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Literature summary for 3.2.1.8 extracted from
- Purification and characterization of two endo-1,4-b-xylanases from Antarctic krill, Euphausia superba Dana (2000), Comp. Biochem. Physiol. B, 127, 325-335.
Activating Compound
| Activating Compound | Comment | Organism | Structure |
|---|---|---|---|
| additional information | activity is not affected by L-cysteine and 1,1-dithioerythreitol | Euphausia superba |
General Stability
| General Stability | Organism |
|---|---|
| Ca2+, Mg2+, DTT, L-cysteine, soybean trypsin inhibitor, PMSF, as well as a 17 kDa component from krill extract, stabilize the isozymes A and B | Euphausia superba |
Inhibitors
| Inhibitors | Comment | Organism | Structure |
|---|---|---|---|
| Co2+ | - |
Euphausia superba |  |
| Cu2+ | - |
Euphausia superba | |
| iodoacetate | isozymes A and B | Euphausia superba | |
| Mn2+ | - |
Euphausia superba | |
| additional information | activity is not affected by L-cysteine and 1,1-dithioerythreitol | Euphausia superba | |
| N-bromosuccinimide | strong inhibition, isozymes A and B | Euphausia superba | |
| p-chloromercuribenzoate | isozymes A and B | Euphausia superba | |
| Zn2+ | - |
Euphausia superba | |
KM Value [mM]
| KM Value [mM] | KM Value Maximum [mM] | Substrate | Comment | Organism | Structure |
|---|---|---|---|---|---|
| additional information | - |
additional information | - |
Euphausia superba |
Metals/Ions
| Metals/Ions | Comment | Organism | Structure |
|---|---|---|---|
| Ca2+ | activation of isozymes A and B | Euphausia superba | |
| Mg2+ | activation of isozymes A and B | Euphausia superba | |
| PMSF | activation of isozymes A and B | Euphausia superba | |
| Soybean trypsin inhibitor | activation of isozymes A and B | Euphausia superba |
Molecular Weight [Da]
| Molecular Weight [Da] | Molecular Weight Maximum [Da] | Comment | Organism |
|---|---|---|---|
| 25000 | - |
isozyme B, gel filtration | Euphausia superba |
| 45000 | - |
isozyme A, gel filtration | Euphausia superba |
Organism
| Organism | UniProt | Comment | Textmining |
|---|---|---|---|
| Euphausia superba | - |
from krill, 2 isozymes A and B | - |
Purification (Commentary)
| Purification (Comment) | Organism |
|---|---|
| isozymes A, 118fold, and B, 82fold | Euphausia superba |
Specific Activity [micromol/min/mg]
| Specific Activity Minimum [µmol/min/mg] | Specific Activity Maximum [µmol/min/mg] | Comment | Organism |
|---|---|---|---|
| 4780 | - |
purified isozyme B | Euphausia superba |
| 6820 | - |
purified isozyme A | Euphausia superba |
Storage Stability
| Storage Stability | Organism |
|---|---|
| unstable enzyme | Euphausia superba |
Substrates and Products (Substrate)
| Substrates | Comment Substrates | Organism | Products | Comment (Products) | Rev. | Reac. |
|---|---|---|---|---|---|---|
| 4-nitrophenyl beta-D-xylopyranoside + H2O | beta-xylosidase activity | Euphausia superba | 4-nitrophenol + beta-D-xylopyranose | - |
? | |
| xylan + H2O | from oat spelt | Euphausia superba | D-xylose + ? | - |
? | |
Synonyms
| Synonyms | Comment | Organism |
|---|---|---|
| (1-4)-beta-xylan 4-xylanohydrolase | - |
Euphausia superba |
| 1,4-beta-xylan xylanohydrolase | - |
Euphausia superba |
| beta-1,4-xylan xylanohydrolase | - |
Euphausia superba |
| beta-1,4-xylanase | - |
Euphausia superba |
| beta-D-xylanase | - |
Euphausia superba |
| beta-xylanase | - |
Euphausia superba |
| endo(1-4)beta-xylanase | - |
Euphausia superba |
| endo-1,4-beta-D-xylanase | - |
Euphausia superba |
| endo-1,4-beta-xylanase | - |
Euphausia superba |
| endo-1,4-xylanase | - |
Euphausia superba |
| endo-beta-1,4-xylanase | - |
Euphausia superba |
| xylanase | - |
Euphausia superba |
Temperature Optimum [°C]
| Temperature Optimum [°C] | Temperature Optimum Maximum [°C] | Comment | Organism |
|---|---|---|---|
| 37 | 40 | isozymes A and B | Euphausia superba |
Temperature Stability [°C]
| Temperature Stability Minimum [°C] | Temperature Stability Maximum [°C] | Comment | Organism |
|---|---|---|---|
| additional information | - |
very low thermostability of isozymes A and B | Euphausia superba |
| 25 | - |
stable up to for at least 10 min, rapid inactivation above, isozymes A and B | Euphausia superba |
| 45 | - |
complete loss of activity within 5 min, isozymes A and B | Euphausia superba |
pH Optimum
| pH Optimum Minimum | pH Optimum Maximum | Comment | Organism |
|---|---|---|---|
| 5.7 | 6 | isozymes A and B | Euphausia superba |
pH Stability
| pH Stability | pH Stability Maximum | Comment | Organism |
|---|---|---|---|
| 5 | 7.5 | isozymes A and B | Euphausia superba |
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