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Literature summary extracted from

  • Guarna, M.M.; Borowsky, R.L.
    Biochemical properties of amylase isoenzymes from Gammarus palustris. A comparative study (1995), Comp. Biochem. Physiol. B, 112, 619-628.
    View publication on PubMed

KM Value [mM]

EC Number KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
3.2.1.1 additional information
-
 additional information
-
 Gammarus palustris

Metals/Ions

EC Number Metals/Ions Comment Organism Structure
3.2.1.1 Cl- activates isoenzyme IC and IW Gammarus palustris

Molecular Weight [Da]

EC Number Molecular Weight [Da] Molecular Weight Maximum [Da] Comment Organism
3.2.1.1 50000
-
 isoenzyme Amy IW, non-denaturing PAGE Gammarus palustris
3.2.1.1 50400
-
 isoenzyme Amy IC, non-denaturing PAGE Gammarus palustris
3.2.1.1 55900
-
 isoenzyme Amy II.55, non-denaturing PAGE Gammarus palustris
3.2.1.1 57100
-
 isoenzyme Amy II.52, non-denaturing PAGE Gammarus palustris
3.2.1.1 69400
-
 isoenzyme Amy III, non-denaturing PAGE Gammarus palustris

Organism

EC Number Organism UniProt Comment Textmining
3.2.1.1 Gammarus palustris
-
 isoenzymes Amy IW, Amy IC, Amy II.52, Amy II.55, and Amy III
-

Purification (Commentary)

EC Number Purification (Comment) Organism
3.2.1.1 isonenzyme Amy IW and Amy IC Gammarus palustris

Substrates and Products (Substrate)

EC Number Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
3.2.1.1 starch + H2O
-
 Gammarus palustris additional information predominant formation of maltotriose ?

Temperature Optimum [°C]

EC Number Temperature Optimum [°C] Temperature Optimum Maximum [°C] Comment Organism
3.2.1.1 30
-
 isoenzyme IC Gammarus palustris

pH Optimum

EC Number pH Optimum Minimum pH Optimum Maximum Comment Organism
3.2.1.1 7.5
-
 isoenzyme IW and IC Gammarus palustris