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Literature summary for 3.2.1.2 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

Application Comment Organism
nutrition use in the brewing industry Hordeum vulgare

Cloned(Commentary)

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

Protein Variants

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 [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

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

Posttranslational Modification

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 (Commentary)

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

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 and Products (Substrate)

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

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

Temperature Stability [°C]

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 [1/s]

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

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