EC Number | Cloned (Comment) | Organism |
---|---|---|
3.2.1.23 | expression of His6-tagged BgaS enzyme and mutant variants in Escherichia coli strain MC1061 (DE3) | Arthrobacter sp. |
EC Number | Protein Variants | Comment | Organism |
---|---|---|---|
3.2.1.23 | E229D | site-directed mutagenesis, enzyme BgaS7a, the mutant shows slightly increased activity compared to the wild-type enzyme | Arthrobacter sp. |
3.2.1.23 | E229D/G803D | site-directed mutagenesis, inactive mutant | Arthrobacter sp. |
3.2.1.23 | E229D/V405A | site-directed mutagenesis, enzyme BgaS7, the mutant shows similar thermal optima and thermostabilities as BgaS, but shows a 2.5fold increase in catalytic activity at 15°C and hydrolyzes 80% of lactose in skim milk in less than half the time of BgaS at 2.5°C | Arthrobacter sp. |
3.2.1.23 | E229D/V405A/G803D | site-directed mutagenesis, enzyme BgaS6, the mutant shows similar thermal optima and thermostabilities as BgaS, the mutant shows slightly increased activity compared to the wild-type enzyme | Arthrobacter sp. |
3.2.1.23 | G803D | site-directed mutagenesis, inactive mutant | Arthrobacter sp. |
3.2.1.23 | additional information | gene bgaS3 encoding a loss of function variant is subjected to random mutagenesis to restore activity and discover potential interactions important in cold activity | Arthrobacter sp. |
3.2.1.23 | V405A | site-directed mutagenesis, enzyme BgaS7b, the mutant shows slightly increased activity compared to the wild-type enzyme | Arthrobacter sp. |
3.2.1.23 | V405A/G803D | site-directed mutagenesis, inactive mutant | Arthrobacter sp. |
EC Number | Inhibitors | Comment | Organism | Structure |
---|---|---|---|---|
3.2.1.23 | D-galactose | product inhibition | Arthrobacter sp. | |
3.2.1.23 | lactose | substrate inhibition | Arthrobacter sp. |
EC Number | KM Value [mM] | KM Value Maximum [mM] | Substrate | Comment | Organism | Structure |
---|---|---|---|---|---|---|
3.2.1.23 | additional information | - |
additional information | temperature dependence of kinetics of wild-type and mutant enzymes, overview | Arthrobacter sp. | |
3.2.1.23 | 7.5 | - |
lactose | 15°C, recombinant mutant BgaS7, i.e. E229D/V405A | Arthrobacter sp. | |
3.2.1.23 | 11.5 | - |
lactose | 15°C, recombinant wild-type BgaS | Arthrobacter sp. | |
3.2.1.23 | 12.7 | - |
lactose | 15°C, recombinant mutant BgaS6, i.e.E229D/V405A/G803D | Arthrobacter sp. |
EC Number | Metals/Ions | Comment | Organism | Structure |
---|---|---|---|---|
3.2.1.23 | Mg2+ | the enzyme requires metal ions, Mg2+ or Mn2+ can restore the enzyme activity of recombinant wild-type and mutant apoenzymes, but not Ca2+, Cu2+, and Na+, overview | Arthrobacter sp. | |
3.2.1.23 | Mn2+ | the enzyme requires metal ions, Mg2+ or Mn2+ can restore the enzyme activity of recombinant wild-type and mutant apoenzymes, but not Ca2+, Cu2+, and Na+, overview | Arthrobacter sp. |
EC Number | Natural Substrates | Organism | Comment (Nat. Sub.) | Natural Products | Comment (Nat. Pro.) | Rev. | Reac. |
---|---|---|---|---|---|---|---|
3.2.1.23 | lactose + H2O | Arthrobacter sp. | - |
D-glucose + D-galactose | - |
? | |
3.2.1.23 | lactose + H2O | Arthrobacter sp. SB | - |
D-glucose + D-galactose | - |
? |
EC Number | Organism | UniProt | Comment | Textmining |
---|---|---|---|---|
3.2.1.23 | Arthrobacter sp. | - |
gene bgaS encoding a cold-active enzyme | - |
3.2.1.23 | Arthrobacter sp. SB | - |
gene bgaS encoding a cold-active enzyme | - |
EC Number | Specific Activity Minimum [µmol/min/mg] | Specific Activity Maximum [µmol/min/mg] | Comment | Organism |
---|---|---|---|---|
3.2.1.23 | additional information | - |
substrate specificity of recombinant wild-type and mutant enzymes, overview | Arthrobacter sp. |
EC Number | Substrates | Comment Substrates | Organism | Products | Comment (Products) | Rev. | Reac. |
---|---|---|---|---|---|---|---|
3.2.1.23 | 2-nitrophenyl beta-D-galactopyranoside + H2O | - |
Arthrobacter sp. | 2-nitrophenol + beta-D-galactose | - |
? | |
3.2.1.23 | 2-nitrophenyl beta-D-galactopyranoside + H2O | - |
Arthrobacter sp. SB | 2-nitrophenol + beta-D-galactose | - |
? | |
3.2.1.23 | 4-nitrophenyl beta-D-galactopyranoside + H2O | - |
Arthrobacter sp. | 4-nitrophenol + beta-D-galactose | - |
? | |
3.2.1.23 | 4-nitrophenyl beta-D-galactopyranoside + H2O | - |
Arthrobacter sp. SB | 4-nitrophenol + beta-D-galactose | - |
? | |
3.2.1.23 | 5-bromo-4-chloro-3-indolyl-beta-D-galactopyranoside + H2O | - |
Arthrobacter sp. | 5-bromo-4-chloroindol + beta-D-galactose | - |
? | |
3.2.1.23 | 5-bromo-4-chloro-3-indolyl-beta-D-galactopyranoside + H2O | - |
Arthrobacter sp. SB | 5-bromo-4-chloroindol + beta-D-galactose | - |
? | |
3.2.1.23 | lactose + H2O | - |
Arthrobacter sp. | D-glucose + D-galactose | - |
? | |
3.2.1.23 | lactose + H2O | - |
Arthrobacter sp. SB | D-glucose + D-galactose | - |
? | |
3.2.1.23 | additional information | substrate specificity of recombinant wild-type and mutant enzymes, overview | Arthrobacter sp. | ? | - |
? | |
3.2.1.23 | additional information | substrate specificity of recombinant wild-type and mutant enzymes, overview | Arthrobacter sp. SB | ? | - |
? |
EC Number | Subunits | Comment | Organism |
---|---|---|---|
3.2.1.23 | tetramer | three-dimensional structure modeling of BgaS, homotetramer that forms a diamond shape with two axes: a long interface and an activating interface, overview | Arthrobacter sp. |
EC Number | Synonyms | Comment | Organism |
---|---|---|---|
3.2.1.23 | BgaS | - |
Arthrobacter sp. |
EC Number | Temperature Optimum [°C] | Temperature Optimum Maximum [°C] | Comment | Organism |
---|---|---|---|---|
3.2.1.23 | - |
20 | assay at, cold-active enzyme | Arthrobacter sp. |
EC Number | Temperature Minimum [°C] | Temperature Maximum [°C] | Comment | Organism |
---|---|---|---|---|
3.2.1.23 | - |
20 | - |
Arthrobacter sp. |
EC Number | Temperature Stability Minimum [°C] | Temperature Stability Maximum [°C] | Comment | Organism |
---|---|---|---|---|
3.2.1.23 | additional information | - |
thermostability of recombinant wild-type and mutant enzymes, overview | Arthrobacter sp. |
3.2.1.23 | 30 | - |
BgaS, mutant BgaS7, and mutant BgaS6 loose all detectable activity after 75, 90, and 120 min, respectively | Arthrobacter sp. |
3.2.1.23 | 37 | - |
10 min, inactivation | Arthrobacter sp. |
3.2.1.23 | 60 | - |
10 min, inactivation | Arthrobacter sp. |
EC Number | Turnover Number Minimum [1/s] | Turnover Number Maximum [1/s] | Substrate | Comment | Organism | Structure |
---|---|---|---|---|---|---|
3.2.1.23 | 4.1 | - |
lactose | 15°C, recombinant mutant BgaS7, i.e. E229D/V405A | Arthrobacter sp. | |
3.2.1.23 | 5.3 | - |
lactose | 15°C, recombinant wild-type BgaS | Arthrobacter sp. | |
3.2.1.23 | 18.7 | - |
lactose | 15°C, recombinant mutant BgaS6, i.e.E229D/V405A/G803D | Arthrobacter sp. |
EC Number | Ki Value [mM] | Ki Value maximum [mM] | Inhibitor | Comment | Organism | Structure |
---|---|---|---|---|---|---|
3.2.1.23 | additional information | - |
additional information | temperature dependence of inhibition kinetics of wild-type and mutant enzymes, overview | Arthrobacter sp. |