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Literature summary for 3.2.1.1 extracted from

  • Yezdani, E.; Sendi, J.J.; Zibaee, A.; Ghadamyari, M.
    Enzymatic properties of alpha-amylase in the midgut and the salivary glands of mulberry moth, Glyphodes pyloalis Walker (Lepidoptera: Pyralidae) (2010), C. R. Biol., 333, 17-22.
    View publication on PubMed
Search for more literature for 3.2.1.1

Inhibitors

Inhibitors Comment Organism Structure
Ca2+ 40% residual activity at 20 mM Ca2+ for midgut alpha-amylase and 46% residual activity at 10 mM Ca2+ for salivary gland alpha-amylase Glyphodes pyloalis
EDTA 37% residual activity at 4 mM EDTA for midgut alpha-amylase and 30% residual activity at 4 mM EDTA for salivary gland alpha-amylase Glyphodes pyloalis
K+ 78% residual activity at 40 mM K+ for midgut alpha-amylase Glyphodes pyloalis
Mg2+ 26% residual activity at 5 mM Mg2+ for midgut alpha-amylase and 28% residual activity at 10 mM Mg2+ for salivary gland alpha-amylase Glyphodes pyloalis
Na+ 25% residual activity at 5 mM Na+ for midgut alpha-amylase and 32% residual activity at 5 mM Na+ for salivary gland alpha-amylase Glyphodes pyloalis
SDS 25% residual activity at 2 mM SDS for midgut alpha-amylase and 49% residual activity at 4 mM SDS for salivary gland alpha-amylase Glyphodes pyloalis
Urea 19% residual activity at 8 mM urea for midgut alpha-amylase and 62% residual activity at 4 mM urea for salivary gland alpha-amylase Glyphodes pyloalis

Metals/Ions

Metals/Ions Comment Organism Structure
Ca2+ 197% relative activity at 20 mM Ca2+ for salivary gland alpha-amylase Glyphodes pyloalis
EDTA 112% relative activity at 2 mM EDTA for salivary gland alpha-amylase Glyphodes pyloalis
K+ 248% relative activity at 20 mM K+ for midgut alpha-amylase and 223% relative activity at 20 mM K+ for salivary gland alpha-amylase Glyphodes pyloalis
Na+ 120% relative activity at 10 mM Na+ for midgut alpha-amylase and 183% relative activity at 20 mM Na+ for salivary gland alpha-amylase Glyphodes pyloalis
Urea 132% relative activity at 8 mM urea for salivary gland alpha-amylase Glyphodes pyloalis

Natural Substrates/ Products (Substrates)

Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
glycogen + H2O Glyphodes pyloalis
-
 malto-oligosaccharides
-
 ?

Organism

Organism UniProt Comment Textmining
Glyphodes pyloalis
-
 mulberry moth
-

Source Tissue

Source Tissue Comment Organism Textmining
midgut
-
 Glyphodes pyloalis
-
salivary gland
-
 Glyphodes pyloalis
-

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
glycogen + H2O
-
 Glyphodes pyloalis malto-oligosaccharides
-
 ?
starch + H2O
-
 Glyphodes pyloalis malto-oligosaccharides
-
 ?

Synonyms

Synonyms Comment Organism
alpha-1,4-glucan-4-glucanohydrolase
-
 Glyphodes pyloalis

Temperature Optimum [°C]

Temperature Optimum [°C] Temperature Optimum Maximum [°C] Comment Organism
37
-
 alpha-amylase from salivary gland Glyphodes pyloalis
37 40 alpha-amylase from midgut Glyphodes pyloalis

pH Optimum

pH Optimum Minimum pH Optimum Maximum Comment Organism
9
-
 alpha-amylase from midgut Glyphodes pyloalis
10
-
 alpha-amylase from salivary gland Glyphodes pyloalis

pH Stability

pH Stability pH Stability Maximum Comment Organism
4 10 the enzyme activity is increased gradually from 4.0 to 9.0 and 4.0 to 10.0 in case of midgut and salivary enzymes, respectively and decreases thereafter with increasing pH Glyphodes pyloalis