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Literature summary extracted from
- A xylanase with high pH stability from Streptomyces sp. S27 and its carbohydrate-binding module with/without linker-region-truncated versions (2009), Appl. Microbiol. Biotechnol., 83, 99-107.
Activating Compound
| EC Number | Activating Compound | Comment | Organism | Structure |
|---|---|---|---|---|
| 3.2.1.8 | beta-mercaptoethanol | 10 mM enhances the activities of XynAS27, XynAS27cd, and XynAS27cdl by about 1.5, 1.7, and 1.4fold, respectively | Streptomyces sp. S27 |  |
Application
| EC Number | Application | Comment | Organism |
|---|---|---|---|
| 3.2.1.8 | industry | XynAS27 may be a compelling tool for the food industry because it generates xylobiose (85% w/w) as the main product of xylan hydrolysis | Streptomyces sp. S27 |
Cloned(Commentary)
| EC Number | Cloned (Comment) | Organism |
|---|---|---|
| 3.2.1.8 | intact, CBM-truncated and CBM-linker-truncated versions cloned into vector pET-22b(+) and expressed in Escherichia coli BL21 (DE3) | Streptomyces sp. S27 |
Protein Variants
| EC Number | Protein Variants | Comment | Organism |
|---|---|---|---|
| 3.2.1.8 | additional information | truncated versions xynAS27cd (CBM-linker-truncated version) and xynAS27cdl (CBM-truncated version) show less pH and thermal stability, and less affinity and hydrolytic activity to insoluble substrate than the intact one | Streptomyces sp. S27 |
Inhibitors
| EC Number | Inhibitors | Comment | Organism | Structure |
|---|---|---|---|---|
| 3.2.1.8 | Ag+ | 1 mM inhibits about 60% of the activity of XynAS27, and less than 20% of the activities of XynAS27cd and XynAS27cdl | Streptomyces sp. S27 | |
| 3.2.1.8 | Co2+ | 10 mM partially inhibits the activity of XynAS27 | Streptomyces sp. S27 | |
| 3.2.1.8 | Cu2+ | strongly inhibits | Streptomyces sp. S27 | |
| 3.2.1.8 | Fe3+ | 10 mM partially inhibits the activity of XynAS27 | Streptomyces sp. S27 | |
| 3.2.1.8 | Hg2+ | almost completely inhibits | Streptomyces sp. S27 | |
| 3.2.1.8 | Ni2+ | 10 mM partially inhibits the activity of XynAS27 | Streptomyces sp. S27 | |
| 3.2.1.8 | Pb2+ | 10 mM partially inhibits the activity of XynAS27 | Streptomyces sp. S27 | |
| 3.2.1.8 | SDS | almost completely inhibits | Streptomyces sp. S27 | |
| 3.2.1.8 | Zn2+ | 10 mM partially inhibits the activity of XynAS27 | Streptomyces sp. S27 | |
Molecular Weight [Da]
| EC Number | Molecular Weight [Da] | Molecular Weight Maximum [Da] | Comment | Organism |
|---|---|---|---|---|
| 3.2.1.8 | 33000 | - |
x * 47000, SDS-PAGE, XynAS27. x * 33000, SDS-PAGE, XynAS27cd. x * 34000, SDS-PAGE, XynAS27cdl | Streptomyces sp. S27 |
| 3.2.1.8 | 34000 | - |
x * 47000, SDS-PAGE, XynAS27. x * 33000, SDS-PAGE, XynAS27cd. x * 34000, SDS-PAGE, XynAS27cdl | Streptomyces sp. S27 |
| 3.2.1.8 | 47000 | - |
x * 47000, SDS-PAGE, XynAS27. x * 33000, SDS-PAGE, XynAS27cd. x * 34000, SDS-PAGE, XynAS27cdl | Streptomyces sp. S27 |
Organism
| EC Number | Organism | UniProt | Comment | Textmining |
|---|---|---|---|---|
| 3.2.1.8 | Streptomyces sp. S27 | C3RYK8 | - |
- |
Purification (Commentary)
| EC Number | Purification (Comment) | Organism |
|---|---|---|
| 3.2.1.8 | intact, CBM-truncated and CBM-linker-truncated versions of the mature proteins purified to electrophoretic homogeneity, by ion exchange chromatography or gel filtration | Streptomyces sp. S27 |
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 | 790.7 | - |
XynAS27 | Streptomyces sp. S27 |
| 3.2.1.8 | 1251 | - |
XynAS27cdl | Streptomyces sp. S27 |
| 3.2.1.8 | 1279 | - |
XynAS27cd | Streptomyces sp. S27 |
Substrates and Products (Substrate)
| EC Number | Substrates | Comment Substrates | Organism | Products | Comment (Products) | Rev. | Reac. |
|---|---|---|---|---|---|---|---|
| 3.2.1.8 | birchwood xylan + H2O | with soluble xylan after 12 h of incubation, about 15% (w/w) of the total reaction products is xylose, and 85% is xylobiose | Streptomyces sp. S27 | D-xylose + xylobiose + ? | - |
? | |
| 3.2.1.8 | additional information | carbohydrate-binding module (CBM) of XynAS27 plays a key role in the hydrolysis of insoluble substrate, and the CBM and linker region are also important for the enzyme stability, and the linker region contributes more | Streptomyces sp. S27 | ? | - |
? | |
| 3.2.1.8 | oat spelt xylan + H2O | with soluble xylan after 12 h of incubation, about 15% (w/w) of the total reaction products is xylose, and 85% is xylobiose. Comparing with the soluble xylan, the activities of XynAS27, XynAS27cd, and XynAS27cdl on insoluble xylan are lower, about 56%, 23% and 24% of the activities on soluble substrate, respectively | Streptomyces sp. S27 | D-xylose + xylobiose + ? | - |
? | |
Subunits
| EC Number | Subunits | Comment | Organism |
|---|---|---|---|
| 3.2.1.8 | ? | x * 47000, SDS-PAGE, XynAS27. x * 33000, SDS-PAGE, XynAS27cd. x * 34000, SDS-PAGE, XynAS27cdl | Streptomyces sp. S27 |
Synonyms
| EC Number | Synonyms | Comment | Organism |
|---|---|---|---|
| 3.2.1.8 | xylanase | - |
Streptomyces sp. S27 |
| 3.2.1.8 | XynAS27 | - |
Streptomyces sp. S27 |
pH Stability
| EC Number | pH Stability | pH Stability Maximum | Comment | Organism |
|---|---|---|---|---|
| 3.2.1.8 | 2.2 | 12 | - |
Streptomyces sp. S27 |
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