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Literature summary extracted from

  • Andreotti, G.; Giordano, A.; Tramice, A.; Mollo, E.; Trincone, A.
    Hydrolyses and transglycosylations performed by purified alpha-D-glucosidase of the marine mollusc Aplysia fasciata (2006), J. Biotechnol., 122, 274-284.
    View publication on PubMed

General Stability

EC Number General Stability Organism
3.2.1.20 bovine serum albumin stabilizes the purified enzyme Aplysia fasciata

KM Value [mM]

EC Number KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
3.2.1.20 0.26
-
 4-nitrophenyl alpha-D-glucopyranoside pH 5.8, 34°C Aplysia fasciata
3.2.1.20 2.06
-
 4-nitrophenyl alpha-D-glucopyranosyl-1,4-alpha-D-glucopyranoside pH 5.8, 34°C Aplysia fasciata
3.2.1.20 5.7
-
 maltose pH 5.8, 34°C Aplysia fasciata

Molecular Weight [Da]

EC Number Molecular Weight [Da] Molecular Weight Maximum [Da] Comment Organism
3.2.1.20 69000
-
 4 * 69000, SDS-PAGE Aplysia fasciata
3.2.1.20 255000
-
 gel filtration Aplysia fasciata

Organism

EC Number Organism UniProt Comment Textmining
3.2.1.20 Aplysia fasciata
-
-
-

Purification (Commentary)

EC Number Purification (Comment) Organism
3.2.1.20 native enzyme 25fold by anion exchange and hydrophobic interaction chromatography, ammonium sulfate fractionation, again ion exchange chromatography, and ultrafiltration Aplysia fasciata

Specific Activity [micromol/min/mg]

EC Number Specific Activity Minimum [µmol/min/mg] Specific Activity Maximum [µmol/min/mg] Comment Organism
3.2.1.20 38.4
-
 purified enzyme Aplysia fasciata

Substrates and Products (Substrate)

EC Number Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
3.2.1.20 4-nitrophenyl alpha-D-glucopyranoside + H2O
-
 Aplysia fasciata 4-nitrophenol + alpha-D-glucose
-
 ?
3.2.1.20 4-nitrophenyl alpha-D-glucopyranosyl-1,4-alpha-D-glucopyranoside + H2O alpha-1,4-glycosidic bond Aplysia fasciata 4-nitrophenol + alpha-D-glucose
-
 ?
3.2.1.20 isomaltose + H2O very low activity Aplysia fasciata 2 alpha-D-glucose
-
 ?
3.2.1.20 maltose + H2O
-
 Aplysia fasciata alpha-D-glucose + D-glucose
-
 ?
3.2.1.20 additional information no activity in hydrolysis with starch, panose, pullulan, amylopectin, amylose, isomaltose, and saccharose, the enzyme also performs transglycosylation reactions with different donors and a variety of acceptors, product determinations, the activity with alpha-1,4-glycosidic linkages is higher compared to alpha-1,6-glycosidic likanges, substrate specificity, overview Aplysia fasciata ?
-
 ?

Subunits

EC Number Subunits Comment Organism
3.2.1.20 tetramer 4 * 69000, SDS-PAGE Aplysia fasciata

Synonyms

EC Number Synonyms Comment Organism
3.2.1.20 alpha-D-glucosidase
-
 Aplysia fasciata

Temperature Optimum [°C]

EC Number Temperature Optimum [°C] Temperature Optimum Maximum [°C] Comment Organism
3.2.1.20 36 44
-
 Aplysia fasciata

Turnover Number [1/s]

EC Number Turnover Number Minimum [1/s] Turnover Number Maximum [1/s] Substrate Comment Organism Structure
3.2.1.20 75.9
-
 4-nitrophenyl alpha-D-glucopyranosyl-1,4-alpha-D-glucopyranoside pH 5.8, 34°C Aplysia fasciata
3.2.1.20 163
-
 4-nitrophenyl alpha-D-glucopyranoside pH 5.8, 34°C Aplysia fasciata
3.2.1.20 489
-
 maltose pH 5.8, 34°C Aplysia fasciata

pH Optimum

EC Number pH Optimum Minimum pH Optimum Maximum Comment Organism
3.2.1.20 5.8
-
-
 Aplysia fasciata

pH Stability

EC Number pH Stability pH Stability Maximum Comment Organism
3.2.1.20 5.5
-
 34°C, 0.009 mg/ml bovine serum albumin, 19 h, 67% remaining activity, the half-life is about 30 h Aplysia fasciata
3.2.1.20 5.8
-
 34°C, 0.009 mg/ml bovine serum albumin, 19 h, 64% remaining activity, the half-life is about 30 h Aplysia fasciata
3.2.1.20 6.5
-
 34°C, 0.009 mg/ml bovine serum albumin, 19 h, 69% remaining activity, the half-life is about 30 h Aplysia fasciata