Any feedback?
Literature summary for 3.2.1.55 extracted from
- Purification and functional characterization of a novel alpha-L-arabinofuranosidase from Bifidobacterium longum B667 (2003), Appl. Environ. Microbiol., 69, 5096-5103.
Cloned(Commentary)
| Cloned (Comment) | Organism |
|---|---|
| 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 |
Inhibitors
| Inhibitors | Comment | Organism | Structure |
|---|---|---|---|
| Cu2+ | - |
Bifidobacterium longum |  |
| Hg2+ | - |
Bifidobacterium longum | |
| additional information | not affected by chelating or reducing agents | Bifidobacterium longum | |
| Zn2+ | - |
Bifidobacterium longum | |
KM Value [mM]
| KM Value [mM] | KM Value Maximum [mM] | Substrate | Comment | Organism | Structure |
|---|---|---|---|---|---|
| 0.295 | - |
4-nitrophenyl-alpha-L-arabinofuranoside | pH 6.0, 45°C | Bifidobacterium longum | |
Molecular Weight [Da]
| Molecular Weight [Da] | Molecular Weight Maximum [Da] | Comment | Organism |
|---|---|---|---|
| 64000 | - |
4 * 64000, SDS-PAGE | Bifidobacterium longum |
| 260000 | - |
detagged enzyme, gel filtration | Bifidobacterium longum |
Natural Substrates/ Products (Substrates)
| Natural Substrates | Organism | Comment (Nat. Sub.) | Natural Products | Comment (Nat. Pro.) | Rev. | Reac. |
|---|---|---|---|---|---|---|
| additional information | Bifidobacterium longum | enzyme might have a role in the degradation of L-arabinose-containing polysaccharides together with other glycosidases | ? | - |
? | |
| additional information | Bifidobacterium longum B667 | enzyme might have a role in the degradation of L-arabinose-containing polysaccharides together with other glycosidases | ? | - |
? | |
Organism
| Organism | UniProt | Comment | Textmining |
|---|---|---|---|
| Bifidobacterium longum | Q841V6 | - |
- |
| Bifidobacterium longum B667 | Q841V6 | - |
- |
Purification (Commentary)
| Purification (Comment) | Organism |
|---|---|
| recombinant His-tagged enzyme from Lactococcus lactis by Ni2+-chelate affinity chromatography | Bifidobacterium longum |
Reaction
| Reaction | Comment | Organism | Reaction ID |
|---|---|---|---|
| 1,5-alpha-L-arabinofuranohexaose + 5 H2O = 6 alpha-L-arabinofuranose | exo-acting enzyme | Bifidobacterium longum |
Substrates and Products (Substrate)
| Substrates | Comment Substrates | Organism | Products | Comment (Products) | Rev. | Reac. |
|---|---|---|---|---|---|---|
| 4-nitrophenyl alpha-L-arabinofuranoside + H2O | - |
Bifidobacterium longum | 4-nitrophenol + alpha-L-arabinofuranose | - |
? | |
| 4-nitrophenyl alpha-L-arabinofuranoside + H2O | - |
Bifidobacterium longum B667 | 4-nitrophenol + alpha-L-arabinofuranose | - |
? | |
| alpha-(1->5)-L-arabinofuranotriose + H2O | - |
Bifidobacterium longum | alpha-L-arabinofuranose | - |
? | |
| alpha-L-arabinofuranobiose + H2O | - |
Bifidobacterium longum | alpha-L-arabinofuranose | - |
? | |
| alpha-L-arabinofuranobiose + H2O | - |
Bifidobacterium longum B667 | alpha-L-arabinofuranose | - |
? | |
| alpha-L-arabinofuranopentaose + H2O | - |
Bifidobacterium longum | alpha-L-arabinofuranose | - |
? | |
| alpha-L-arabinofuranopentaose + H2O | - |
Bifidobacterium longum B667 | alpha-L-arabinofuranose | - |
? | |
| alpha-L-arabinofuranoptetraose + H2O | - |
Bifidobacterium longum | alpha-L-arabinofuranose | - |
? | |
| arabinan + H2O | - |
Bifidobacterium longum | alpha-L-arabinose + ? | - |
? | |
| arabinoxylan + H2O | - |
Bifidobacterium longum | alpha-L-arabinose + ? | - |
? | |
| additional information | enzyme might have a role in the degradation of L-arabinose-containing polysaccharides together with other glycosidases | Bifidobacterium longum | ? | - |
? | |
| additional information | substrate specificity, no endoarabinanase activity | Bifidobacterium longum | ? | - |
? | |
| additional information | enzyme might have a role in the degradation of L-arabinose-containing polysaccharides together with other glycosidases | Bifidobacterium longum B667 | ? | - |
? | |
| additional information | substrate specificity, no endoarabinanase activity | Bifidobacterium longum B667 | ? | - |
? | |
Subunits
| Subunits | Comment | Organism |
|---|---|---|
| tetramer | 4 * 64000, SDS-PAGE | Bifidobacterium longum |
Synonyms
| Synonyms | Comment | Organism |
|---|---|---|
| AbfB | - |
Bifidobacterium longum |
| alpha-L-arabinofuranosidase | - |
Bifidobacterium longum |
| More | enzyme belongs to the family 51 of glycosidases | Bifidobacterium longum |
Temperature Optimum [°C]
| Temperature Optimum [°C] | Temperature Optimum Maximum [°C] | Comment | Organism |
|---|---|---|---|
| 45 | - |
- |
Bifidobacterium longum |
Temperature Range [°C]
| Temperature Minimum [°C] | Temperature Maximum [°C] | Comment | Organism |
|---|---|---|---|
| 20 | 70 | - |
Bifidobacterium longum |
Temperature Stability [°C]
| Temperature Stability Minimum [°C] | Temperature Stability Maximum [°C] | Comment | Organism |
|---|---|---|---|
| 55 | - |
half-life: 3 h | Bifidobacterium longum |
pH Optimum
| pH Optimum Minimum | pH Optimum Maximum | Comment | Organism |
|---|---|---|---|
| 6 | - |
- |
Bifidobacterium longum |
pH Range
| pH Minimum | pH Maximum | Comment | Organism |
|---|---|---|---|
| 4.5 | 7.5 | - |
Bifidobacterium longum |
Use of this online version of BRENDA is free under the CC BY 4.0 license. See terms of use for full details.
Release 2023.1 (January 2023)
Legal
Curated at
Member of
