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Information on EC 3.2.1.1 - alpha-amylase and Organism(s) Thermotoga maritima and UniProt Accession P96107

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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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Thermotoga maritima
UNIPROT: P96107
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The taxonomic range for the selected organisms is: Thermotoga maritima
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
1,4-alpha-D-glucan glucanohydrolase
-
-
-
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alkaline alpha-amylase
-
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alpha-1,4-glucan-4-glucanohydrolase
-
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Alpha-amylase carcinoid
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-
-
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Amy c6
-
-
-
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AMY1
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-
-
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Amylase THC 250
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-
-
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amylase, alpha-
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-
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Amylopsin
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-
-
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AmyN26
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recombinant enzyme
Bactosol TK
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-
-
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Buclamase
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-
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Clarase
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-
-
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Clone 103
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-
-
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Clone 168
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-
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Clone PHV19
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-
-
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Clones GRAMY56 and 963
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-
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diastase
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-
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endoamylase
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-
-
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Fortizyme
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-
-
-
G 995
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-
-
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glycogenase
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-
-
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High pI alpha-amylase
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-
-
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Isozyme 1B
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-
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Kleistase L 1
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-
-
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Low pI alpha-amylase
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-
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Maxamyl
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-
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Maxilase
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Meiotic expression upregulated protein 30
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-
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Pancreatic alpha-amylase
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-
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Pivozin
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Ptyalin
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Spitase CP 1
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-
-
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TAA
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-
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Taka-amylase A
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Takatherm
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-
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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
-
SUBSTRATE
PRODUCT                       
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
amylose + H2O
D-glucose + maltose + maltotriose + maltodextrins
show the reaction diagram
-
best substrate for AmyC, hydrolysis of alpha-1,4-glucosidic linkages
small amount of longer maltodextrins, degradation process via malto-oligosaccharides
-
?
beta-limit-dextrin + H2O
D-glucose + maltose + maltotriose + maltodextrins
show the reaction diagram
-
28% of the activity with amylose, hydrolysis of alpha-1,4-glucosidic linkages
small amount of longer maltodextrins, degradation process via malto-oligosaccharides
-
?
glycogen + H2O
?
show the reaction diagram
-
-
-
-
?
maltotriose + H2O
maltose + D-glucose
show the reaction diagram
-
hydrolysis of alpha-1,4-glucosidic linkages
-
-
?
starch + H2O
D-glucose + maltose + maltotriose + maltodextrins
show the reaction diagram
-
soluble starch, 68% of the activity with amylose, hydrolysis of alpha-1,4-glucosidic linkages
small amount of longer maltodextrins, degradation process via malto-oligosaccharides
-
?
starch + H2O
malto-oligosaccharides
show the reaction diagram
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-
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-
?
additional information
?
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hydrolysis of alpha-1,4-glucosidic linkages, glycogen and beta-cyclodextrin are poor substrates for AmyC, no activity with pullulan and maltose
-
-
?
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
glycogen + H2O
?
show the reaction diagram
-
-
-
-
?
starch + H2O
malto-oligosaccharides
show the reaction diagram
-
-
-
-
?
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
ATP
-
90% inhibition at 5 mM, reversible by addition of Ca2+ or Mg2+
Ca2+
-
added alone Ca2+ is inhibitory
EDTA
-
complete inhibition at 0.1 mM, reversible by addition of Ca2+ or Mg2+
EGTA
-
complete inhibition at 0.1 mM, reversible by addition of Ca2+ or Mg2+
Mg2+
-
added alone Mg2+ is inhibitory
NaCl
-
50% inhibition at 50 mM
additional information
-
the enzyme is inhibited by several metal ions
-
ACTIVATING COMPOUND
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
2-mercaptoethanol
-
slightly activates the recombinant enzyme
DTT
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recombinant enzyme, activates 3fold at 5-10 mM
L-cysteine
-
slightly activates the recombinant enzyme
SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
0.3 - 1.6
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purified
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
85
-
recombinant enzyme made from Escherichia coli
LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY hide
GeneOntology No.
LITERATURE
SOURCE
UNIPROT
ENTRY NAME
ORGANISM
NO. OF AA
NO. OF TRANSM. HELICES
MOLECULAR WEIGHT[Da]
SOURCE
SEQUENCE
LOCALIZATION PREDICTION?
P96107_THEMT
553
1
64741
TrEMBL
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MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
241000
-
recombinant AmyC, gel filtration
62000
62060
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calculated from amino acid sequence
62859
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4 * 62859, AmyC, amino acid sequence calculation, 4 * 62000, recombinant AmyC, SDS-PAGE
SUBUNIT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
tetramer
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4 * 62859, AmyC, amino acid sequence calculation, 4 * 62000, recombinant AmyC, SDS-PAGE
TEMPERATURE STABILITY
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
37 - 100
-
there is no detectable activity of plant-made AmyN26 below 37°C when compared to the wild type. The plant-made enzyme retains 85% of its initial activity after 3 h incubation at 100°C, the recombinant enzyme is completely inactivated after 30 min under the same conditions
90
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6 h, 80% remaining activity
PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
Q-Sepharose column chromatography
-
recombinant AmyC from Escherichia coli
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CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
expressed in Nicotiana tabacum NT1 cells and in Escherichia coli BL21(DE3) cells
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gene amyC, DNA and amino acid sequence determination and analysis, overexpression in Escherichia coli
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REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Ballschmiter, M.; Fuetterer, O.; Liebl, W.
Identification and characterization of a novel intracellular alkaline alpha-amylase from the hyperthermophilic bacterium Thermotoga maritima MSB8
Appl. Environ. Microbiol.
72
2206-2211
2006
Thermotoga maritima, Thermotoga maritima MSB8 / DSM 3109 / ATCC 43589
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
Santa-Maria, M.C.; Chou, C.J.; Yencho, G.C.; Haigler, C.H.; Thompson, W.F.; Kelly, R.M.; Sosinski, B.
Plant cell calcium-rich environment enhances thermostability of recombinantly produced alpha-amylase from the hyperthermophilic bacterium Thermotoga maritima
Biotechnol. Bioeng.
104
947-956
2009
Thermotoga maritima
Manually annotated by BRENDA team