EC Number | Cloned (Comment) | Organism |
---|---|---|
3.2.1.55 | DNA and amino acid sequence determination and analysis, overexpression of the C-terminally His-tagged enzyme in Lactococcus lactis NZ9000 under control of nisin-inducible nisA promotor | Bifidobacterium longum |
EC Number | Inhibitors | Comment | Organism | Structure |
---|---|---|---|---|
3.2.1.55 | Cu2+ | - |
Bifidobacterium longum | |
3.2.1.55 | Hg2+ | - |
Bifidobacterium longum | |
3.2.1.55 | additional information | not affected by chelating or reducing agents | Bifidobacterium longum | |
3.2.1.55 | Zn2+ | - |
Bifidobacterium longum |
EC Number | KM Value [mM] | KM Value Maximum [mM] | Substrate | Comment | Organism | Structure |
---|---|---|---|---|---|---|
3.2.1.55 | 0.295 | - |
4-nitrophenyl-alpha-L-arabinofuranoside | pH 6.0, 45°C | Bifidobacterium longum |
EC Number | Molecular Weight [Da] | Molecular Weight Maximum [Da] | Comment | Organism |
---|---|---|---|---|
3.2.1.55 | 64000 | - |
4 * 64000, SDS-PAGE | Bifidobacterium longum |
3.2.1.55 | 260000 | - |
detagged enzyme, gel filtration | Bifidobacterium longum |
EC Number | Natural Substrates | Organism | Comment (Nat. Sub.) | Natural Products | Comment (Nat. Pro.) | Rev. | Reac. |
---|---|---|---|---|---|---|---|
3.2.1.55 | additional information | Bifidobacterium longum | enzyme might have a role in the degradation of L-arabinose-containing polysaccharides together with other glycosidases | ? | - |
? | |
3.2.1.55 | additional information | Bifidobacterium longum B667 | enzyme might have a role in the degradation of L-arabinose-containing polysaccharides together with other glycosidases | ? | - |
? |
EC Number | Organism | UniProt | Comment | Textmining |
---|---|---|---|---|
3.2.1.55 | Bifidobacterium longum | Q841V6 | - |
- |
3.2.1.55 | Bifidobacterium longum B667 | Q841V6 | - |
- |
EC Number | Purification (Comment) | Organism |
---|---|---|
3.2.1.55 | recombinant His-tagged enzyme from Lactococcus lactis by Ni2+-chelate affinity chromatography | Bifidobacterium longum |
EC Number | Reaction | Comment | Organism | Reaction ID |
---|---|---|---|---|
3.2.1.55 | 1,5-alpha-L-arabinofuranohexaose + 5 H2O = 6 alpha-L-arabinofuranose | exo-acting enzyme | Bifidobacterium longum |
EC Number | Substrates | Comment Substrates | Organism | Products | Comment (Products) | Rev. | Reac. |
---|---|---|---|---|---|---|---|
3.2.1.55 | 4-nitrophenyl alpha-L-arabinofuranoside + H2O | - |
Bifidobacterium longum | 4-nitrophenol + alpha-L-arabinofuranose | - |
? | |
3.2.1.55 | 4-nitrophenyl alpha-L-arabinofuranoside + H2O | - |
Bifidobacterium longum B667 | 4-nitrophenol + alpha-L-arabinofuranose | - |
? | |
3.2.1.55 | alpha-(1->5)-L-arabinofuranotriose + H2O | - |
Bifidobacterium longum | alpha-L-arabinofuranose | - |
? | |
3.2.1.55 | alpha-L-arabinofuranobiose + H2O | - |
Bifidobacterium longum | alpha-L-arabinofuranose | - |
? | |
3.2.1.55 | alpha-L-arabinofuranobiose + H2O | - |
Bifidobacterium longum B667 | alpha-L-arabinofuranose | - |
? | |
3.2.1.55 | alpha-L-arabinofuranopentaose + H2O | - |
Bifidobacterium longum | alpha-L-arabinofuranose | - |
? | |
3.2.1.55 | alpha-L-arabinofuranopentaose + H2O | - |
Bifidobacterium longum B667 | alpha-L-arabinofuranose | - |
? | |
3.2.1.55 | alpha-L-arabinofuranoptetraose + H2O | - |
Bifidobacterium longum | alpha-L-arabinofuranose | - |
? | |
3.2.1.55 | arabinan + H2O | - |
Bifidobacterium longum | alpha-L-arabinose + ? | - |
? | |
3.2.1.55 | arabinoxylan + H2O | - |
Bifidobacterium longum | alpha-L-arabinose + ? | - |
? | |
3.2.1.55 | additional information | enzyme might have a role in the degradation of L-arabinose-containing polysaccharides together with other glycosidases | Bifidobacterium longum | ? | - |
? | |
3.2.1.55 | additional information | substrate specificity, no endoarabinanase activity | Bifidobacterium longum | ? | - |
? | |
3.2.1.55 | additional information | enzyme might have a role in the degradation of L-arabinose-containing polysaccharides together with other glycosidases | Bifidobacterium longum B667 | ? | - |
? | |
3.2.1.55 | additional information | substrate specificity, no endoarabinanase activity | Bifidobacterium longum B667 | ? | - |
? |
EC Number | Subunits | Comment | Organism |
---|---|---|---|
3.2.1.55 | tetramer | 4 * 64000, SDS-PAGE | Bifidobacterium longum |
EC Number | Synonyms | Comment | Organism |
---|---|---|---|
3.2.1.55 | AbfB | - |
Bifidobacterium longum |
3.2.1.55 | alpha-L-arabinofuranosidase | - |
Bifidobacterium longum |
3.2.1.55 | More | enzyme belongs to the family 51 of glycosidases | Bifidobacterium longum |
EC Number | Temperature Optimum [°C] | Temperature Optimum Maximum [°C] | Comment | Organism |
---|---|---|---|---|
3.2.1.55 | 45 | - |
- |
Bifidobacterium longum |
EC Number | Temperature Minimum [°C] | Temperature Maximum [°C] | Comment | Organism |
---|---|---|---|---|
3.2.1.55 | 20 | 70 | - |
Bifidobacterium longum |
EC Number | Temperature Stability Minimum [°C] | Temperature Stability Maximum [°C] | Comment | Organism |
---|---|---|---|---|
3.2.1.55 | 55 | - |
half-life: 3 h | Bifidobacterium longum |
EC Number | pH Optimum Minimum | pH Optimum Maximum | Comment | Organism |
---|---|---|---|---|
3.2.1.55 | 6 | - |
- |
Bifidobacterium longum |
EC Number | pH Minimum | pH Maximum | Comment | Organism |
---|---|---|---|---|
3.2.1.55 | 4.5 | 7.5 | - |
Bifidobacterium longum |