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