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Information on EC 3.2.1.1 - alpha-amylase

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EC Tree
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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This record set is specific for:
UNIPROT: Q2QC88
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Word Map
The enzyme appears in 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
1,4-alpha-D-glucan glucanohydrolase
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Alpha-amylase carcinoid
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Amy c6
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AMY1
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Amylase THC 250
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amylase, alpha-
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Amylopsin
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Bactosol TK
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Buclamase
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Clarase
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Clone 103
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Clone 168
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Clone PHV19
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Clones GRAMY56 and 963
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diastase
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endoamylase
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Fortizyme
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G 995
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glycogenase
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High pI alpha-amylase
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Isozyme 1B
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Kleistase L 1
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Low pI alpha-amylase
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Maxamyl
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Maxilase
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Meiotic expression upregulated protein 30
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Pancreatic alpha-amylase
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Pivozin
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Ptyalin
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Spitase CP 1
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TAA
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Taka-amylase A
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Takatherm
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Thermamyl
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Thermolase
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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
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SUBSTRATE
PRODUCT                       
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
amylopectin + H2O
?
show the reaction diagram
the enzyme shows a liquefying activity, hydrolyzing maltooligosaccharides, amylopectin, and starch to produce mainly maltose (G2) to maltoheptaose (G7)
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?
maltooligosaccharide + H2O
?
show the reaction diagram
the enzyme shows a liquefying activity, hydrolyzing maltooligosaccharides, amylopectin, and starch to produce mainly maltose (G2) to maltoheptaose (G7)
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?
starch + H2O
?
show the reaction diagram
the enzyme shows a liquefying activity, hydrolyzing maltooligosaccharides, amylopectin, and starch to produce mainly maltose (G2) to maltoheptaose (G7)
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?
additional information
?
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no hydrolysis of pullulan and cyclodextrin
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?
ACTIVATING COMPOUND
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
EDTA
1 mM, 2 ng enzyme, 96% inhibition
KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
additional information
starch
soluble starch: Km 4.57 mg/ml
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
TEMPERATURE RANGE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
40 - 80
less than 20% of maximal activity observed at 40-50°C, 80°C: optimum
pI VALUE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
UNIPROT
ENTRY NAME
ORGANISM
NO. OF AA
NO. OF TRANSM. HELICES
MOLECULAR WEIGHT[Da]
SOURCE
SEQUENCE
LOCALIZATION PREDICTION?
Q2QC88_9EURY
458
0
51948
TrEMBL
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MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
51948
x * 51948, calculated from sequence
SUBUNIT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
?
x * 51948, calculated from sequence
TEMPERATURE STABILITY
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
80
pH 6, half-life: 30 min. Addition of 0.5 mM Ca2+ changes t1/2 at 90°C to 7581 min
90
at pH 6, half-life: 10 min. Addition of 0.5 mM Ca2+ changes t1/2 at 90°C to 153 min. The thermostability is not enhanced by the addition of Zn2+ or other divalent metals, irrespective of the concentration
PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
expression in Escherichia coli
REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Lim, J.K.; Lee, H.S.; Kim, Y.J.; Bae, S.S.; Jeon, J.H.; Kang, S.G.; Lee, J.H.
Critical factors to high thermostability of an alpha-amylase from hyperthermophilic archaeon Thermococcus onnurineus NA1
J. Microbiol. Biotechnol.
17
1242-1248
2007
Thermococcus onnurineus (Q2QC88)
Manually annotated by BRENDA team