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Literature summary extracted from

  • Hamada, S.; Ito, H.; Ueno, H.; Takeda, Y.; Matsui, H.
    The N-terminal region of the starch-branching enzyme from Phaseolus vulgaris L. is essential for optimal catalysis and structural stability (2007), Phytochemistry, 68, 1367-1375.
    View publication on PubMed

Activating Compound

EC Number Activating Compound Comment Organism Structure
2.4.1.18 citrate in the presence of 0.1 M citrate, the activity of the active enzyme increases Phaseolus vulgaris

Cloned(Commentary)

EC Number Cloned (Comment) Organism
2.4.1.18 expressed in Escherichia coli BL21 (DE3) Phaseolus vulgaris

Protein Variants

EC Number Protein Variants Comment Organism
2.4.1.18 D15A D15A-PvSBE2 enzyme shows 13.1% of the specific activity of the wild type enzyme. The large decrease in the specific activities of the mutant is predominatly attributed to the reduced Vmax value. Phaseolus vulgaris
2.4.1.18 D15E D15E-PvSBE2 enzyme shows 31.3% of the specific activity of the wild type enzyme. The large decrease in the specific activities of the mutant is predominatly attributed to the reduced Vmax value. Phaseolus vulgaris
2.4.1.18 H24A H24A-PvSBE2 enzyme shows 38.3% of the specific activity of the wild type enzyme. The large decrease in the specific activities of the mutant is predominatly attributed to the reduced Vmax value. Phaseolus vulgaris
2.4.1.18 additional information chimeric enzymes of PvSBE2: only one chimeric recombinant protein ((I Na/2Nb)-II) has enzyme activity. It shows 6.1% of the specific activity of the wild type enzyme. Phaseolus vulgaris
2.4.1.18 additional information N-termial truncated enzyme of PvSBE2. Delta46-PvSBE2 has no branching enzyme activity. Phaseolus vulgaris
2.4.1.18 R28A R28A-PvSBE2 enzyme shows 10.7% of the specific activity of the wild type enzyme. The large decrease in the specific activities of the mutant is predominatly attributed to the reduced Vmax value. Phaseolus vulgaris
2.4.1.18 R28K R28K-PvSBE2 enzyme shows 93.5% of the specific activity of the wild type enzyme. Phaseolus vulgaris

KM Value [mM]

EC Number KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
2.4.1.18 additional information
-
 additional information Km value of the chimeric enzyme (1Na/2Nb)-II is 0.63 mg/ml. The Km value of D15A-PvSBE2 is 1.3 mg/ml, 1.52 mg/ml for D15E-PvSBE2, 1.57 mg/ml for R28A-PvSBE2, 1.55 mg/ml for R28K-PvSBE2 and 1.59 mg/ml for H24A-PvSBE2. Phaseolus vulgaris

Organism

EC Number Organism UniProt Comment Textmining
2.4.1.18 Phaseolus vulgaris
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-
-

Purification (Commentary)

EC Number Purification (Comment) Organism
2.4.1.18 chimeric and N-terminal truncated enzymes: DEAE-Sepharose Cl6B column, Bio-Gel P-200 and Gigapite column all at 4°C and pH 7.5. Site-directed mutant enzymes: chelating Sepharose FF column and DEAE-Sepharose CL-6B column, all at 4°C. Phaseolus vulgaris

Specific Activity [micromol/min/mg]

EC Number Specific Activity Minimum [µmol/min/mg] Specific Activity Maximum [µmol/min/mg] Comment Organism
2.4.1.18 additional information
-
 the chimeric (1Na/2Nb)II enzyme has a specific activity of 13 U/mg in the presence of 0.1 M citrate or 6.1 U/mg in the absence of citrate. The iodine-staining assay is performed by monitoring the decrease in absorbance at 660 nm for amylose, one unit of enzyme activity is defined as the amount of enzyme yielding a decrease in A660 of 0.1 per minute at 30°C. Phaseolus vulgaris

Synonyms

EC Number Synonyms Comment Organism
2.4.1.18 SBE starch-branching enzyme Phaseolus vulgaris

Temperature Stability [°C]

EC Number Temperature Stability Minimum [°C] Temperature Stability Maximum [°C] Comment Organism
2.4.1.18 additional information
-
 when the enzymes are maintained for 15 min at various temperatures ranging from 30°C to 60°C, more than 80% of the original activity was retained up to 47.5°C for PvSBE2, up to 40°C for D15A- and D15E-PvSBE2, up to 42.5°C for R28A- and H24A-PvSBE2, and up to 45°C for R28K-PvSBE2. Phaseolus vulgaris