Literature summary extracted from
Gangadharan, D.; Nampoothiri, K.M.; Sivaramakrishnan, S.; Pandey, A.
Biochemical characterization of raw-starch-digesting alpha amylase purified from Bacillus amyloliquefaciens (2009), Appl. Biochem. Biotechnol., 158, 653-662.
Inhibitors
EC Number |
Inhibitors |
Comment |
Organism |
Structure |
---|
3.2.1.1 |
EDTA |
80% of the enzyme activity is lost when the enzyme is incubated with 10 mM EDTA, indicating the enzyme is a metalloenzyme, pH 5.0, 50°C |
Bacillus amyloliquefaciens |
|
3.2.1.1 |
K+ |
inhibits enzyme activity, 60 and 42% relative activity with 5 and 10 mM K+, pH 5.0, 50°C |
Bacillus amyloliquefaciens |
|
3.2.1.1 |
Mg2+ |
shows no significant effect with 5 mM Mg2+, 92% relative activity, lead to inhibition with 10 mM, 48% relative activity, pH 5.0, 50°C |
Bacillus amyloliquefaciens |
|
3.2.1.1 |
Mn2+ |
inhibits enzyme activity, 50 and 21% relative activity with 5 and 10 mM Mn2+, pH 5.0, 50°C |
Bacillus amyloliquefaciens |
|
3.2.1.1 |
SDS |
retains 30 and 12% relative activity after inhibition with 5 and 10 mM SDS, respectively, pH 5.0, 50°C |
Bacillus amyloliquefaciens |
|
3.2.1.1 |
Urea |
retains 58 and 16% relative activity after inhibition with 5 and 10 mM urea, respectively, pH 5.0, 50°C |
Bacillus amyloliquefaciens |
|
3.2.1.1 |
Zn2+ |
shows no significant effect with 5 mM Zn2+, 90% relative activity, lead to inhibition with 10 mM, 56% relative activity |
Bacillus amyloliquefaciens |
|
KM Value [mM]
EC Number |
KM Value [mM] |
KM Value Maximum [mM] |
Substrate |
Comment |
Organism |
Structure |
---|
3.2.1.1 |
additional information |
- |
amylose |
Km: 2.34 mg and Vmax: 3.047 mg/min |
Bacillus amyloliquefaciens |
|
Metals/Ions
EC Number |
Metals/Ions |
Comment |
Organism |
Structure |
---|
3.2.1.1 |
Ca2+ |
enhances the enzyme activity with 5 mM Ca2+, 120% relative activity, and with 10 mM 96% relative activity, pH 5.0, 50°C |
Bacillus amyloliquefaciens |
|
3.2.1.1 |
Cu2+ |
enhances the enzyme activity with 5 mM Cu2+, 120% relative activity, and with 10 mM 87% relative activity, pH 5.0, 50°C |
Bacillus amyloliquefaciens |
|
Molecular Weight [Da]
EC Number |
Molecular Weight [Da] |
Molecular Weight Maximum [Da] |
Comment |
Organism |
---|
3.2.1.1 |
58000 |
- |
SDS-PAGE |
Bacillus amyloliquefaciens |
Organism
EC Number |
Organism |
UniProt |
Comment |
Textmining |
---|
3.2.1.1 |
Bacillus amyloliquefaciens |
- |
ATCC 23842 |
- |
Purification (Commentary)
EC Number |
Purification (Comment) |
Organism |
---|
3.2.1.1 |
38.46fold purified, to near homogeneity |
Bacillus amyloliquefaciens |
Specific Activity [micromol/min/mg]
EC Number |
Specific Activity Minimum [µmol/min/mg] |
Specific Activity Maximum [µmol/min/mg] |
Comment |
Organism |
---|
3.2.1.1 |
72 |
- |
purified to near homogeneity, pH 5.0, 50°C |
Bacillus amyloliquefaciens |
Substrates and Products (Substrate)
EC Number |
Substrates |
Comment Substrates |
Organism |
Products |
Comment (Products) |
Rev. |
Reac. |
---|
3.2.1.1 |
amylose + H2O |
120% relative enzyme activity compared to reaction with soluble starch as substrate, pH 5.0, 50°C |
Bacillus amyloliquefaciens |
? |
- |
? |
|
3.2.1.1 |
corn starch + H2O |
62% relative enzyme activity compared to reaction with soluble starch as substrate, pH 5.0, 50°C |
Bacillus amyloliquefaciens |
? |
- |
? |
|
3.2.1.1 |
potato starch + H2O |
95% relative enzyme activity compared to reaction with soluble starch as substrate, pH 5.0, 50°C |
Bacillus amyloliquefaciens |
? |
- |
? |
|
3.2.1.1 |
rice starch + H2O |
43% relative enzyme activity compared to reaction with soluble starch as substrate, pH 5.0, 50°C |
Bacillus amyloliquefaciens |
? |
- |
? |
|
3.2.1.1 |
starch + H2O |
soluble starch as substrate, pH 5.0, 50°C, 100% relative enzyme activity |
Bacillus amyloliquefaciens |
? |
the liberated reducing sugars (glucose equivalents) are estimated by the dinitrosalicylic acid method |
? |
|
3.2.1.1 |
wheat starch + H2O |
56.5% relative enzyme activity compared to reaction with soluble starch as substrate, pH 5.0, 50°C |
Bacillus amyloliquefaciens |
? |
- |
? |
|
Subunits
EC Number |
Subunits |
Comment |
Organism |
---|
3.2.1.1 |
? |
x * 58000, SDS-PAGE |
Bacillus amyloliquefaciens |
Synonyms
EC Number |
Synonyms |
Comment |
Organism |
---|
3.2.1.1 |
alpha amylase |
- |
Bacillus amyloliquefaciens |
Temperature Optimum [°C]
EC Number |
Temperature Optimum [°C] |
Temperature Optimum Maximum [°C] |
Comment |
Organism |
---|
3.2.1.1 |
50 |
- |
optimum and assay at |
Bacillus amyloliquefaciens |
Temperature Range [°C]
EC Number |
Temperature Minimum [°C] |
Temperature Maximum [°C] |
Comment |
Organism |
---|
3.2.1.1 |
40 |
80 |
40, 50, 60, 70, and 80°C with relative activities of 78, 100, 80, 40, and 18%, respectively |
Bacillus amyloliquefaciens |
Temperature Stability [°C]
EC Number |
Temperature Stability Minimum [°C] |
Temperature Stability Maximum [°C] |
Comment |
Organism |
---|
3.2.1.1 |
60 |
- |
in the absence of CaCl2, the enzyme is stable up to 25 min retaining 65% of the activity. In the presence of 5 mM CaCl2 90% of the activity retained after 25 min incubation at 60°C |
Bacillus amyloliquefaciens |
pH Optimum
EC Number |
pH Optimum Minimum |
pH Optimum Maximum |
Comment |
Organism |
---|
3.2.1.1 |
5 |
- |
optimum and assay at |
Bacillus amyloliquefaciens |
pH Range
EC Number |
pH Minimum |
pH Maximum |
Comment |
Organism |
---|
3.2.1.1 |
4 |
10 |
pH 4.0, 5.0, 6.0, 7.0, 8.0, 9.0, and 10.0 with relative activities of 62, 100, 82, 78, 65, 35, and 20%, respectively |
Bacillus amyloliquefaciens |