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Literature summary for 3.2.1.54 extracted from

  • Kim, T.J.; Shin, J.H.; Oh, J.H.; Kim, M.J.; Lee, S.B.; Ryu, S.; Kwon, K.; Kim, J.W.; Choi, E.H.; Robyt, J.F.; Park, K.H.
    Analysis of the gene encoding cyclomaltodextrinase from alkalophilic Bacillus sp. I-5 and cgaracterization of enzymatic properties (1998), Arch. Biochem. Biophys., 353, 221-227.
    View publication on PubMed

Activating Compound

Activating Compound Comment Organism Structure
EDTA 5 mM EDTA, activity increases more than 2fold, relative activity 237.2% Bacillus sp. (in: Bacteria)
EGTA increases activity about 2.3fold, relative activity 236.3% Bacillus sp. (in: Bacteria)

Cloned(Commentary)

Cloned (Comment) Organism
CDase I-5 gene, pBR322, expression in Escherichia coli MC1061 Bacillus sp. (in: Bacteria)

Inhibitors

Inhibitors Comment Organism Structure
Ag+
-
Bacillus sp. (in: Bacteria)
Cr3+ relative activity 58.4% Bacillus sp. (in: Bacteria)
Cu2+
-
Bacillus sp. (in: Bacteria)
Fe3+ relative activity 37.7% Bacillus sp. (in: Bacteria)
Li+ relative activity 75.5% Bacillus sp. (in: Bacteria)
Mg2+ relative activity 43% Bacillus sp. (in: Bacteria)
Mn2+ relative activity 64.2% Bacillus sp. (in: Bacteria)
Ni2+ relative activity 72.2% Bacillus sp. (in: Bacteria)
Zn2+ relative activity 5.6% Bacillus sp. (in: Bacteria)

Metals/Ions

Metals/Ions Comment Organism Structure
Ba2+ relative activity 101.5% Bacillus sp. (in: Bacteria)
Ca2+ activated and stabilized by Ca2+, relative activity 128.7% Bacillus sp. (in: Bacteria)

Molecular Weight [Da]

Molecular Weight [Da] Molecular Weight Maximum [Da] Comment Organism
63000
-
MW deduced from the nucleotide sequence 64884 Bacillus sp. (in: Bacteria)

Organism

Organism UniProt Comment Textmining
Bacillus sp. (in: Bacteria)
-
I-5
-
Bacillus sp. (in: Bacteria) I-5
-
I-5
-

Purification (Commentary)

Purification (Comment) Organism
gene encoding enzyme cloned in Escherichia coli, expressed and purified from Escherichia coli Bacillus sp. (in: Bacteria)

Specific Activity [micromol/min/mg]

Specific Activity Minimum [µmol/min/mg] Specific Activity Maximum [µmol/min/mg] Comment Organism
148
-
crude enzyme, purification 1fold Bacillus sp. (in: Bacteria)

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
acarbose + H2O pseudotetrasaccharide inhibitor of glucosidases and alpha-amylases, binding the active sites of the enzyme Bacillus sp. (in: Bacteria) ?
-
?
acarbose + H2O pseudotetrasaccharide inhibitor of glucosidases and alpha-amylases, binding the active sites of the enzyme Bacillus sp. (in: Bacteria) I-5 ?
-
?
cyclomaltodextrin + H2O
-
Bacillus sp. (in: Bacteria) maltodextrin
-
?
cyclomaltodextrin + H2O
-
Bacillus sp. (in: Bacteria) I-5 maltodextrin
-
?
pullulan + H2O
-
Bacillus sp. (in: Bacteria) glucose + panose + isopanose + large saccharides containing alpha 1,6-glucosidic bonds
-
?
pullulan + H2O
-
Bacillus sp. (in: Bacteria) I-5 glucose + panose + isopanose + large saccharides containing alpha 1,6-glucosidic bonds
-
?
starch + H2O
-
Bacillus sp. (in: Bacteria) glucose + maltose
-
?
starch + H2O
-
Bacillus sp. (in: Bacteria) I-5 glucose + maltose
-
?

Temperature Optimum [°C]

Temperature Optimum [°C] Temperature Optimum Maximum [°C] Comment Organism
40 50 in the presence of Ca2+ Bacillus sp. (in: Bacteria)
50
-
pullulan, optimum temperature variable depending on the substrate Bacillus sp. (in: Bacteria)

Temperature Range [°C]

Temperature Minimum [°C] Temperature Maximum [°C] Comment Organism
30 80
-
Bacillus sp. (in: Bacteria)

Temperature Stability [°C]

Temperature Stability Minimum [°C] Temperature Stability Maximum [°C] Comment Organism
60
-
thermal activity more than 80% in presence of Ca2+ Bacillus sp. (in: Bacteria)

pH Optimum

pH Optimum Minimum pH Optimum Maximum Comment Organism
6 7 pullulan as substrate Bacillus sp. (in: Bacteria)
6
-
soluble starch, the optimum pH depending on the substrate Bacillus sp. (in: Bacteria)
7
-
beta-cyclodextrin as substrate Bacillus sp. (in: Bacteria)