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Literature summary extracted from
- Genetic and biochemical characterization of an oligo-alpha-1,6-glucosidase from Lactobacillus plantarum (2017), Int. J. Food Microbiol., 246, 32-39 .
Cloned(Commentary)
| EC Number | Cloned (Comment) | Organism |
|---|---|---|
| 3.2.1.10 | gene malL, DNA and amino acid sequence determination and analysis, sequence comparisons and phylogenetic tree, recombinant expression of His-tagged enzyme | Lactiplantibacillus plantarum subsp. plantarum |
| 3.2.1.70 | overexpressed as a histidine-tagged protein in Escherichia coli BL21(DE3) cells | Lactiplantibacillus plantarum |
KM Value [mM]
| EC Number | KM Value [mM] | KM Value Maximum [mM] | Substrate | Comment | Organism | Structure |
|---|---|---|---|---|---|---|
| 3.2.1.10 | 6.22 | - |
isomaltose | pH 5.5, 30°C, recombinant His-tagged enzyme | Lactiplantibacillus plantarum subsp. plantarum |  |
| 3.2.1.10 | 244.5 | - |
isomaltulose | pH 5.5, 30°C, recombinant His-tagged enzyme | Lactiplantibacillus plantarum subsp. plantarum | |
| 3.2.1.70 | 6.22 | - |
isomaltose | at pH 5.5 and 37°C | Lactiplantibacillus plantarum | |
| 3.2.1.70 | 244.52 | - |
isomaltulose | at pH 5.5 and 37°C | Lactiplantibacillus plantarum | |
Localization
| EC Number | Localization | Comment | Organism | GeneOntology No. | Textmining |
|---|---|---|---|---|---|
| 3.2.1.10 | intracellular | no predicted signal peptide is observed, suggesting an intracellular localization for the enzyme | Lactiplantibacillus plantarum subsp. plantarum | 5622 | - |
| 3.2.1.70 | cytoplasm | - |
Lactiplantibacillus plantarum | 5737 | - |
Organism
| EC Number | Organism | UniProt | Comment | Textmining |
|---|---|---|---|---|
| 3.2.1.10 | Lactiplantibacillus plantarum subsp. plantarum | D7VFY4 | - |
- |
| 3.2.1.10 | Lactiplantibacillus plantarum subsp. plantarum ATCC 149917 | D7VFY4 | - |
- |
| 3.2.1.10 | Lactiplantibacillus plantarum subsp. plantarum LL441 | D7VFY4 | - |
- |
| 3.2.1.70 | Lactiplantibacillus plantarum | - |
- |
- |
| 3.2.1.70 | Lactiplantibacillus plantarum LL441 | - |
- |
- |
Purification (Commentary)
| EC Number | Purification (Comment) | Organism |
|---|---|---|
| 3.2.1.10 | recombinant His-tagged enzyme by nickel affinity chromatography to homogeneity | Lactiplantibacillus plantarum subsp. plantarum |
| 3.2.1.70 | Ni-NTA column chromatography | Lactiplantibacillus plantarum |
Specific Activity [micromol/min/mg]
| EC Number | Specific Activity Minimum [µmol/min/mg] | Specific Activity Maximum [µmol/min/mg] | Comment | Organism |
|---|---|---|---|---|
| 3.2.1.10 | additional information | - |
Vmax is 0.4789 mM/mg/min | Lactiplantibacillus plantarum subsp. plantarum |
Substrates and Products (Substrate)
| EC Number | Substrates | Comment Substrates | Organism | Products | Comment (Products) | Rev. | Reac. |
|---|---|---|---|---|---|---|---|
| 3.2.1.10 | 4-nitrophenyl-alpha-D-glucopyranoside + H2O | - |
Lactiplantibacillus plantarum subsp. plantarum | 4-nitrophenol + D-glucose | - |
? | |
| 3.2.1.10 | 4-nitrophenyl-alpha-D-glucopyranoside + H2O | - |
Lactiplantibacillus plantarum subsp. plantarum ATCC 149917 | 4-nitrophenol + D-glucose | - |
? | |
| 3.2.1.10 | 4-nitrophenyl-alpha-D-glucopyranoside + H2O | - |
Lactiplantibacillus plantarum subsp. plantarum LL441 | 4-nitrophenol + D-glucose | - |
? | |
| 3.2.1.10 | isomaltose + H2O | the hydrolysing percentages are 54.06% | Lactiplantibacillus plantarum subsp. plantarum | 2 D-glucose | - |
? | |
| 3.2.1.10 | isomaltose + H2O | the hydrolysing percentages are 54.06% | Lactiplantibacillus plantarum subsp. plantarum ATCC 149917 | 2 D-glucose | - |
? | |
| 3.2.1.10 | isomaltose + H2O | the hydrolysing percentages are 54.06% | Lactiplantibacillus plantarum subsp. plantarum LL441 | 2 D-glucose | - |
? | |
| 3.2.1.10 | isomaltulose + H2O | the hydrolysing percentages are 37.7% | Lactiplantibacillus plantarum subsp. plantarum | D-glucose + D-fructose | - |
? | |
| 3.2.1.10 | isomaltulose + H2O | the hydrolysing percentages are 37.7% | Lactiplantibacillus plantarum subsp. plantarum ATCC 149917 | D-glucose + D-fructose | - |
? | |
| 3.2.1.10 | isomaltulose + H2O | the hydrolysing percentages are 37.7% | Lactiplantibacillus plantarum subsp. plantarum LL441 | D-glucose + D-fructose | - |
? | |
| 3.2.1.10 | additional information | the enzyme degrades isomaltose and isomaltulose, but not isomaltrotriose, melibiose, panose and raffinose. The enzyme shows no activity with trehalose, sucrose, turanose or maltose, i.e. sugars with glycosidic bonds other than 1->6, nor with 4-nitrophenyl-beta-D-glucopyranoside. Isomaltose and isomaltulose are the preferred substrates. Under the conditions of the assay, no transglycosylation activity of recombinant His-tagged enzyme MalL is observed with respect to the disaccharides sucrose, maltose, gentibiose, panose and isomaltulose | Lactiplantibacillus plantarum subsp. plantarum | ? | - |
? | |
| 3.2.1.10 | additional information | the enzyme degrades isomaltose and isomaltulose, but not isomaltrotriose, melibiose, panose and raffinose. The enzyme shows no activity with trehalose, sucrose, turanose or maltose, i.e. sugars with glycosidic bonds other than 1->6, nor with 4-nitrophenyl-beta-D-glucopyranoside. Isomaltose and isomaltulose are the preferred substrates. Under the conditions of the assay, no transglycosylation activity of recombinant His-tagged enzyme MalL is observed with respect to the disaccharides sucrose, maltose, gentibiose, panose and isomaltulose | Lactiplantibacillus plantarum subsp. plantarum ATCC 149917 | ? | - |
? | |
| 3.2.1.10 | additional information | the enzyme degrades isomaltose and isomaltulose, but not isomaltrotriose, melibiose, panose and raffinose. The enzyme shows no activity with trehalose, sucrose, turanose or maltose, i.e. sugars with glycosidic bonds other than 1->6, nor with 4-nitrophenyl-beta-D-glucopyranoside. Isomaltose and isomaltulose are the preferred substrates. Under the conditions of the assay, no transglycosylation activity of recombinant His-tagged enzyme MalL is observed with respect to the disaccharides sucrose, maltose, gentibiose, panose and isomaltulose | Lactiplantibacillus plantarum subsp. plantarum LL441 | ? | - |
? | |
| 3.2.1.70 | 4-nitrophenyl alpha-D-glucopyranoside + H2O | strong hydrolytic activity | Lactiplantibacillus plantarum | 4-nitrophenol + D-glucopyranose | - |
? | |
| 3.2.1.70 | 4-nitrophenyl alpha-D-glucopyranoside + H2O | strong hydrolytic activity | Lactiplantibacillus plantarum LL441 | 4-nitrophenol + D-glucopyranose | - |
? | |
| 3.2.1.70 | isomaltose + H2O | 54.06% hydrolysis | Lactiplantibacillus plantarum | 2 D-glucose | - |
? | |
| 3.2.1.70 | isomaltose + H2O | 54.06% hydrolysis | Lactiplantibacillus plantarum LL441 | 2 D-glucose | - |
? | |
| 3.2.1.70 | isomaltulose + H2O | 37.3% hydrolysis | Lactiplantibacillus plantarum | D-glucose | - |
? | |
| 3.2.1.70 | isomaltulose + H2O | 37.3% hydrolysis | Lactiplantibacillus plantarum LL441 | D-glucose | - |
? | |
| 3.2.1.70 | additional information | the enzyme has no activity with 4-nitrophenyl beta-D-glucopyranoside, 4-nitrophenyl alpha-D-galactopyranoside, 4-nitrophenyl beta-D-galactopyranoside, 4-nitrophenyl alpha-D-manopyranoside, 4-nitrophenyl beta-D-fucopyranoside, 4-nitrophenyl alpha-D-fucopyranoside, 4-nitrophenyl beta-D-arabinopyranoside, 4-nitrophenyl alpha-D-arabinopyranoside, 4-nitrophenyl alpha-D-maltohexaoside, isomaltrotriose, melibiose, panose and raffinose, trehalose, sucrose, turanose or maltose. The enzyme shows no transglycosylation activity | Lactiplantibacillus plantarum | ? | - |
? | |
| 3.2.1.70 | additional information | the enzyme has no activity with 4-nitrophenyl beta-D-glucopyranoside, 4-nitrophenyl alpha-D-galactopyranoside, 4-nitrophenyl beta-D-galactopyranoside, 4-nitrophenyl alpha-D-manopyranoside, 4-nitrophenyl beta-D-fucopyranoside, 4-nitrophenyl alpha-D-fucopyranoside, 4-nitrophenyl beta-D-arabinopyranoside, 4-nitrophenyl alpha-D-arabinopyranoside, 4-nitrophenyl alpha-D-maltohexaoside, isomaltrotriose, melibiose, panose and raffinose, trehalose, sucrose, turanose or maltose. The enzyme shows no transglycosylation activity | Lactiplantibacillus plantarum LL441 | ? | - |
? | |
Subunits
| EC Number | Subunits | Comment | Organism |
|---|---|---|---|
| 3.2.1.10 | ? | x * 66310, sequence calculation, x * 68000, recombinant His-tagged enzyme, SDS-PAGE | Lactiplantibacillus plantarum subsp. plantarum |
| 3.2.1.10 | More | tertiary structure prediction of MalL from Lactobacillus plantarum LL441 | Lactiplantibacillus plantarum subsp. plantarum |
| 3.2.1.70 | ? | x * 68000, SDS-PAGE | Lactiplantibacillus plantarum |
| 3.2.1.70 | ? | x * 66310, calculated from amino acid sequence | Lactiplantibacillus plantarum |
Synonyms
| EC Number | Synonyms | Comment | Organism |
|---|---|---|---|
| 3.2.1.10 | HMPREF0531_13057 | locus name | Lactiplantibacillus plantarum subsp. plantarum |
| 3.2.1.10 | MalL | - |
Lactiplantibacillus plantarum subsp. plantarum |
| 3.2.1.10 | oligo-alpha-1,6-glucosidase | - |
Lactiplantibacillus plantarum subsp. plantarum |
| 3.2.1.70 | MalL | - |
Lactiplantibacillus plantarum |
| 3.2.1.70 | oligo-alpha-1,6-glucosidase | - |
Lactiplantibacillus plantarum |
Temperature Optimum [°C]
| EC Number | Temperature Optimum [°C] | Temperature Optimum Maximum [°C] | Comment | Organism |
|---|---|---|---|---|
| 3.2.1.10 | 30 | - |
recombinant His-tagged enzyme | Lactiplantibacillus plantarum subsp. plantarum |
| 3.2.1.70 | 30 | - |
- |
Lactiplantibacillus plantarum |
Temperature Range [°C]
| EC Number | Temperature Minimum [°C] | Temperature Maximum [°C] | Comment | Organism |
|---|---|---|---|---|
| 3.2.1.10 | 20 | 40 | activity range, recombinant enzyme, activity declines sharply above 40°C | Lactiplantibacillus plantarum subsp. plantarum |
| 3.2.1.70 | 20 | 40 | the activity of the enzyme declines sharply before 20°C and after 40°C | Lactiplantibacillus plantarum |
pH Optimum
| EC Number | pH Optimum Minimum | pH Optimum Maximum | Comment | Organism |
|---|---|---|---|---|
| 3.2.1.10 | 5 | 6 | recombinant His-tagged enzyme | Lactiplantibacillus plantarum subsp. plantarum |
| 3.2.1.70 | 5 | 6 | the enzyme shows high specific activity between pH 5.0 and 6.0, with no clear maximum | Lactiplantibacillus plantarum |
General Information
| EC Number | General Information | Comment | Organism |
|---|---|---|---|
| 3.2.1.10 | evolution | the enzyme is a member of the alpha-amylase (AmyAC) superfamily of the glycosyl hydrolases (GH) family 13 (GH13), subfamily 31 (GH13_31) | Lactiplantibacillus plantarum subsp. plantarum |
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Release 2023.1 (January 2023)
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