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Literature summary for 3.2.1.41 extracted from

  • Plant, A.R.; Morgan, H.W.; Daniel, R.M.
    A highly stable pullulanase from Thermus aquaticus YT-1 (1986), Enzyme Microb. Technol., 8, 668-672.
No PubMed abstract available
Search for more literature for 3.2.1.41

Inhibitors

Inhibitors Comment Organism Structure
EDTA
-
 Thermus aquaticus
Hg2+
-
 Thermus aquaticus
Mn2+
-
 Thermus aquaticus

Metals/Ions

Metals/Ions Comment Organism Structure
Ca2+
-
 Thermus aquaticus

Molecular Weight [Da]

Molecular Weight [Da] Molecular Weight Maximum [Da] Comment Organism
80000 83000 gel filtration, gel electrophoresis Thermus aquaticus

Natural Substrates/ Products (Substrates)

Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
amylopectin + H2O Thermus aquaticus branched polysaccharides maltooligosaccharides + maltose
-
 ?
pullulan + H2O Thermus aquaticus
-
 maltotriose + ?
-
 ?

Organism

Organism UniProt Comment Textmining
Thermus aquaticus
-
-
-

Purification (Commentary)

Purification (Comment) Organism
-
 Thermus aquaticus

Specific Activity [micromol/min/mg]

Specific Activity Minimum [µmol/min/mg] Specific Activity Maximum [µmol/min/mg] Comment Organism
0.949
-
-
 Thermus aquaticus

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
amylopectin + H2O
-
 Thermus aquaticus maltooligosaccharides + maltose
-
 ?
amylopectin + H2O branched polysaccharides Thermus aquaticus maltooligosaccharides + maltose
-
 ?
pullulan + H2O
-
 Thermus aquaticus maltotriose + ?
-
 ?

Synonyms

Synonyms Comment Organism
pullulanase type I hydrolyzes (1-6)-alpha-D-glucosidic linkages in pullulan Thermus aquaticus

pH Optimum

pH Optimum Minimum pH Optimum Maximum Comment Organism
6.5
-
-
 Thermus aquaticus