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Literature summary extracted from
- Molecular and physiological role of the trehalose-hydrolyzing alpha-glucosidase from Thermus thermophilus HB27 (2008), J. Bacteriol., 190, 2298-2305.
Cloned(Commentary)
| EC Number | Cloned (Comment) | Organism |
|---|---|---|
| 3.2.1.20 | expressed in Escherichia coli DH5alpha | Thermus thermophilus HB8 |
| 3.2.1.20 | expressed in Escherichia coli DH5alpha | Thermus thermophilus HB27 |
Protein Variants
| EC Number | Protein Variants | Comment | Organism |
|---|---|---|---|
| 3.2.1.20 | additional information | site-specific GK24 alpha-glucosidase mutant with the LGEHNLPP peptide of the HB27 enzyme | Thermus thermophilus HB27 |
| 3.2.1.20 | additional information | site-specific mutant of HB27 alpha-glucosidase with the EPTAYHTL peptide of the strain GK24. aglH::Kan, disruption mutant to investigate the specific role of this enzyme in strain HB27 and study the organism's adaptation to specific nutritional conditions, disruption of the alpha-glucosidase gene significantly affects the growth of Thermus thermophilus HB27 | Thermus thermophilus HB27 |
Inhibitors
| EC Number | Inhibitors | Comment | Organism | Structure |
|---|---|---|---|---|
| 3.2.1.20 | Ba2+ | - |
Thermus thermophilus HB27 |  |
| 3.2.1.20 | Co2+ | - |
Thermus thermophilus HB27 | |
| 3.2.1.20 | Cu2+ | - |
Thermus thermophilus HB27 | |
| 3.2.1.20 | Fe2+ | - |
Thermus thermophilus HB27 | |
| 3.2.1.20 | KCl | increasing concentration up to 1 M gradually inhibits the enzyme activity to about 50% | Thermus thermophilus HB27 | |
| 3.2.1.20 | NaCl | increasing concentration up to 0.5 M gradually inhibits the enzyme activity to about 50% | Thermus thermophilus HB27 | |
| 3.2.1.20 | Ni2+ | - |
Thermus thermophilus HB27 | |
| 3.2.1.20 | Zn2+ | - |
Thermus thermophilus HB27 | |
KM Value [mM]
| EC Number | KM Value [mM] | KM Value Maximum [mM] | Substrate | Comment | Organism | Structure |
|---|---|---|---|---|---|---|
| 3.2.1.20 | 4.1 | - |
isomaltose | site-specific GK24 alpha-glucosidase mutant, Vmax: 162 micromol/min mg | Thermus thermophilus HB27 | |
| 3.2.1.20 | 4.9 | - |
trehalose | wild-type, Vmax: 333 micromol/min mg | Thermus thermophilus HB27 | |
| 3.2.1.20 | 5.2 | - |
isomaltose | wild-type, Vmax: 357 micromol/min mg | Thermus thermophilus HB27 | |
| 3.2.1.20 | 6.9 | - |
trehalose | site-specific GK24 alpha-glucosidase mutant, Vmax: 20 micromol/min mg | Thermus thermophilus HB27 | |
| 3.2.1.20 | 8.5 | - |
isomaltose | site-specific mutant of HB27 alpha-glucosidase, Vmax: 286 micromol/min mg | Thermus thermophilus HB27 | |
| 3.2.1.20 | 8.7 | - |
isomaltose | wild-type, Vmax: 250 micromol/min mg | Thermus thermophilus HB27 | |
| 3.2.1.20 | 17 | - |
trehalose | site-specific mutant of HB27 alpha-glucosidase, Vmax: 46 micromol/min mg | Thermus thermophilus HB27 | |
| 3.2.1.20 | 50 | - |
maltose | wild-type, Vmax: 21 micromol/min mg | Thermus thermophilus HB27 | |
| 3.2.1.20 | 55 | - |
maltose | site-specific mutant of HB27 alpha-glucosidase, Vmax: 1.9 micromol/min mg | Thermus thermophilus HB27 | |
| 3.2.1.20 | 69 | - |
maltose | wild-type, Vmax: 11 micromol/min mg | Thermus thermophilus HB27 | |
| 3.2.1.20 | 72 | - |
maltose | site-specific GK24 alpha-glucosidase mutant, Vmax: 3.4 micromol/min mg | Thermus thermophilus HB27 | |
Metals/Ions
| EC Number | Metals/Ions | Comment | Organism | Structure |
|---|---|---|---|---|
| 3.2.1.20 | Ca2+ | 20 mM Ca2+ stimulates activity (153%) | Thermus thermophilus HB27 | |
| 3.2.1.20 | Mn2+ | 20 mM Mn2+ stimulates activity (114%) | Thermus thermophilus HB27 | |
| 3.2.1.20 | additional information | effect of the cations Ca2+, Fe2+, Zn2+, Sr2+, Ni2+, Mn2+, Mg2+, Cu2+, Co2+, and Ba2+ is tested using 25 mM Bis-Tris propane buffer, pH 7, containing cations at concentrations of 2 or 20 mM or no cations. Mg2+ does not affect the activity of the enzyme. Effects of NaCl (20, 50, 100, and 500 mM) and KCl (50, 100, 500, and 1000 mM) are also tested | Thermus thermophilus HB27 | |
| 3.2.1.20 | Sr2+ | 20 mM Sr2+ stimulates activity (123%) | Thermus thermophilus HB27 | |
Molecular Weight [Da]
| EC Number | Molecular Weight [Da] | Molecular Weight Maximum [Da] | Comment | Organism |
|---|---|---|---|---|
| 3.2.1.20 | 61800 | - |
calculated | Thermus thermophilus HB27 |
| 3.2.1.20 | 132000 | - |
recombinant enzyme | Thermus thermophilus HB27 |
Organism
| EC Number | Organism | UniProt | Comment | Textmining |
|---|---|---|---|---|
| 3.2.1.20 | Thermus thermophilus HB27 | Q745T6 | DSM 7039, gene TTC0107 | - |
| 3.2.1.20 | Thermus thermophilus HB27 HB27 / ATCC BAA-163 / DSM 7039 | Q745T6 | DSM 7039, gene TTC0107 | - |
| 3.2.1.20 | Thermus thermophilus HB8 | Q5SL12 | - |
- |
Posttranslational Modification
| EC Number | Posttranslational Modification | Comment | Organism |
|---|---|---|---|
| 3.2.1.20 | glycoprotein | - |
Thermus thermophilus HB8 |
| 3.2.1.20 | glycoprotein | - |
Thermus thermophilus HB27 |
Purification (Commentary)
| EC Number | Purification (Comment) | Organism |
|---|---|---|
| 3.2.1.20 | purified to homogeneity | Thermus thermophilus HB8 |
| 3.2.1.20 | purified to homogeneity | Thermus thermophilus HB27 |
Substrates and Products (Substrate)
| EC Number | Substrates | Comment Substrates | Organism | Products | Comment (Products) | Rev. | Reac. |
|---|---|---|---|---|---|---|---|
| 3.2.1.20 | alpha,alpha-1,1-trehalose + H2O | preferred substrate | Thermus thermophilus HB27 | ? | - |
? | |
| 3.2.1.20 | alpha,beta-1,1-trehalose + H2O | - |
Thermus thermophilus HB27 | ? | - |
? | |
| 3.2.1.20 | isomaltose + H2O | - |
Thermus thermophilus HB27 | ? | - |
? | |
| 3.2.1.20 | isomaltose + H2O | preferred substrate for strain GK24 and HB8 | Thermus thermophilus HB8 | ? | - |
? | |
| 3.2.1.20 | isomaltose + H2O | preferred substrate for strain GK24 and HB8 | Thermus thermophilus HB27 | ? | - |
? | |
| 3.2.1.20 | isomaltotriose + H2O | - |
Thermus thermophilus HB8 | ? | - |
? | |
| 3.2.1.20 | isomaltotriose + H2O | - |
Thermus thermophilus HB27 | ? | - |
? | |
| 3.2.1.20 | isomaltotriose + H2O | - |
Thermus thermophilus HB27 HB27 / ATCC BAA-163 / DSM 7039 | ? | - |
? | |
| 3.2.1.20 | kojibiose + H2O | - |
Thermus thermophilus HB8 | alpha-D-glucose + D-glucose | - |
? | |
| 3.2.1.20 | kojibiose + H2O | - |
Thermus thermophilus HB27 | alpha-D-glucose + D-glucose | - |
? | |
| 3.2.1.20 | leucrose + H2O | alpha-1,5 linkage | Thermus thermophilus HB8 | ? | - |
? | |
| 3.2.1.20 | leucrose + H2O | alpha-1,5 linkage | Thermus thermophilus HB27 | ? | - |
? | |
| 3.2.1.20 | maltose + H2O | alpha-1,4 linkage, poor substrate | Thermus thermophilus HB27 | ? | - |
? | |
| 3.2.1.20 | maltose + H2O | alpha-1,4 linkage, poor substrate. Enzyme can hydrolyze maltose but only at higher substrate and enzyme concentrations | Thermus thermophilus HB8 | ? | - |
? | |
| 3.2.1.20 | maltose + H2O | alpha-1,4 linkage, poor substrate. Enzyme can hydrolyze maltose but only at higher substrate and enzyme concentrations | Thermus thermophilus HB27 | ? | - |
? | |
| 3.2.1.20 | maltotriose + H2O | poor substrate | Thermus thermophilus HB27 | ? | - |
? | |
| 3.2.1.20 | maltotriose + H2O | poor substrate. Enzyme can hydrolyze maltotriose but only at higher substrate and enzyme concentrations | Thermus thermophilus HB8 | ? | - |
? | |
| 3.2.1.20 | maltotriose + H2O | poor substrate. Enzyme can hydrolyze maltotriose but only at higher substrate and enzyme concentrations | Thermus thermophilus HB27 | ? | - |
? | |
| 3.2.1.20 | additional information | cellobiose, alpha,beta-trehalose, beta,beta-trehalose, alpha,alpha-trehalose, gentiobiose, melibiose, melizitose, trehalose-6-phosphate and raffinose are no substrates | Thermus thermophilus HB8 | ? | - |
? | |
| 3.2.1.20 | additional information | cellobiose, alpha,beta-trehalose, beta,beta-trehalose, alpha,alpha-trehalose, gentiobiose, melibiose, melizitose, trehalose-6-phosphate and raffinose are no substrates | Thermus thermophilus HB27 | ? | - |
? | |
| 3.2.1.20 | additional information | cellobiose, beta,beta-trehalose, gentiobiose, melibiose, melizitose, trehalose-6-phosphate and raffinose are no substrates for Thermus thermophilus | Thermus thermophilus HB27 | ? | - |
? | |
| 3.2.1.20 | additional information | cellobiose, alpha,beta-trehalose, beta,beta-trehalose, alpha,alpha-trehalose, gentiobiose, melibiose, melizitose, trehalose-6-phosphate and raffinose are no substrates | Thermus thermophilus HB27 HB27 / ATCC BAA-163 / DSM 7039 | ? | - |
? | |
| 3.2.1.20 | additional information | cellobiose, beta,beta-trehalose, gentiobiose, melibiose, melizitose, trehalose-6-phosphate and raffinose are no substrates for Thermus thermophilus | Thermus thermophilus HB27 HB27 / ATCC BAA-163 / DSM 7039 | ? | - |
? | |
| 3.2.1.20 | nigerose + H2O | - |
Thermus thermophilus HB8 | ? | - |
? | |
| 3.2.1.20 | nigerose + H2O | - |
Thermus thermophilus HB27 | ? | - |
? | |
| 3.2.1.20 | palatinose + H2O | alpha-1,6 linkage | Thermus thermophilus HB8 | ? | - |
? | |
| 3.2.1.20 | palatinose + H2O | alpha-1,6 linkage | Thermus thermophilus HB27 | ? | - |
? | |
| 3.2.1.20 | panose + H2O | - |
Thermus thermophilus HB8 | ? | - |
? | |
| 3.2.1.20 | panose + H2O | - |
Thermus thermophilus HB27 | ? | - |
? | |
| 3.2.1.20 | panose + H2O | - |
Thermus thermophilus HB27 HB27 / ATCC BAA-163 / DSM 7039 | ? | - |
? | |
| 3.2.1.20 | sucrose + H2O | alpha-1,2 linkage | Thermus thermophilus HB8 | D-fructose + D-glucose | - |
? | |
| 3.2.1.20 | sucrose + H2O | alpha-1,2 linkage | Thermus thermophilus HB27 | D-fructose + D-glucose | - |
? | |
| 3.2.1.20 | sucrose + H2O | alpha-1,2 linkage | Thermus thermophilus HB27 HB27 / ATCC BAA-163 / DSM 7039 | D-fructose + D-glucose | - |
? | |
| 3.2.1.20 | trehalose + H2O | - |
Thermus thermophilus HB27 | alpha-D-glucose | - |
? | |
| 3.2.1.20 | trehalose + H2O | site-specific GK24 alpha-glucosidase mutant, Vmax: 20 micromol/min mg | Thermus thermophilus HB27 | alpha-D-glucose | - |
? | |
| 3.2.1.20 | turanose + H2O | alpha-1,3 linkage | Thermus thermophilus HB8 | ? | - |
? | |
| 3.2.1.20 | turanose + H2O | alpha-1,3 linkage | Thermus thermophilus HB27 | ? | - |
? | |
Subunits
| EC Number | Subunits | Comment | Organism |
|---|---|---|---|
| 3.2.1.20 | dimer | the three catalytic residues in the alpha-glucosidase of strain HB27 are Asp197, Glu264, and Asp326, and the substrate-binding histidines are His100 and His325 | Thermus thermophilus HB27 |
Synonyms
| EC Number | Synonyms | Comment | Organism |
|---|---|---|---|
| 3.2.1.20 | alpha-glucosidase | - |
Thermus thermophilus HB8 |
| 3.2.1.20 | alpha-glucosidase | - |
Thermus thermophilus HB27 |
Temperature Optimum [°C]
| EC Number | Temperature Optimum [°C] | Temperature Optimum Maximum [°C] | Comment | Organism |
|---|---|---|---|---|
| 3.2.1.20 | 90 | - |
maximal activity at | Thermus thermophilus HB27 |
Temperature Range [°C]
| EC Number | Temperature Minimum [°C] | Temperature Maximum [°C] | Comment | Organism |
|---|---|---|---|---|
| 3.2.1.20 | 30 | 100 | - |
Thermus thermophilus HB27 |
Temperature Stability [°C]
| EC Number | Temperature Stability Minimum [°C] | Temperature Stability Maximum [°C] | Comment | Organism |
|---|---|---|---|---|
| 3.2.1.20 | 30 | 100 | alpha-glucosidase from strain HB27 has maximal activity at 90°C and about 50% of maximal activity at 70°C but is inactive below 30°C. The enzyme also retains 44% of maximal activity at 100°C | Thermus thermophilus HB27 |
Turnover Number [1/s]
| EC Number | Turnover Number Minimum [1/s] | Turnover Number Maximum [1/s] | Substrate | Comment | Organism | Structure |
|---|---|---|---|---|---|---|
| 3.2.1.20 | 2 | - |
maltose | site-specific mutant of HB27 alpha-glucosidase, Vmax: 1.9 micromol/min mg | Thermus thermophilus HB27 | |
| 3.2.1.20 | 3.5 | - |
N-[[2-carboxy-5-(4-methoxyphenyl)thiophen-3-yl]carbamoyl]-L-tyrosine | site-specific GK24 alpha-glucosidase mutant, Vmax: 3.4 micromol/min mg | Thermus thermophilus HB27 | |
| 3.2.1.20 | 11 | - |
maltose | wild-type, Vmax: 11 micromol/min mg | Thermus thermophilus HB27 | |
| 3.2.1.20 | 20 | - |
trehalose | site-specific GK24 alpha-glucosidase mutant, Vmax: 20 micromol/min mg | Thermus thermophilus HB27 | |
| 3.2.1.20 | 22 | - |
maltose | wild-type, Vmax: 21 micromol/min mg | Thermus thermophilus HB27 | |
| 3.2.1.20 | 47 | - |
trehalose | site-specific mutant of HB27 alpha-glucosidase, Vmax: 46 micromol/min mg | Thermus thermophilus HB27 | |
| 3.2.1.20 | 164 | - |
isomaltose | site-specific GK24 alpha-glucosidase mutant, Vmax: 162 micromol/min mg | Thermus thermophilus HB27 | |
| 3.2.1.20 | 257 | - |
isomaltose | wild-type, Vmax: 250 micromol/min mg | Thermus thermophilus HB27 | |
| 3.2.1.20 | 295 | - |
isomaltose | site-specific mutant of HB27 alpha-glucosidase, Vmax: 286 micromol/min mg | Thermus thermophilus HB27 | |
| 3.2.1.20 | 343 | - |
trehalose | wild-type, Vmax: 333 micromol/min mg | Thermus thermophilus HB27 | |
| 3.2.1.20 | 361 | - |
isomaltose | wild-type, Vmax: 357 micromol/min mg | Thermus thermophilus HB27 | |
pH Optimum
| EC Number | pH Optimum Minimum | pH Optimum Maximum | Comment | Organism |
|---|---|---|---|---|
| 3.2.1.20 | 6.2 | - |
- |
Thermus thermophilus HB27 |
pH Range
| EC Number | pH Minimum | pH Maximum | Comment | Organism |
|---|---|---|---|---|
| 3.2.1.20 | 4 | 9 | testing the effect of pH on enzyme activity | Thermus thermophilus HB27 |
pH Stability
| EC Number | pH Stability | pH Stability Maximum | Comment | Organism |
|---|---|---|---|---|
| 3.2.1.20 | 5.2 | 6.8 | 80% of maximal activity of alpha-glucosidase from strain HB27 is retained between pH 5.2 and 6.8 | Thermus thermophilus HB27 |
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