Any feedback?
Please rate this page
(literature.php)
(0/150)

BRENDA support

Literature summary extracted from

  • Ballschmiter, M.; Fuetterer, O.; Liebl, W.
    Identification and characterization of a novel intracellular alkaline alpha-amylase from the hyperthermophilic bacterium Thermotoga maritima MSB8 (2006), Appl. Environ. Microbiol., 72, 2206-2211.
    View publication on PubMedView publication on EuropePMC

Activating Compound

EC Number Activating Compound Comment Organism Structure
3.2.1.1 2-mercaptoethanol slightly activates the recombinant enzyme Thermotoga maritima
3.2.1.1 DTT recombinant enzyme, activates 3fold at 5-10 mM Thermotoga maritima
3.2.1.1 L-cysteine slightly activates the recombinant enzyme Thermotoga maritima

Cloned(Commentary)

EC Number Cloned (Comment) Organism
3.2.1.1 gene amyC, DNA and amino acid sequence determination and analysis, overexpression in Escherichia coli Thermotoga maritima

Inhibitors

EC Number Inhibitors Comment Organism Structure
3.2.1.1 ATP 90% inhibition at 5 mM, reversible by addition of Ca2+ or Mg2+ Thermotoga maritima
3.2.1.1 Ca2+ added alone Ca2+ is inhibitory Thermotoga maritima
3.2.1.1 EDTA complete inhibition at 0.1 mM, reversible by addition of Ca2+ or Mg2+ Thermotoga maritima
3.2.1.1 EGTA complete inhibition at 0.1 mM, reversible by addition of Ca2+ or Mg2+ Thermotoga maritima
3.2.1.1 Mg2+ added alone Mg2+ is inhibitory Thermotoga maritima
3.2.1.1 additional information the enzyme is inhibited by several metal ions Thermotoga maritima
3.2.1.1 NaCl 50% inhibition at 50 mM Thermotoga maritima

Localization

EC Number Localization Comment Organism GeneOntology No. Textmining
3.2.1.1 intracellular
-
Thermotoga maritima 5622
-

Molecular Weight [Da]

EC Number Molecular Weight [Da] Molecular Weight Maximum [Da] Comment Organism
3.2.1.1 62000
-
4 * 62859, AmyC, amino acid sequence calculation, 4 * 62000, recombinant AmyC, SDS-PAGE Thermotoga maritima
3.2.1.1 62859
-
4 * 62859, AmyC, amino acid sequence calculation, 4 * 62000, recombinant AmyC, SDS-PAGE Thermotoga maritima
3.2.1.1 241000
-
recombinant AmyC, gel filtration Thermotoga maritima

Organism

EC Number Organism UniProt Comment Textmining
3.2.1.1 Thermotoga maritima
-
gene amyC or tm1438
-
3.2.1.1 Thermotoga maritima MSB8 / DSM 3109 / ATCC 43589
-
gene amyC or tm1438
-

Purification (Commentary)

EC Number Purification (Comment) Organism
3.2.1.1 recombinant AmyC from Escherichia coli Thermotoga maritima

Specific Activity [micromol/min/mg]

EC Number Specific Activity Minimum [µmol/min/mg] Specific Activity Maximum [µmol/min/mg] Comment Organism
3.2.1.1 0.3 1.6 purified Thermotoga maritima

Substrates and Products (Substrate)

EC Number Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
3.2.1.1 amylose + H2O best substrate for AmyC, hydrolysis of alpha-1,4-glucosidic linkages Thermotoga maritima D-glucose + maltose + maltotriose + maltodextrins small amount of longer maltodextrins, degradation process via malto-oligosaccharides ?
3.2.1.1 amylose + H2O best substrate for AmyC, hydrolysis of alpha-1,4-glucosidic linkages Thermotoga maritima MSB8 / DSM 3109 / ATCC 43589 D-glucose + maltose + maltotriose + maltodextrins small amount of longer maltodextrins, degradation process via malto-oligosaccharides ?
3.2.1.1 beta-limit-dextrin + H2O 28% of the activity with amylose, hydrolysis of alpha-1,4-glucosidic linkages Thermotoga maritima D-glucose + maltose + maltotriose + maltodextrins small amount of longer maltodextrins, degradation process via malto-oligosaccharides ?
3.2.1.1 beta-limit-dextrin + H2O 28% of the activity with amylose, hydrolysis of alpha-1,4-glucosidic linkages Thermotoga maritima MSB8 / DSM 3109 / ATCC 43589 D-glucose + maltose + maltotriose + maltodextrins small amount of longer maltodextrins, degradation process via malto-oligosaccharides ?
3.2.1.1 maltotriose + H2O hydrolysis of alpha-1,4-glucosidic linkages Thermotoga maritima maltose + D-glucose
-
?
3.2.1.1 maltotriose + H2O hydrolysis of alpha-1,4-glucosidic linkages Thermotoga maritima MSB8 / DSM 3109 / ATCC 43589 maltose + D-glucose
-
?
3.2.1.1 additional information hydrolysis of alpha-1,4-glucosidic linkages, glycogen and beta-cyclodextrin are poor substrates for AmyC, no activity with pullulan and maltose Thermotoga maritima ?
-
?
3.2.1.1 additional information hydrolysis of alpha-1,4-glucosidic linkages, glycogen and beta-cyclodextrin are poor substrates for AmyC, no activity with pullulan and maltose Thermotoga maritima MSB8 / DSM 3109 / ATCC 43589 ?
-
?
3.2.1.1 starch + H2O soluble starch, 68% of the activity with amylose, hydrolysis of alpha-1,4-glucosidic linkages Thermotoga maritima D-glucose + maltose + maltotriose + maltodextrins small amount of longer maltodextrins, degradation process via malto-oligosaccharides ?
3.2.1.1 starch + H2O soluble starch, 68% of the activity with amylose, hydrolysis of alpha-1,4-glucosidic linkages Thermotoga maritima MSB8 / DSM 3109 / ATCC 43589 D-glucose + maltose + maltotriose + maltodextrins small amount of longer maltodextrins, degradation process via malto-oligosaccharides ?

Subunits

EC Number Subunits Comment Organism
3.2.1.1 tetramer 4 * 62859, AmyC, amino acid sequence calculation, 4 * 62000, recombinant AmyC, SDS-PAGE Thermotoga maritima

Synonyms

EC Number Synonyms Comment Organism
3.2.1.1 alkaline alpha-amylase
-
Thermotoga maritima
3.2.1.1 AmyC
-
Thermotoga maritima

Temperature Optimum [°C]

EC Number Temperature Optimum [°C] Temperature Optimum Maximum [°C] Comment Organism
3.2.1.1 90
-
-
Thermotoga maritima

Temperature Stability [°C]

EC Number Temperature Stability Minimum [°C] Temperature Stability Maximum [°C] Comment Organism
3.2.1.1 90
-
6 h, 80% remaining activity Thermotoga maritima

pH Optimum

EC Number pH Optimum Minimum pH Optimum Maximum Comment Organism
3.2.1.1 8.5
-
-
Thermotoga maritima