB): 8.A.9.1.3
Use of this online version of BRENDA is free under the CC BY 4.0 license. See terms of use for full details.
Release 2023.1 (January 2023)
Legal
Curated at
Member of
