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Literature summary for 3.2.1.10 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)
| Cloned (Comment) | Organism |
|---|---|
| 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 |
KM Value [mM]
| KM Value [mM] | KM Value Maximum [mM] | Substrate | Comment | Organism | Structure |
|---|---|---|---|---|---|
| 6.22 | - |
isomaltose | pH 5.5, 30°C, recombinant His-tagged enzyme | Lactiplantibacillus plantarum subsp. plantarum |  |
| 244.5 | - |
isomaltulose | pH 5.5, 30°C, recombinant His-tagged enzyme | Lactiplantibacillus plantarum subsp. plantarum | |
Localization
| Localization | Comment | Organism | GeneOntology No. | Textmining |
|---|---|---|---|---|
| intracellular | no predicted signal peptide is observed, suggesting an intracellular localization for the enzyme | Lactiplantibacillus plantarum subsp. plantarum | 5622 | - |
Organism
| Organism | UniProt | Comment | Textmining |
|---|---|---|---|
| Lactiplantibacillus plantarum subsp. plantarum | D7VFY4 | - |
- |
| Lactiplantibacillus plantarum subsp. plantarum ATCC 149917 | D7VFY4 | - |
- |
| Lactiplantibacillus plantarum subsp. plantarum LL441 | D7VFY4 | - |
- |
Purification (Commentary)
| Purification (Comment) | Organism |
|---|---|
| recombinant His-tagged enzyme by nickel affinity chromatography to homogeneity | Lactiplantibacillus plantarum subsp. plantarum |
Specific Activity [micromol/min/mg]
| Specific Activity Minimum [µmol/min/mg] | Specific Activity Maximum [µmol/min/mg] | Comment | Organism |
|---|---|---|---|
| additional information | - |
Vmax is 0.4789 mM/mg/min | Lactiplantibacillus plantarum subsp. plantarum |
Substrates and Products (Substrate)
| Substrates | Comment Substrates | Organism | Products | Comment (Products) | Rev. | Reac. |
|---|---|---|---|---|---|---|
| 4-nitrophenyl-alpha-D-glucopyranoside + H2O | - |
Lactiplantibacillus plantarum subsp. plantarum | 4-nitrophenol + D-glucose | - |
? | |
| 4-nitrophenyl-alpha-D-glucopyranoside + H2O | - |
Lactiplantibacillus plantarum subsp. plantarum ATCC 149917 | 4-nitrophenol + D-glucose | - |
? | |
| 4-nitrophenyl-alpha-D-glucopyranoside + H2O | - |
Lactiplantibacillus plantarum subsp. plantarum LL441 | 4-nitrophenol + D-glucose | - |
? | |
| isomaltose + H2O | the hydrolysing percentages are 54.06% | Lactiplantibacillus plantarum subsp. plantarum | 2 D-glucose | - |
? | |
| isomaltose + H2O | the hydrolysing percentages are 54.06% | Lactiplantibacillus plantarum subsp. plantarum ATCC 149917 | 2 D-glucose | - |
? | |
| isomaltose + H2O | the hydrolysing percentages are 54.06% | Lactiplantibacillus plantarum subsp. plantarum LL441 | 2 D-glucose | - |
? | |
| isomaltulose + H2O | the hydrolysing percentages are 37.7% | Lactiplantibacillus plantarum subsp. plantarum | D-glucose + D-fructose | - |
? | |
| isomaltulose + H2O | the hydrolysing percentages are 37.7% | Lactiplantibacillus plantarum subsp. plantarum ATCC 149917 | D-glucose + D-fructose | - |
? | |
| isomaltulose + H2O | the hydrolysing percentages are 37.7% | Lactiplantibacillus plantarum subsp. plantarum LL441 | D-glucose + D-fructose | - |
? | |
| 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 | ? | - |
? | |
| 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 | ? | - |
? | |
| 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 | ? | - |
? | |
Subunits
| Subunits | Comment | Organism |
|---|---|---|
| ? | x * 66310, sequence calculation, x * 68000, recombinant His-tagged enzyme, SDS-PAGE | Lactiplantibacillus plantarum subsp. plantarum |
| More | tertiary structure prediction of MalL from Lactobacillus plantarum LL441 | Lactiplantibacillus plantarum subsp. plantarum |
Synonyms
| Synonyms | Comment | Organism |
|---|---|---|
| HMPREF0531_13057 | locus name | Lactiplantibacillus plantarum subsp. plantarum |
| MalL | - |
Lactiplantibacillus plantarum subsp. plantarum |
| oligo-alpha-1,6-glucosidase | - |
Lactiplantibacillus plantarum subsp. plantarum |
Temperature Optimum [°C]
| Temperature Optimum [°C] | Temperature Optimum Maximum [°C] | Comment | Organism |
|---|---|---|---|
| 30 | - |
recombinant His-tagged enzyme | Lactiplantibacillus plantarum subsp. plantarum |
Temperature Range [°C]
| Temperature Minimum [°C] | Temperature Maximum [°C] | Comment | Organism |
|---|---|---|---|
| 20 | 40 | activity range, recombinant enzyme, activity declines sharply above 40°C | Lactiplantibacillus plantarum subsp. plantarum |
pH Optimum
| pH Optimum Minimum | pH Optimum Maximum | Comment | Organism |
|---|---|---|---|
| 5 | 6 | recombinant His-tagged enzyme | Lactiplantibacillus plantarum subsp. plantarum |
General Information
| General Information | Comment | Organism |
|---|---|---|
| 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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