Cloned (Comment) | Organism |
---|---|
expressed in Escherichia coli DH5alpha | Thermus thermophilus HB8 |
expressed in Escherichia coli DH5alpha | Thermus thermophilus HB27 |
Protein Variants | Comment | Organism |
---|---|---|
additional information | site-specific GK24 alpha-glucosidase mutant with the LGEHNLPP peptide of the HB27 enzyme | Thermus thermophilus HB27 |
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 | Comment | Organism | Structure |
---|---|---|---|
Ba2+ | - |
Thermus thermophilus HB27 | |
Co2+ | - |
Thermus thermophilus HB27 | |
Cu2+ | - |
Thermus thermophilus HB27 | |
Fe2+ | - |
Thermus thermophilus HB27 | |
KCl | increasing concentration up to 1 M gradually inhibits the enzyme activity to about 50% | Thermus thermophilus HB27 | |
NaCl | increasing concentration up to 0.5 M gradually inhibits the enzyme activity to about 50% | Thermus thermophilus HB27 | |
Ni2+ | - |
Thermus thermophilus HB27 | |
Zn2+ | - |
Thermus thermophilus HB27 |
KM Value [mM] | KM Value Maximum [mM] | Substrate | Comment | Organism | Structure |
---|---|---|---|---|---|
4.1 | - |
isomaltose | site-specific GK24 alpha-glucosidase mutant, Vmax: 162 micromol/min mg | Thermus thermophilus HB27 | |
4.9 | - |
trehalose | wild-type, Vmax: 333 micromol/min mg | Thermus thermophilus HB27 | |
5.2 | - |
isomaltose | wild-type, Vmax: 357 micromol/min mg | Thermus thermophilus HB27 | |
6.9 | - |
trehalose | site-specific GK24 alpha-glucosidase mutant, Vmax: 20 micromol/min mg | Thermus thermophilus HB27 | |
8.5 | - |
isomaltose | site-specific mutant of HB27 alpha-glucosidase, Vmax: 286 micromol/min mg | Thermus thermophilus HB27 | |
8.7 | - |
isomaltose | wild-type, Vmax: 250 micromol/min mg | Thermus thermophilus HB27 | |
17 | - |
trehalose | site-specific mutant of HB27 alpha-glucosidase, Vmax: 46 micromol/min mg | Thermus thermophilus HB27 | |
50 | - |
maltose | wild-type, Vmax: 21 micromol/min mg | Thermus thermophilus HB27 | |
55 | - |
maltose | site-specific mutant of HB27 alpha-glucosidase, Vmax: 1.9 micromol/min mg | Thermus thermophilus HB27 | |
69 | - |
maltose | wild-type, Vmax: 11 micromol/min mg | Thermus thermophilus HB27 | |
72 | - |
maltose | site-specific GK24 alpha-glucosidase mutant, Vmax: 3.4 micromol/min mg | Thermus thermophilus HB27 |
Metals/Ions | Comment | Organism | Structure |
---|---|---|---|
Ca2+ | 20 mM Ca2+ stimulates activity (153%) | Thermus thermophilus HB27 | |
Mn2+ | 20 mM Mn2+ stimulates activity (114%) | Thermus thermophilus HB27 | |
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 | |
Sr2+ | 20 mM Sr2+ stimulates activity (123%) | Thermus thermophilus HB27 |
Molecular Weight [Da] | Molecular Weight Maximum [Da] | Comment | Organism |
---|---|---|---|
61800 | - |
calculated | Thermus thermophilus HB27 |
132000 | - |
recombinant enzyme | Thermus thermophilus HB27 |
Organism | UniProt | Comment | Textmining |
---|---|---|---|
Thermus thermophilus HB27 | Q745T6 | DSM 7039, gene TTC0107 | - |
Thermus thermophilus HB27 HB27 / ATCC BAA-163 / DSM 7039 | Q745T6 | DSM 7039, gene TTC0107 | - |
Thermus thermophilus HB8 | Q5SL12 | - |
- |
Posttranslational Modification | Comment | Organism |
---|---|---|
glycoprotein | - |
Thermus thermophilus HB8 |
glycoprotein | - |
Thermus thermophilus HB27 |
Purification (Comment) | Organism |
---|---|
purified to homogeneity | Thermus thermophilus HB8 |
purified to homogeneity | Thermus thermophilus HB27 |
Substrates | Comment Substrates | Organism | Products | Comment (Products) | Rev. | Reac. |
---|---|---|---|---|---|---|
alpha,alpha-1,1-trehalose + H2O | preferred substrate | Thermus thermophilus HB27 | ? | - |
? | |
alpha,beta-1,1-trehalose + H2O | - |
Thermus thermophilus HB27 | ? | - |
? | |
isomaltose + H2O | - |
Thermus thermophilus HB27 | ? | - |
? | |
isomaltose + H2O | preferred substrate for strain GK24 and HB8 | Thermus thermophilus HB8 | ? | - |
? | |
isomaltose + H2O | preferred substrate for strain GK24 and HB8 | Thermus thermophilus HB27 | ? | - |
? | |
isomaltotriose + H2O | - |
Thermus thermophilus HB8 | ? | - |
? | |
isomaltotriose + H2O | - |
Thermus thermophilus HB27 | ? | - |
? | |
isomaltotriose + H2O | - |
Thermus thermophilus HB27 HB27 / ATCC BAA-163 / DSM 7039 | ? | - |
? | |
kojibiose + H2O | - |
Thermus thermophilus HB8 | alpha-D-glucose + D-glucose | - |
? | |
kojibiose + H2O | - |
Thermus thermophilus HB27 | alpha-D-glucose + D-glucose | - |
? | |
leucrose + H2O | alpha-1,5 linkage | Thermus thermophilus HB8 | ? | - |
? | |
leucrose + H2O | alpha-1,5 linkage | Thermus thermophilus HB27 | ? | - |
? | |
maltose + H2O | alpha-1,4 linkage, poor substrate | Thermus thermophilus HB27 | ? | - |
? | |
maltose + H2O | alpha-1,4 linkage, poor substrate. Enzyme can hydrolyze maltose but only at higher substrate and enzyme concentrations | Thermus thermophilus HB8 | ? | - |
? | |
maltose + H2O | alpha-1,4 linkage, poor substrate. Enzyme can hydrolyze maltose but only at higher substrate and enzyme concentrations | Thermus thermophilus HB27 | ? | - |
? | |
maltotriose + H2O | poor substrate | Thermus thermophilus HB27 | ? | - |
? | |
maltotriose + H2O | poor substrate. Enzyme can hydrolyze maltotriose but only at higher substrate and enzyme concentrations | Thermus thermophilus HB8 | ? | - |
? | |
maltotriose + H2O | poor substrate. Enzyme can hydrolyze maltotriose but only at higher substrate and enzyme concentrations | Thermus thermophilus HB27 | ? | - |
? | |
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 | ? | - |
? | |
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 | ? | - |
? | |
additional information | cellobiose, beta,beta-trehalose, gentiobiose, melibiose, melizitose, trehalose-6-phosphate and raffinose are no substrates for Thermus thermophilus | Thermus thermophilus HB27 | ? | - |
? | |
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 | ? | - |
? | |
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 | ? | - |
? | |
nigerose + H2O | - |
Thermus thermophilus HB8 | ? | - |
? | |
nigerose + H2O | - |
Thermus thermophilus HB27 | ? | - |
? | |
palatinose + H2O | alpha-1,6 linkage | Thermus thermophilus HB8 | ? | - |
? | |
palatinose + H2O | alpha-1,6 linkage | Thermus thermophilus HB27 | ? | - |
? | |
panose + H2O | - |
Thermus thermophilus HB8 | ? | - |
? | |
panose + H2O | - |
Thermus thermophilus HB27 | ? | - |
? | |
panose + H2O | - |
Thermus thermophilus HB27 HB27 / ATCC BAA-163 / DSM 7039 | ? | - |
? | |
sucrose + H2O | alpha-1,2 linkage | Thermus thermophilus HB8 | D-fructose + D-glucose | - |
? | |
sucrose + H2O | alpha-1,2 linkage | Thermus thermophilus HB27 | D-fructose + D-glucose | - |
? | |
sucrose + H2O | alpha-1,2 linkage | Thermus thermophilus HB27 HB27 / ATCC BAA-163 / DSM 7039 | D-fructose + D-glucose | - |
? | |
trehalose + H2O | - |
Thermus thermophilus HB27 | alpha-D-glucose | - |
? | |
trehalose + H2O | site-specific GK24 alpha-glucosidase mutant, Vmax: 20 micromol/min mg | Thermus thermophilus HB27 | alpha-D-glucose | - |
? | |
turanose + H2O | alpha-1,3 linkage | Thermus thermophilus HB8 | ? | - |
? | |
turanose + H2O | alpha-1,3 linkage | Thermus thermophilus HB27 | ? | - |
? |
Subunits | Comment | Organism |
---|---|---|
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 | Comment | Organism |
---|---|---|
alpha-glucosidase | - |
Thermus thermophilus HB8 |
alpha-glucosidase | - |
Thermus thermophilus HB27 |
Temperature Optimum [°C] | Temperature Optimum Maximum [°C] | Comment | Organism |
---|---|---|---|
90 | - |
maximal activity at | Thermus thermophilus HB27 |
Temperature Minimum [°C] | Temperature Maximum [°C] | Comment | Organism |
---|---|---|---|
30 | 100 | - |
Thermus thermophilus HB27 |
Temperature Stability Minimum [°C] | Temperature Stability Maximum [°C] | Comment | Organism |
---|---|---|---|
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 Minimum [1/s] | Turnover Number Maximum [1/s] | Substrate | Comment | Organism | Structure |
---|---|---|---|---|---|
2 | - |
maltose | site-specific mutant of HB27 alpha-glucosidase, Vmax: 1.9 micromol/min mg | Thermus thermophilus HB27 | |
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 | |
11 | - |
maltose | wild-type, Vmax: 11 micromol/min mg | Thermus thermophilus HB27 | |
20 | - |
trehalose | site-specific GK24 alpha-glucosidase mutant, Vmax: 20 micromol/min mg | Thermus thermophilus HB27 | |
22 | - |
maltose | wild-type, Vmax: 21 micromol/min mg | Thermus thermophilus HB27 | |
47 | - |
trehalose | site-specific mutant of HB27 alpha-glucosidase, Vmax: 46 micromol/min mg | Thermus thermophilus HB27 | |
164 | - |
isomaltose | site-specific GK24 alpha-glucosidase mutant, Vmax: 162 micromol/min mg | Thermus thermophilus HB27 | |
257 | - |
isomaltose | wild-type, Vmax: 250 micromol/min mg | Thermus thermophilus HB27 | |
295 | - |
isomaltose | site-specific mutant of HB27 alpha-glucosidase, Vmax: 286 micromol/min mg | Thermus thermophilus HB27 | |
343 | - |
trehalose | wild-type, Vmax: 333 micromol/min mg | Thermus thermophilus HB27 | |
361 | - |
isomaltose | wild-type, Vmax: 357 micromol/min mg | Thermus thermophilus HB27 |
pH Optimum Minimum | pH Optimum Maximum | Comment | Organism |
---|---|---|---|
6.2 | - |
- |
Thermus thermophilus HB27 |
pH Minimum | pH Maximum | Comment | Organism |
---|---|---|---|
4 | 9 | testing the effect of pH on enzyme activity | Thermus thermophilus HB27 |
pH Stability | pH Stability Maximum | Comment | Organism |
---|---|---|---|
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 |