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Literature summary extracted from

  • Fisher, S.Z.; Govindasamy, L.; Tu, C.; Agbandje-McKenna, M.; Silverman, D.N.; Rajaniemi, H.J.; McKenna, R.
    Structure of human salivary alpha-amylase crystallized in a C-centered monoclinic space group (2006), Acta Crystallogr. Sect. F, 62, 88-93.
    View publication on PubMedView publication on EuropePMC

Crystallization (Commentary)

EC Number Crystallization (Comment) Organism
3.2.1.1 purified dimeric enzyme, hanging drop vapour diffusion method, 0.001 ml of 10 mg/ml protein in 50 mM Tris-HCl, pH 7.5, is mixed with 0.001 ml of precipitation solution, three different successful variations, overview, 1 week, X-ray diffraction structure determination and analysis at 3.0 A resolution Homo sapiens

Localization

EC Number Localization Comment Organism GeneOntology No. Textmining
3.2.1.1 extracellular the enzyme is secreted Homo sapiens
-
-

Molecular Weight [Da]

EC Number Molecular Weight [Da] Molecular Weight Maximum [Da] Comment Organism
3.2.1.1 56000
-
x * 62000, glycosylated HSA, SDS-PAGE, x * 56000, deglycosylated HSA, SDS-PAGE Homo sapiens
3.2.1.1 62000
-
x * 62000, glycosylated HSA, SDS-PAGE, x * 56000, deglycosylated HSA, SDS-PAGE Homo sapiens

Organism

EC Number Organism UniProt Comment Textmining
3.2.1.1 Homo sapiens
-
-
-

Posttranslational Modification

EC Number Posttranslational Modification Comment Organism
3.2.1.1 glycoprotein
-
Homo sapiens

Purification (Commentary)

EC Number Purification (Comment) Organism
3.2.1.1 accidental co-purification of the native alpha-amylase with carbonic anhydrase VI from saliva by 4-aminobenzenesulfonamide affinity chromatography Homo sapiens

Source Tissue

EC Number Source Tissue Comment Organism Textmining
3.2.1.1 saliva the enzyme is a major secretory protein component of the saliva Homo sapiens
-

Substrates and Products (Substrate)

EC Number Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
3.2.1.1 malto-oligosaccharides + H2O hydrolysis of alpha-1,4-glucosidic linkages Homo sapiens maltose
-
?

Subunits

EC Number Subunits Comment Organism
3.2.1.1 ? x * 62000, glycosylated HSA, SDS-PAGE, x * 56000, deglycosylated HSA, SDS-PAGE Homo sapiens
3.2.1.1 More HSA consists of three domains, dimer structure, packing, and interface, overview Homo sapiens

Synonyms

EC Number Synonyms Comment Organism
3.2.1.1 HSA
-
Homo sapiens