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Literature summary for 3.2.1.41 extracted from

  • Kahar, U.M.; Ng, C.L.; Chan, K.G.; Goh, K.M.
    Characterization of a type I pullulanase from Anoxybacillus sp. SK3-4 reveals an unusual substrate hydrolysis (2016), Appl. Microbiol. Biotechnol., 100, 6291-6307.
    View publication on PubMed
Search for more literature for 3.2.1.41

Activating Compound

Activating Compound Comment Organism Structure
2-mercaptoethanol 2 mM, 143% of initial activtiy Anoxybacillus sp.
Tween-20 1% v/v, 143% of initial activtiy Anoxybacillus sp.

Cloned(Commentary)

Cloned (Comment) Organism
expression in Escherichia coli Anoxybacillus sp.

Protein Variants

Protein Variants Comment Organism
additional information amino acids 362-370 of Ask are replaced with the corresponding sequence of type I pullulanase Pul-LM14-2 from Anoxybacillus sp. LM14-2. Unlike wild-type, the mutant enzyme forms reducing sugars on digesting starch Anoxybacillus sp.

Inhibitors

Inhibitors Comment Organism Structure
Ba2+ 2 mM, 54% of initial activtiy Anoxybacillus sp.
Co2+ 2 mM, 15% of initial activtiy Anoxybacillus sp.
Cu2+ 2 mM, 8% of initial activtiy Anoxybacillus sp.
EDTA 2 mM, 68% of initial activtiy Anoxybacillus sp.
Fe2+ 2 mM, 6% of initial activtiy Anoxybacillus sp.
Mn2+ 2 mM, 40% of initial activtiy Anoxybacillus sp.
NH4+ 2 mM, 49% of initial activtiy Anoxybacillus sp.
Ni2+ 2 mM, 47% of initial activtiy Anoxybacillus sp.
Sr2+ 2 mM, 73% of initial activtiy Anoxybacillus sp.
Triton X-100 1% v/v, 72% of initial activtiy Anoxybacillus sp.
Urea 2 mM, 57% of initial activtiy Anoxybacillus sp.
Zn2+ 2 mM, 22% of initial activtiy Anoxybacillus sp.

Metals/Ions

Metals/Ions Comment Organism Structure
K+ 2 mM, 132% of initial activtiy Anoxybacillus sp.
Mg2+ 2 mM, 122% of initial activtiy Anoxybacillus sp.
Na+ 2 mM, 128% of initial activtiy Anoxybacillus sp.

Molecular Weight [Da]

Molecular Weight [Da] Molecular Weight Maximum [Da] Comment Organism
80000
-
 x * 80000, SDS-PAGE Anoxybacillus sp.

Organic Solvent Stability

Organic Solvent Comment Organism
DMSO 2 mM, 59% of initial activtiy Anoxybacillus sp.

Organism

Organism UniProt Comment Textmining
Anoxybacillus sp. EPZ37738
-
-
Anoxybacillus sp. SK3-4 EPZ37738
-
-

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
additional information the enzyme preferably debranches long branches at alpha-1,6 glycosidic bonds of starch, producing amylose, linear or branched oligosaccharides, but is nonreactive against short branches. In addition, the enzyme acts as limit dextrinase, reaction of EC 3.2.1.142, releasing maltotriose, maltotetraose and maltopentaose from limit dextrin Anoxybacillus sp. ?
-
 ?
additional information the enzyme preferably debranches long branches at alpha-1,6 glycosidic bonds of starch, producing amylose, linear or branched oligosaccharides, but is nonreactive against short branches. In addition, the enzyme acts as limit dextrinase, reaction of EC 3.2.1.142, releasing maltotriose, maltotetraose and maltopentaose from limit dextrin Anoxybacillus sp. SK3-4 ?
-
 ?
pullulan + H2O
-
 Anoxybacillus sp. maltotriose + ?
-
 ?
pullulan + H2O
-
 Anoxybacillus sp. SK3-4 maltotriose + ?
-
 ?

Subunits

Subunits Comment Organism
? x * 80000, SDS-PAGE Anoxybacillus sp.

Synonyms

Synonyms Comment Organism
Ask
-
 Anoxybacillus sp.

Temperature Optimum [°C]

Temperature Optimum [°C] Temperature Optimum Maximum [°C] Comment Organism
60
-
-
 Anoxybacillus sp.

Temperature Stability [°C]

Temperature Stability Minimum [°C] Temperature Stability Maximum [°C] Comment Organism
30 60 20 min, stable Anoxybacillus sp.
60
-
 9 h, 50% residual activity Anoxybacillus sp.

pH Optimum

pH Optimum Minimum pH Optimum Maximum Comment Organism
6
-
-
 Anoxybacillus sp.

pH Stability

pH Stability pH Stability Maximum Comment Organism
5 6
-
 Anoxybacillus sp.