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Literature summary extracted from

  • Ma, Y.F.; Eglinton, J.K.; Evans, D.E.; Logue, S.J.; Langridge, P.
    Removal of the four C-terminal glycine-rich repeats enhances the thermostability and substrate binding affinity of barley beta-amylase (2000), Biochemistry, 39, 13350-13355.
    View publication on PubMed

Application

EC Number Application Comment Organism
3.2.1.2 nutrition use in the brewing industry Hordeum vulgare

Cloned(Commentary)

EC Number Cloned (Comment) Organism
3.2.1.2 Sd1 and Sd2L, from developing grain, expression in Escherichia coli M15 Hordeum vulgare

Protein Variants

EC Number Protein Variants Comment Organism
3.2.1.2 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]

EC Number KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
3.2.1.2 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

EC Number Organism UniProt Comment Textmining
3.2.1.2 Hordeum vulgare P16098 var. Franklin: Sd1, var. Schooner: Sd2L
-

Posttranslational Modification

EC Number Posttranslational Modification Comment Organism
3.2.1.2 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 (Commentary)

EC Number Purification (Comment) Organism
3.2.1.2 native beta-amylase from both mature grain and germinated barley of Sd1 and Sd2L barley varieties, recombinant beta-amylase Hordeum vulgare

Source Tissue

EC Number Source Tissue Comment Organism Textmining
3.2.1.2 caryopsis mature, of Sd1 and Sd2L barley varieties Hordeum vulgare
-
3.2.1.2 germ germinated barley, of Sd1 and Sd2L barley varieties Hordeum vulgare
-

Substrates and Products (Substrate)

EC Number Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
3.2.1.2 p-nitrophenylmaltopentaoside + H2O catalyzes the release of maltose Hordeum vulgare ?
-
 ?
3.2.1.2 starch + H2O from potato, catalyzes the release of maltose from the non-reducing ends of starch, three-dimensional structure of Sd2L Hordeum vulgare ?
-
 ?

Synonyms

EC Number Synonyms Comment Organism
3.2.1.2 Sd1 one of three allelic forms of Hordeum beta-amylase Hordeum vulgare
3.2.1.2 Sd2H one of three allelic forms of Hordeum beta-amylase Hordeum vulgare
3.2.1.2 Sd2L one of three allelic forms of Hordeum beta-amylase Hordeum vulgare

Temperature Optimum [°C]

EC Number Temperature Optimum [°C] Temperature Optimum Maximum [°C] Comment Organism
3.2.1.2 40
-
 assay at Hordeum vulgare

Temperature Stability [°C]

EC Number Temperature Stability Minimum [°C] Temperature Stability Maximum [°C] Comment Organism
3.2.1.2 52.6
-
 T50, Sd2L, mature grain Hordeum vulgare
3.2.1.2 54.7
-
 T50, Sd1, mature grain Hordeum vulgare

Turnover Number [1/s]

EC Number Turnover Number Minimum [1/s] Turnover Number Maximum [1/s] Substrate Comment Organism Structure
3.2.1.2 additional information
-
 additional information kinetic parameters for several deletion mutants Hordeum vulgare

pH Optimum

EC Number pH Optimum Minimum pH Optimum Maximum Comment Organism
3.2.1.2 5
-
 assay at, potato starch as substrate Hordeum vulgare
3.2.1.2 6.2
-
 assay at, p-nitrophenylmaltopentaoside as substrate Hordeum vulgare