EC Number | Cloned (Comment) | Organism |
---|---|---|
3.2.1.1 | AMY1, subcloning in Escherichia coli strain DH5alpha, expression of the alpha-amylase C-terminally fused to the Aspergillus niger glucoamlyase starch binding domain in Aspergillus niger strain AB4.1, the mutant enzyme is secreted to the culture medium due to the signal peptide of the barley alpha-amylase | Hordeum vulgare |
EC Number | Protein Variants | Comment | Organism |
---|---|---|---|
3.2.1.1 | additional information | construction of a mutant alpha-amylase, containing its signal peptide, which is fused to the starch binding domain, SBD, of the glucoamylase GA-I of Aspergillus niger via a 37 amino acid GA-I linker segment, the activity of the fusion protein is 2fold enhanced with amylose, and with starch at low concentration, not at high concentration, compared to the wild-type enzyme | Hordeum vulgare |
EC Number | KM Value [mM] | KM Value Maximum [mM] | Substrate | Comment | Organism | Structure |
---|---|---|---|---|---|---|
3.2.1.1 | additional information | - |
additional information | kinetics | Hordeum vulgare | |
3.2.1.1 | 0.23 | - |
amylose DP440 | pH 5.5, 37°C, recombinant AMY1-SBD fusion enzyme | Hordeum vulgare | |
3.2.1.1 | 0.37 | - |
amylose DP17 | pH 5.5, 37°C, recombinant AMY1-SBD fusion enzyme | Hordeum vulgare | |
3.2.1.1 | 2.3 | - |
2-chloro-4-nitrophenyl alpha-D-maltoheptaoside | pH 6.8, 30°C, recombinant AMY1-SBD fusion enzyme | Hordeum vulgare |
EC Number | Metals/Ions | Comment | Organism | Structure |
---|---|---|---|---|
3.2.1.1 | Ca2+ | - |
Hordeum vulgare |
EC Number | Molecular Weight [Da] | Molecular Weight Maximum [Da] | Comment | Organism |
---|---|---|---|---|
3.2.1.1 | 68900 | - |
x * 68900, recombinant AMY1-SBD fusion enzyme, amino acid sequence calculation, x * 75000, recombinant glycosylated AMY1-SBD fusion enzyme, SDS-PAGE | Hordeum vulgare |
3.2.1.1 | 75000 | - |
x * 68900, recombinant AMY1-SBD fusion enzyme, amino acid sequence calculation, x * 75000, recombinant glycosylated AMY1-SBD fusion enzyme, SDS-PAGE | Hordeum vulgare |
EC Number | Natural Substrates | Organism | Comment (Nat. Sub.) | Natural Products | Comment (Nat. Pro.) | Rev. | Reac. |
---|---|---|---|---|---|---|---|
3.2.1.1 | amylose + H2O | Hordeum vulgare | - |
malto-oligosaccharides | - |
? | |
3.2.1.1 | starch + H2O | Hordeum vulgare | - |
malto-oligosaccharides | - |
? |
EC Number | Organism | UniProt | Comment | Textmining |
---|---|---|---|---|
3.2.1.1 | Hordeum vulgare | - |
- |
- |
EC Number | Posttranslational Modification | Comment | Organism |
---|---|---|---|
3.2.1.1 | glycoprotein | the recombinant AMY1-SBD fusion enzyme is O-glycosylated at aminoacid residues 471-509 | Hordeum vulgare |
EC Number | Purification (Comment) | Organism |
---|---|---|
3.2.1.1 | recombinant AMY1-SBD fusion enzyme from Aspergillus niger strain AB4.1 by beta-cyclodextrin affinity chromatography | Hordeum vulgare |
EC Number | Specific Activity Minimum [µmol/min/mg] | Specific Activity Maximum [µmol/min/mg] | Comment | Organism |
---|---|---|---|---|
3.2.1.1 | additional information | - |
activity of recombinant AMY1-SBD fusion enzyme towards different starch substrates | Hordeum vulgare |
EC Number | Storage Stability | Organism |
---|---|---|
3.2.1.1 | 4°C, concentrated purified recombinant AMY1-SBD fusion enzyme, 50 mM MES, pH 6.5, 5 mM CaCl2, stable | Hordeum vulgare |
EC Number | Substrates | Comment Substrates | Organism | Products | Comment (Products) | Rev. | Reac. |
---|---|---|---|---|---|---|---|
3.2.1.1 | 2-chloro-4-nitrophenyl alpha-D-maltoheptaoside + H2O | - |
Hordeum vulgare | 2-chloro-4-nitrophenol + alpha-D-maltoheptaose | - |
? | |
3.2.1.1 | amylose + H2O | - |
Hordeum vulgare | malto-oligosaccharides | - |
? | |
3.2.1.1 | amylose + H2O | amylose DP440 and amylose DP17 | Hordeum vulgare | malto-oligosaccharides | - |
? | |
3.2.1.1 | amylose DP17 + H2O | - |
Hordeum vulgare | ? | - |
? | |
3.2.1.1 | amylose DP440 + H2O | - |
Hordeum vulgare | ? | - |
? | |
3.2.1.1 | starch + H2O | - |
Hordeum vulgare | malto-oligosaccharides | - |
? | |
3.2.1.1 | starch + H2O | starch granules, high affinity for the substrate is mediated by the enzyme's separate starch binding domain, SBD | Hordeum vulgare | malto-oligosaccharides | - |
? |
EC Number | Subunits | Comment | Organism |
---|---|---|---|
3.2.1.1 | ? | x * 68900, recombinant AMY1-SBD fusion enzyme, amino acid sequence calculation, x * 75000, recombinant glycosylated AMY1-SBD fusion enzyme, SDS-PAGE | Hordeum vulgare |
EC Number | Synonyms | Comment | Organism |
---|---|---|---|
3.2.1.1 | AMY1 | - |
Hordeum vulgare |
EC Number | Temperature Optimum [°C] | Temperature Optimum Maximum [°C] | Comment | Organism |
---|---|---|---|---|
3.2.1.1 | 30 | - |
assay at, substrate 2-chloro-4-nitrophenyl alpha-D-maltoheptoside | Hordeum vulgare |
3.2.1.1 | 37 | - |
assay at, substrate starch and amylose | Hordeum vulgare |
EC Number | Turnover Number Minimum [1/s] | Turnover Number Maximum [1/s] | Substrate | Comment | Organism | Structure |
---|---|---|---|---|---|---|
3.2.1.1 | 132 | - |
2-chloro-4-nitrophenyl alpha-D-maltoheptaoside | pH 6.8, 30°C, recombinant AMY1-SBD fusion enzyme | Hordeum vulgare | |
3.2.1.1 | 209 | - |
amylose DP440 | pH 5.5, 37°C, recombinant AMY1-SBD fusion enzyme | Hordeum vulgare | |
3.2.1.1 | 225 | - |
amylose DP17 | pH 5.5, 37°C, recombinant AMY1-SBD fusion enzyme | Hordeum vulgare |
EC Number | pH Optimum Minimum | pH Optimum Maximum | Comment | Organism |
---|---|---|---|---|
3.2.1.1 | 5.5 | - |
assay at, substrate starch and amylose | Hordeum vulgare |
3.2.1.1 | 6.8 | - |
assay at, substrate 2-chloro-4-nitrophenyl alpha-D-maltoheptoside | Hordeum vulgare |
EC Number | Organism | Comment | pI Value Maximum | pI Value |
---|---|---|---|---|
3.2.1.1 | Hordeum vulgare | recombinant AMY1-SBD fusion enzyme, amino acid sequence calculation | - |
4.74 |