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Literature summary for 3.2.1.1 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
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KM Value [mM]

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

Metals/Ions

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

Molecular Weight [Da]

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

Organism

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

Purification (Commentary)

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

Substrates and Products (Substrate)

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

Temperature Optimum [°C]

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

pH Optimum

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