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Literature summary for 3.2.1.1 extracted from

  • Bealin-Kelly, F.J.; Kelly, C.T.; Fogarty, W.M.
    The alpha-amylase of the caldoactive bacterium Bacillus caldovelox (1990), Biochem. Soc. Trans., 18, 310-311.
    View publication on PubMed

Activating Compound

Activating Compound Comment Organism Structure
2-mercaptoethanol 1.6fold stimulation at 10 mM, 2.5fold stimulation at 100 mM [Bacillus] caldovelox
dithiothreitol 1.6fold stimulation at 10 mM, 2.5fold stimulation at 100 mM [Bacillus] caldovelox

Inhibitors

Inhibitors Comment Organism Structure
PCMB
-
[Bacillus] caldovelox
phenylmercuric acetate
-
[Bacillus] caldovelox
PHMB
-
[Bacillus] caldovelox

Organism

Organism UniProt Comment Textmining
[Bacillus] caldovelox
-
-
-

Posttranslational Modification

Posttranslational Modification Comment Organism
no modification the enzyme is not a glycoprotein [Bacillus] caldovelox

Purification (Commentary)

Purification (Comment) Organism
-
[Bacillus] caldovelox

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
starch + H2O
-
[Bacillus] caldovelox additional information maltohexaose + maltopentaose + maltotriose and low levels of glucose, maltose and maltotetraose ?

Temperature Optimum [°C]

Temperature Optimum [°C] Temperature Optimum Maximum [°C] Comment Organism
60
-
-
[Bacillus] caldovelox

Temperature Stability [°C]

Temperature Stability Minimum [°C] Temperature Stability Maximum [°C] Comment Organism
60
-
stable [Bacillus] caldovelox
70
-
1 h, 80% loss of activity [Bacillus] caldovelox

pH Optimum

pH Optimum Minimum pH Optimum Maximum Comment Organism
4.5
-
-
[Bacillus] caldovelox

pH Stability

pH Stability pH Stability Maximum Comment Organism
3 9 stable [Bacillus] caldovelox