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Literature summary extracted from

  • Van Damme, E.J.M.; Hu, J.; Barre, A.; Hause, B.; Baggerman, G.; Rouge, P.; Peumans, W.J.
    Purification, characterization, immunolocalization and structural analysis of the abundant cytoplasmic beta-amylase from Calystegia sepium (hedge bindweed) rhizomes (2001), Eur. J. Biochem., 268, 6263-6273.
    View publication on PubMed

Cloned(Commentary)

EC Number Cloned (Comment) Organism
3.2.1.2
-
 Calystegia sepium

Inhibitors

EC Number Inhibitors Comment Organism Structure
3.2.1.2 cyclohexaamylose iodine staining method, competitive inhibition Calystegia sepium
3.2.1.2 D-glucose p-nitrophenylmaltopentaoside hydrolysis: 125 mM, 87.5% inhibition, iodine staining method: mixed-type, weak inhibition compared with maltose and cyclohexaamylose Calystegia sepium
3.2.1.2 D-maltose
-
 Calystegia sepium
3.2.1.2 D-mannose 125 mM, 6% inhibition, p-nitrophenylmaltopentaoside hydrolysis Calystegia sepium
3.2.1.2 maltose p-nitrophenylmaltopentaoside hydrolysis: 125 mM, 87.5% inhibition, iodine staining method: competitive inhibition Calystegia sepium
3.2.1.2 additional information not inhibited by 250 mM lactose Calystegia sepium

Localization

EC Number Localization Comment Organism GeneOntology No. Textmining
3.2.1.2 cytoplasm exclusively located in Calystegia sepium 5737
-

Molecular Weight [Da]

EC Number Molecular Weight [Da] Molecular Weight Maximum [Da] Comment Organism
3.2.1.2 55000
-
 4 * 55000, SDS-PAGE, 4 * 56068, mass spectrometry, 4 * 56204, sequence calculation inclusive the N-terminal methionine Calystegia sepium
3.2.1.2 56068
-
 4 * 55000, SDS-PAGE, 4 * 56068, mass spectrometry, 4 * 56204, sequence calculation inclusive the N-terminal methionine Calystegia sepium
3.2.1.2 56204
-
 4 * 55000, SDS-PAGE, 4 * 56068, mass spectrometry, 4 * 56204, sequence calculation inclusive the N-terminal methionine Calystegia sepium
3.2.1.2 200000
-
 gel filtration Calystegia sepium

Natural Substrates/ Products (Substrates)

EC Number Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
3.2.1.2 additional information Calystegia sepium rhizome beta-amylase is a cytoplasmic vegetative storage protein ?
-
 ?

Organism

EC Number Organism UniProt Comment Textmining
3.2.1.2 Calystegia sepium Q9FQ07 hedge bindweed, collected in Leuven in winter
-

Posttranslational Modification

EC Number Posttranslational Modification Comment Organism
3.2.1.2 additional information apart from the removal of the N-terminal methionine no co- or posttranslational processing Calystegia sepium
3.2.1.2 no glycoprotein
-
 Calystegia sepium

Purification (Commentary)

EC Number Purification (Comment) Organism
3.2.1.2
-
 Calystegia sepium

Source Tissue

EC Number Source Tissue Comment Organism Textmining
3.2.1.2 rhizome resting, localized in the cortex and the pith of rhizomes, but not in vascular tissues, pericycle, endodermis and rhizodermis Calystegia sepium
-

Substrates and Products (Substrate)

EC Number Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
3.2.1.2 amylopectin + H2O catalyzes the release of maltose residues, amylopectin and starch are better substrates than amylose Calystegia sepium maltose + ?
-
 ?
3.2.1.2 amylose + H2O catalyzes the release of maltose residues, less good substrate than starch and amylopectin Calystegia sepium maltose + ?
-
 ?
3.2.1.2 additional information rhizome beta-amylase is a cytoplasmic vegetative storage protein Calystegia sepium ?
-
 ?
3.2.1.2 additional information beta-amylase exclusively catalyzes the release of beta-maltose from the non-reducing ends of alpha-1,4-linked oligo- and polyglucans, three-dimensional structure Calystegia sepium ?
-
 ?
3.2.1.2 p-nitrophenylmaltopentaoside + H2O catalyzes the release of p-nitrophenol, specific substrate Calystegia sepium p-nitrophenol + maltopentaose
-
 ?
3.2.1.2 starch + H2O catalyzes the release of maltose residues, starch and amylopectin are better substrates than amylose Calystegia sepium maltose + ?
-
 ?

Subunits

EC Number Subunits Comment Organism
3.2.1.2 homotetramer 4 * 55000, SDS-PAGE, 4 * 56068, mass spectrometry, 4 * 56204, sequence calculation inclusive the N-terminal methionine Calystegia sepium

Temperature Optimum [°C]

EC Number Temperature Optimum [°C] Temperature Optimum Maximum [°C] Comment Organism
3.2.1.2 20
-
 assay at, starch, amylose or amylopectin as substrate Calystegia sepium
3.2.1.2 40
-
 assay at, p-nitrophenylmaltopentaoside as substrate Calystegia sepium

Temperature Stability [°C]

EC Number Temperature Stability Minimum [°C] Temperature Stability Maximum [°C] Comment Organism
3.2.1.2 60
-
 stable up to Calystegia sepium
3.2.1.2 70
-
 10 min, complete inactivation Calystegia sepium

pH Optimum

EC Number pH Optimum Minimum pH Optimum Maximum Comment Organism
3.2.1.2 4.8
-
-
 Calystegia sepium

pH Range

EC Number pH Minimum pH Maximum Comment Organism
3.2.1.2 3 7 active in the range Calystegia sepium

pH Stability

EC Number pH Stability pH Stability Maximum Comment Organism
3.2.1.2 3 11 stable in the range Calystegia sepium
3.2.1.2 3 12 irreversible inactivation below pH 3 and above pH 12 Calystegia sepium

Ki Value [mM]

EC Number Ki Value [mM] Ki Value maximum [mM] Inhibitor Comment Organism Structure
3.2.1.2 0.36
-
 cyclohexaamylose pH 5, 20°C, iodine staining method Calystegia sepium
3.2.1.2 11.7
-
 D-maltose pH 5, 20°C, iodine staining method Calystegia sepium
3.2.1.2 262
-
 D-glucose pH 5, 20°C, iodine staining method Calystegia sepium

pI Value

EC Number Organism Comment pI Value Maximum pI Value
3.2.1.2 Calystegia sepium isoelectric focusing
-
 4.9