Application | Comment | Organism |
---|---|---|
nutrition | use in the brewing industry | Hordeum vulgare |
Cloned (Comment) | Organism |
---|---|
Sd1 and Sd2L, from developing grain, expression in Escherichia coli M15 | Hordeum vulgare |
Protein Variants | Comment | Organism |
---|---|---|
additional information | generation of different specific deletions at the C-terminal tail and complete deletion of the four C-terminal glycine-rich repeats, complete deletion enhances the thermostability, but the incomplete not, both enhance the substrate binding affinity | Hordeum vulgare |
KM Value [mM] | KM Value Maximum [mM] | Substrate | Comment | Organism | Structure |
---|---|---|---|---|---|
additional information | - |
additional information | beta-amylase from germinated barley has a higher substrate binding affinity for starch than enzyme from mature grain, removal of the four C-terminal glycine-rich repeats enhances the substrate binding affinity, kinetic parameters for several deletion mutants | Hordeum vulgare |
Organism | UniProt | Comment | Textmining |
---|---|---|---|
Hordeum vulgare | P16098 | var. Franklin: Sd1, var. Schooner: Sd2L | - |
Posttranslational Modification | Comment | Organism |
---|---|---|
proteolytic modification | beta-amylase undergoes proteolytic cleavage of the C-terminal region after germination, removal of the four C-terminal glycine-rich repeats enhances the thermostability and substrate binding affinity | Hordeum vulgare |
Purification (Comment) | Organism |
---|---|
native beta-amylase from both mature grain and germinated barley of Sd1 and Sd2L barley varieties, recombinant beta-amylase | Hordeum vulgare |
Source Tissue | Comment | Organism | Textmining |
---|---|---|---|
caryopsis | mature, of Sd1 and Sd2L barley varieties | Hordeum vulgare | - |
germ | germinated barley, of Sd1 and Sd2L barley varieties | Hordeum vulgare | - |
Substrates | Comment Substrates | Organism | Products | Comment (Products) | Rev. | Reac. |
---|---|---|---|---|---|---|
p-nitrophenylmaltopentaoside + H2O | catalyzes the release of maltose | Hordeum vulgare | ? | - |
? | |
starch + H2O | from potato, catalyzes the release of maltose from the non-reducing ends of starch, three-dimensional structure of Sd2L | Hordeum vulgare | ? | - |
? |
Synonyms | Comment | Organism |
---|---|---|
Sd1 | one of three allelic forms of Hordeum beta-amylase | Hordeum vulgare |
Sd2H | one of three allelic forms of Hordeum beta-amylase | Hordeum vulgare |
Sd2L | one of three allelic forms of Hordeum beta-amylase | Hordeum vulgare |
Temperature Optimum [°C] | Temperature Optimum Maximum [°C] | Comment | Organism |
---|---|---|---|
40 | - |
assay at | Hordeum vulgare |
Temperature Stability Minimum [°C] | Temperature Stability Maximum [°C] | Comment | Organism |
---|---|---|---|
52.6 | - |
T50, Sd2L, mature grain | Hordeum vulgare |
54.7 | - |
T50, Sd1, mature grain | Hordeum vulgare |
Turnover Number Minimum [1/s] | Turnover Number Maximum [1/s] | Substrate | Comment | Organism | Structure |
---|---|---|---|---|---|
additional information | - |
additional information | kinetic parameters for several deletion mutants | Hordeum vulgare |
pH Optimum Minimum | pH Optimum Maximum | Comment | Organism |
---|---|---|---|
5 | - |
assay at, potato starch as substrate | Hordeum vulgare |
6.2 | - |
assay at, p-nitrophenylmaltopentaoside as substrate | Hordeum vulgare |