EC Number | KM Value [mM] | KM Value Maximum [mM] | Substrate | Comment | Organism | Structure |
---|---|---|---|---|---|---|
3.2.1.37 | 0.4 | - |
p-nitrophenyl beta-D-xyloside | - |
Ruminiclostridium cellulolyticum |
EC Number | Molecular Weight [Da] | Molecular Weight Maximum [Da] | Comment | Organism |
---|---|---|---|---|
3.2.1.37 | 43000 | - |
SDS-PAGE | Ruminiclostridium cellulolyticum |
EC Number | Natural Substrates | Organism | Comment (Nat. Sub.) | Natural Products | Comment (Nat. Pro.) | Rev. | Reac. |
---|---|---|---|---|---|---|---|
3.2.1.37 | xylan + H2O | Ruminiclostridium cellulolyticum | low activity | beta-D-xylose + ? | - |
? | |
3.2.1.37 | xylan + H2O | Ruminiclostridium cellulolyticum | complete degration of xylan requires synergistic action of two types of enzyme, endo-1,4-xylanase to form xylooligosaccharides and beta-D-xylosidase, which hydrolyses xylooligosaccharides to xylose | beta-D-xylose + ? | - |
? | |
3.2.1.37 | xylobiose + H2O | Ruminiclostridium cellulolyticum | - |
beta-D-xylose + D-xylose | - |
? |
EC Number | Organism | UniProt | Comment | Textmining |
---|---|---|---|---|
3.2.1.37 | Ruminiclostridium cellulolyticum | - |
- |
- |
EC Number | Purification (Comment) | Organism |
---|---|---|
3.2.1.37 | to homogeneity by 3step chromatography techniques | Ruminiclostridium cellulolyticum |
EC Number | Source Tissue | Comment | Organism | Textmining |
---|---|---|---|---|
3.2.1.37 | cell culture | enzyme production most induced in xylan medium | Ruminiclostridium cellulolyticum | - |
EC Number | Specific Activity Minimum [µmol/min/mg] | Specific Activity Maximum [µmol/min/mg] | Comment | Organism |
---|---|---|---|---|
3.2.1.37 | 15.1 | - |
- |
Ruminiclostridium cellulolyticum |
EC Number | Substrates | Comment Substrates | Organism | Products | Comment (Products) | Rev. | Reac. |
---|---|---|---|---|---|---|---|
3.2.1.37 | p-nitrophenyl alpha-L-arabinofuranoside + H2O | low activity | Ruminiclostridium cellulolyticum | p-nitrophenol + alpha-L-arabinofuranose | - |
? | |
3.2.1.37 | p-nitrophenyl beta-D-xylopyranoside + H2O | - |
Ruminiclostridium cellulolyticum | p-nitrophenol + beta-D-xylopyranose | - |
? | |
3.2.1.37 | xylan + H2O | low activity | Ruminiclostridium cellulolyticum | beta-D-xylose + ? | - |
? | |
3.2.1.37 | xylan + H2O | complete degration of xylan requires synergistic action of two types of enzyme, endo-1,4-xylanase to form xylooligosaccharides and beta-D-xylosidase, which hydrolyses xylooligosaccharides to xylose | Ruminiclostridium cellulolyticum | beta-D-xylose + ? | - |
? | |
3.2.1.37 | xylobiose + H2O | - |
Ruminiclostridium cellulolyticum | beta-D-xylose + D-xylose | - |
? | |
3.2.1.37 | xylopentaose + H2O | extend of hydrolysis varies with chain length of the substrate | Ruminiclostridium cellulolyticum | beta-D-xylose + ? | - |
? | |
3.2.1.37 | xylotetraose + H2O | acts by inverting the anomeric configuration | Ruminiclostridium cellulolyticum | xylotriose + beta-D-xylose | - |
? | |
3.2.1.37 | xylotriose + H2O | - |
Ruminiclostridium cellulolyticum | beta-D-xylose + xylobiose | - |
? |
EC Number | Subunits | Comment | Organism |
---|---|---|---|
3.2.1.37 | monomer | 1 * 43000, SDS-PAGE | Ruminiclostridium cellulolyticum |
EC Number | Temperature Optimum [°C] | Temperature Optimum Maximum [°C] | Comment | Organism |
---|---|---|---|---|
3.2.1.37 | 35 | - |
- |
Ruminiclostridium cellulolyticum |
EC Number | pH Optimum Minimum | pH Optimum Maximum | Comment | Organism |
---|---|---|---|---|
3.2.1.37 | 7.5 | - |
- |
Ruminiclostridium cellulolyticum |
EC Number | pH Stability | pH Stability Maximum | Comment | Organism |
---|---|---|---|---|
3.2.1.37 | 6 | - |
no activity below | Ruminiclostridium cellulolyticum |