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Literature summary 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

Inhibitors

EC Number Inhibitors Comment Organism Structure
3.2.1.1 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
3.2.1.1 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
3.2.1.1 K+ 78% residual activity at 40 mM K+ for midgut alpha-amylase Glyphodes pyloalis
3.2.1.1 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
3.2.1.1 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
3.2.1.1 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
3.2.1.1 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

EC Number Metals/Ions Comment Organism Structure
3.2.1.1 Ca2+ 197% relative activity at 20 mM Ca2+ for salivary gland alpha-amylase Glyphodes pyloalis
3.2.1.1 EDTA 112% relative activity at 2 mM EDTA for salivary gland alpha-amylase Glyphodes pyloalis
3.2.1.1 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
3.2.1.1 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
3.2.1.1 Urea 132% relative activity at 8 mM urea for salivary gland alpha-amylase Glyphodes pyloalis

Natural Substrates/ Products (Substrates)

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

Organism

EC Number Organism UniProt Comment Textmining
3.2.1.1 Glyphodes pyloalis
-
 mulberry moth
-

Source Tissue

EC Number Source Tissue Comment Organism Textmining
3.2.1.1 midgut
-
 Glyphodes pyloalis
-
3.2.1.1 salivary gland
-
 Glyphodes pyloalis
-

Substrates and Products (Substrate)

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

Synonyms

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

Temperature Optimum [°C]

EC Number Temperature Optimum [°C] Temperature Optimum Maximum [°C] Comment Organism
3.2.1.1 37
-
 alpha-amylase from salivary gland Glyphodes pyloalis
3.2.1.1 37 40 alpha-amylase from midgut Glyphodes pyloalis

pH Optimum

EC Number pH Optimum Minimum pH Optimum Maximum Comment Organism
3.2.1.1 9
-
 alpha-amylase from midgut Glyphodes pyloalis
3.2.1.1 10
-
 alpha-amylase from salivary gland Glyphodes pyloalis

pH Stability

EC Number pH Stability pH Stability Maximum Comment Organism
3.2.1.1 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