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Literature summary for 2.4.1.211 extracted from
- Directed evolution to enhance thermostability of galacto-N-biose/lacto-N-biose I phosphorylase (2013), Protein Eng. Des. Sel., 26, 755-761.
Cloned(Commentary)
| Cloned (Comment) | Organism |
|---|---|
| gene lnpA, sequence comparisons, recombinant expression of wild-type and mutant enzymes in Escherichia coli strain strain BL21 | Bifidobacterium longum subsp. Longum |
Crystallization (Commentary)
| Crystallization (Comment) | Organism |
|---|---|
| purified recombinant enzyme mutant C236Y, X-ray diffraction structure determination and analysis at 2.6 A resolution | Bifidobacterium longum subsp. Longum |
Protein Variants
| Protein Variants | Comment | Organism |
|---|---|---|
| C236E | random mutagenesis, the mutant shows decreased thermostability and reduced activity compared to the wild-type | Bifidobacterium longum subsp. Longum |
| C236F | random mutagenesis, the mutant shows highly increased thermostability and inacreased activity compared to the wild-type | Bifidobacterium longum subsp. Longum |
| C236H | random mutagenesis, the mutant shows slightly increased thermostability compared to the wild-type | Bifidobacterium longum subsp. Longum |
| C236P | random mutagenesis, the mutant shows highly increased thermostability and reduced activity compared to the wild-type | Bifidobacterium longum subsp. Longum |
| C236W | random mutagenesis, the mutant shows slightly increased thermostability compared to the wild-type | Bifidobacterium longum subsp. Longum |
| C236Y | random mutagenesis, the mutant shows highly increased thermostability and increased activity compared to the wild-type. In the mutant, the hydroxyl group of Tyr236 forms a hydrogen bond with the carboxyl group of E319. Mutant C236Y shows a 1.6fold higher specific activity than the wild-type | Bifidobacterium longum subsp. Longum |
| C236Y/D576V | random mutagenesis, the mutant shows highly increased thermostability compared to the wild-type | Bifidobacterium longum subsp. Longum |
| D576A | random mutagenesis, the mutant shows highly increased thermostability compared to the wild-type | Bifidobacterium longum subsp. Longum |
| D576F | random mutagenesis, the mutant shows highly increased thermostability and reduced activity compared to the wild-type | Bifidobacterium longum subsp. Longum |
| D576G | random mutagenesis, the mutant shows highly increased thermostability and increased activity compared to the wild-type | Bifidobacterium longum subsp. Longum |
| D576I | random mutagenesis, the mutant shows highly increased thermostability compared to the wild-type | Bifidobacterium longum subsp. Longum |
| D576L | random mutagenesis, the mutant shows highly increased thermostability compared to the wild-type | Bifidobacterium longum subsp. Longum |
| D576M | random mutagenesis, the mutant shows highly increased thermostability compared to the wild-type | Bifidobacterium longum subsp. Longum |
| D576P | random mutagenesis, the mutant shows decreased thermostability compared to the wild-type | Bifidobacterium longum subsp. Longum |
| D576V | random mutagenesis, the mutant shows highly increased thermostability compared to the wild-type | Bifidobacterium longum subsp. Longum |
| D576W | random mutagenesis, the mutant shows highly increased thermostability and reduced activity compared to the wild-type | Bifidobacterium longum subsp. Longum |
| G437S | random mutagenesis, the mutant shows slightly increased thermostability and slightly reducd activity compared to the wild-type | Bifidobacterium longum subsp. Longum |
| additional information | enzyme engineering for improved thermostability, random mutagenesis GLNBP library construction using error-prone polymerase chain reaction and mutant screening, overview | Bifidobacterium longum subsp. Longum |
| N506S | random mutagenesis, the mutant shows slightly increased thermostability and reduced activity compared to the wild-type | Bifidobacterium longum subsp. Longum |
| R290H | random mutagenesis, the mutant shows slightly increased thermostability and slightly reduced activity compared to the wild-type | Bifidobacterium longum subsp. Longum |
| R290H/G437S/N506S | random mutagenesis, the mutant shows highly increased thermostability and reduced activity compared to the wild-type | Bifidobacterium longum subsp. Longum |
Natural Substrates/ Products (Substrates)
| Natural Substrates | Organism | Comment (Nat. Sub.) | Natural Products | Comment (Nat. Pro.) | Rev. | Reac. |
|---|---|---|---|---|---|---|
| additional information | Bifidobacterium longum subsp. Longum | the enzyme reversibly phosphorolyzes galacto-N-biose (Galbeta1, 3GalNAc, GNB) and/or lacto-N-biose I (Galbeta1,3GlcNAc,LNB) to form alpha-galactose 1-phosphate (Gal1P) and the corresponding N-acetylhexosamine | ? | - |
? |  |
| additional information | Bifidobacterium longum subsp. Longum JCM 1217 | the enzyme reversibly phosphorolyzes galacto-N-biose (Galbeta1, 3GalNAc, GNB) and/or lacto-N-biose I (Galbeta1,3GlcNAc,LNB) to form alpha-galactose 1-phosphate (Gal1P) and the corresponding N-acetylhexosamine | ? | - |
? | |
Organism
| Organism | UniProt | Comment | Textmining |
|---|---|---|---|
| Bifidobacterium longum subsp. Longum | E8MF13 | gene lnpA, located in a gene cluster encoding a specific pathway for utilization of galacto-N-biose and lacto-N-biose | - |
| Bifidobacterium longum subsp. Longum JCM 1217 | E8MF13 | gene lnpA, located in a gene cluster encoding a specific pathway for utilization of galacto-N-biose and lacto-N-biose | - |
Substrates and Products (Substrate)
| Substrates | Comment Substrates | Organism | Products | Comment (Products) | Rev. | Reac. |
|---|---|---|---|---|---|---|
| additional information | the enzyme reversibly phosphorolyzes galacto-N-biose (Galbeta1, 3GalNAc, GNB) and/or lacto-N-biose I (Galbeta1,3GlcNAc,LNB) to form alpha-galactose 1-phosphate (Gal1P) and the corresponding N-acetylhexosamine | Bifidobacterium longum subsp. Longum | ? | - |
? | |
| additional information | the enzyme reversibly phosphorolyzes galacto-N-biose (Galbeta1, 3GalNAc, GNB) and/or lacto-N-biose I (Galbeta1,3GlcNAc,LNB) to form alpha-galactose 1-phosphate (Gal1P) and the corresponding N-acetylhexosamine | Bifidobacterium longum subsp. Longum JCM 1217 | ? | - |
? | |
Synonyms
| Synonyms | Comment | Organism |
|---|---|---|
| galacto-N-biose/lacto-N-biose I phosphorylase | - |
Bifidobacterium longum subsp. Longum |
| GLNBP | - |
Bifidobacterium longum subsp. Longum |
| GNB/LNB phosphorylase | - |
Bifidobacterium longum subsp. Longum |
Temperature Optimum [°C]
| Temperature Optimum [°C] | Temperature Optimum Maximum [°C] | Comment | Organism |
|---|---|---|---|
| 55 | - |
wild-type enzyme | Bifidobacterium longum subsp. Longum |
Temperature Range [°C]
| Temperature Minimum [°C] | Temperature Maximum [°C] | Comment | Organism |
|---|---|---|---|
| 30 | 60 | temperature-activity profiles of recombinant wild-type and mutant enzymes, overview | Bifidobacterium longum subsp. Longum |
Temperature Stability [°C]
| Temperature Stability Minimum [°C] | Temperature Stability Maximum [°C] | Comment | Organism |
|---|---|---|---|
| 55 | - |
rapid inactivation of wild-type enzyme, slower inactivation of mutants R209H, G437S, and N506S, mutants C236Y and D576V retain some activity | Bifidobacterium longum subsp. Longum |
pH Optimum
| pH Optimum Minimum | pH Optimum Maximum | Comment | Organism |
|---|---|---|---|
| 7 | - |
assay at | Bifidobacterium longum subsp. Longum |
General Information
| General Information | Comment | Organism |
|---|---|---|
| metabolism | the enzyme is important in the specific pathway for utilization of galacto-N-biose and lacto-N-biose, the latter is a major structural disaccharide in the core structures of human milk oligosaccharides | Bifidobacterium longum subsp. Longum |
| physiological function | key enzyme in the enzymatic production of lacto-N-biose I | Bifidobacterium longum subsp. Longum |
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