Activating Compound | Comment | Organism | Structure |
---|---|---|---|
DTT | 23% activation at 5 mM | Streptomyces thermocarboxydus | |
Triton X-100 | 42% activation at 0.5% | Streptomyces thermocarboxydus | |
Tween-80 | 38% activation at 0.5% | Streptomyces thermocarboxydus |
Cloned (Comment) | Organism |
---|---|
gene xylG, DNA and amino acid sequence determination and analysis, expression of His-tagged enzyme in Escherichia coli strain BL21 | Streptomyces thermocarboxydus |
Inhibitors | Comment | Organism | Structure |
---|---|---|---|
Ca2+ | 7% inhibition at 1 mM | Streptomyces thermocarboxydus | |
Cu2+ | 77% inhibition at 1 mM | Streptomyces thermocarboxydus | |
EDTA | 59% inhibition at 5 mM | Streptomyces thermocarboxydus | |
Hg2+ | complete inhibition at 1 mM | Streptomyces thermocarboxydus | |
iodoacetamide | 59% inhibition at 5 mM | Streptomyces thermocarboxydus | |
N-bromosuccimide | complete inhibition at 5 mM | Streptomyces thermocarboxydus | |
NEM | 49% inhibition at 5 mM | Streptomyces thermocarboxydus | |
Sodium azide | 43% inhibition at 5 mM | Streptomyces thermocarboxydus |
KM Value [mM] | KM Value Maximum [mM] | Substrate | Comment | Organism | Structure |
---|---|---|---|---|---|
additional information | - |
additional information | Michaelis-Menten kinetics | Streptomyces thermocarboxydus |
Metals/Ions | Comment | Organism | Structure |
---|---|---|---|
Co2+ | 27% activation at 1 mM | Streptomyces thermocarboxydus | |
Fe2+ | 16% activation at 1 mM | Streptomyces thermocarboxydus | |
Mn2+ | 42% activation at 1 mM | Streptomyces thermocarboxydus | |
additional information | no effect by Ca2+, Sn2+, Ba2+, Ni2+, Zn2+, and Mg2+ at 1 mM, and by 2-mercaptoethanol at 5 mM | Streptomyces thermocarboxydus |
Molecular Weight [Da] | Molecular Weight Maximum [Da] | Comment | Organism |
---|---|---|---|
43962 | - |
x * 43962, sequence calculation | Streptomyces thermocarboxydus |
Natural Substrates | Organism | Comment (Nat. Sub.) | Natural Products | Comment (Nat. Pro.) | Rev. | Reac. |
---|---|---|---|---|---|---|
beta-1,4-xylan + H2O | Streptomyces thermocarboxydus | - |
? | - |
? | |
beta-1,4-xylan + H2O | Streptomyces thermocarboxydus HY-15 | - |
? | - |
? |
Organism | UniProt | Comment | Textmining |
---|---|---|---|
Streptomyces thermocarboxydus | C6ZHB0 | isolated from the gut of Eisenia fetida, gene xylG | - |
Streptomyces thermocarboxydus HY-15 | C6ZHB0 | isolated from the gut of Eisenia fetida, gene xylG | - |
Purification (Comment) | Organism |
---|---|
recombinant His-tagged enzyme from Escherichia coli strain BVL21 by affinity chromatography | Streptomyces thermocarboxydus |
Specific Activity Minimum [µmol/min/mg] | Specific Activity Maximum [µmol/min/mg] | Comment | Organism |
---|---|---|---|
additional information | - |
substrate specificity, overview | Streptomyces thermocarboxydus |
70.3 | - |
purified enzyme, substrate is xylan from birchwood | Streptomyces thermocarboxydus |
Substrates | Comment Substrates | Organism | Products | Comment (Products) | Rev. | Reac. |
---|---|---|---|---|---|---|
4-nitrophenyl cellobioside + H2O | high activity | Streptomyces thermocarboxydus | 4-nitrophenol + cellobiose | - |
? | |
4-nitrophenyl cellobioside + H2O | high activity | Streptomyces thermocarboxydus HY-15 | 4-nitrophenol + cellobiose | - |
? | |
beta-1,4-xylan + H2O | - |
Streptomyces thermocarboxydus | ? | - |
? | |
beta-1,4-xylan + H2O | from oat spelt, birchwood, or beechwood in descending order | Streptomyces thermocarboxydus | ? | - |
? | |
beta-1,4-xylan + H2O | - |
Streptomyces thermocarboxydus HY-15 | ? | - |
? | |
beta-1,4-xylan + H2O | from oat spelt, birchwood, or beechwood in descending order | Streptomyces thermocarboxydus HY-15 | ? | - |
? | |
additional information | substrate specificity, overview | Streptomyces thermocarboxydus | ? | - |
? | |
additional information | substrate specificity, overview | Streptomyces thermocarboxydus HY-15 | ? | - |
? |
Subunits | Comment | Organism |
---|---|---|
? | x * 43962, sequence calculation | Streptomyces thermocarboxydus |
More | structure homology modelling, XylG folds to form an (alpha/beta)8-barrel with two catalytic residues of an acid/base Glu181 and a nucleophile Glu289. The formation of a disulfide bond between Cys321 and Cys327 is predicted by homology modeling | Streptomyces thermocarboxydus |
Synonyms | Comment | Organism |
---|---|---|
GH10 endo-beta-1,4-xylanase | - |
Streptomyces thermocarboxydus |
More | the enzyme belongs to the glycosyl hydrolase family 10, GH10 | Streptomyces thermocarboxydus |
XylG | - |
Streptomyces thermocarboxydus |
Temperature Optimum [°C] | Temperature Optimum Maximum [°C] | Comment | Organism |
---|---|---|---|
55 | - |
recombinant enzyme | Streptomyces thermocarboxydus |
Temperature Minimum [°C] | Temperature Maximum [°C] | Comment | Organism |
---|---|---|---|
35 | 75 | activity range | Streptomyces thermocarboxydus |
pH Optimum Minimum | pH Optimum Maximum | Comment | Organism |
---|---|---|---|
6 | - |
recombinant enzyme | Streptomyces thermocarboxydus |
pH Minimum | pH Maximum | Comment | Organism |
---|---|---|---|
4.5 | 10.5 | activity range, over 85% of its maximum activity at a pH range of pH 5.0 to pH 6.5 | Streptomyces thermocarboxydus |
Organism | Comment | pI Value Maximum | pI Value |
---|---|---|---|
Streptomyces thermocarboxydus | sequence calculation | - |
6.74 |